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acetyl-CoA + H2O + oxaloacetate
citrate + CoA
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
acetyl-CoA + oxaloacetate + H2O
citrate + CoA + H+
oxaloacetate + acetyl-CoA + H2O
citrate + CoA
-
-
-
?
propanoyl-CoA + H2O + oxaloacetate
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
bifunctional enzyme with 2.3-fold higher activity as a 2-methylcitrate synthase
-
-
?
propionyl-CoA + H2O + oxaloacetate
(2S,3S)-2-methylcitrate + CoA
propionyl-CoA + oxaloacetate + H2O
2-methylcitrate + CoA
additional information
?
-
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase. The enzyme is involved in the methylcitric acid cycle
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
bifunctional enzyme with 2.3-fold higher activity as a 2-methylcitrate synthase
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase. The enzyme is involved in the methylcitric acid cycle
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
the activity with propanoyl-CoA is not tested
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
the activity with propanoyl-CoA is not tested
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
ir
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
the enzyme is required for fatty acid respiration and seed germination, the enzyme is not only a key enzyme of the glyoxylate cycle but also catalyzes an essential step in the respiration of fatty acids
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
contributes little to flux control in the pathway
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
contributes little to flux control in the pathway
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
high activity necessary for N2 fixation
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
key enzyme of glyoxylate cycle in fat-storing seedlings
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
involved in poly 3-hydroxybutyrate synthesis
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
key enzyme of tricarboxylic acid cycle
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
key enzyme of tricarboxylic acid cycle
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
involved in poly 3-hydroxybutyrate synthesis
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
the activity with propanoyl-CoA is not tested
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
the activity with propanoyl-CoA is not tested
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
no channeling of oxaloacetate between malate dehydrogenase and citrate synthase in a recombinant fusion protein using a coupled assay
-
ir
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
regulation of mitochondrial uptake and efflux by citrate synthase activity
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
regulation
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
condensation step is reversible
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
also acting as structural protein in oral morphogenesis and conjugation
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
also acting as structural protein in oral morphogenesis and conjugation
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
condensation step nearly irreversible, reversibility is increased at 70°C
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA + H+
-
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA + H+
-
-
-
-
?
propionyl-CoA + H2O + oxaloacetate
(2S,3S)-2-methylcitrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase. The enzyme is involved in the methylcitric acid cycle
-
-
?
propionyl-CoA + H2O + oxaloacetate
(2S,3S)-2-methylcitrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase
-
-
?
propionyl-CoA + oxaloacetate + H2O
2-methylcitrate + CoA
-
-
-
-
?
propionyl-CoA + oxaloacetate + H2O
2-methylcitrate + CoA
-
-
-
-
?
propionyl-CoA + oxaloacetate + H2O
2-methylcitrate + CoA
methylcitrase synthase, also exhibiting citrate synthase activity
-
?
propionyl-CoA + oxaloacetate + H2O
2-methylcitrate + CoA
-
only the dimeric enzyme form, no activity with the hexameric enzyme form
-
?
additional information
?
-
-
differences in acid accumulation between acidless and acid-containing fruits may not be attributed to changes in the ativity of citrate synthase
-
-
?
additional information
?
-
-
differences in acid accumulation between acidless and acid-containing fruits may not be attributed to changes in the ativity of citrate synthase
-
-
?
additional information
?
-
-
differences in acid accumulation between acidless and acid-containing fruits may not be attributed to changes in the ativity of citrate synthase
-
-
?
additional information
?
-
-
mechanism for domain closure. It appears that there is a common barrier between the open- and closed-domain conformations that cannot be overcome in either exploring or targeting simulations. For citrate synthase in the open conformation there are 258 atoms from both domains that are in the domain-contact sets. This increases to only 284 for the closed structure. These atoms come from 61 residues in the open which increases to 66 in the closed. Of these, 57 are common to both open and closed conformations
-
-
?
additional information
?
-
the enzyme does not have any methylcitrate synthase activity
-
-
?
additional information
?
-
the activity with propanoyl-CoA is not tested
-
-
?
additional information
?
-
the activity with propanoyl-CoA is not tested
-
-
?
additional information
?
-
-
cells with cit1 deletion show higher tendency toward glutathione depletion and subsequent accumulation of reactive oxygen species than the wild type. GSH deficiency in cit1 null cells is caused by an insufficient supply of glutamate necessary for biosynthesis of GSH rather than the depletion of reducing power required for reduction of GSSG to GSH
-
-
?
additional information
?
-
-
yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase or aconitase share several growth phenotypes as well as patterns of specific protein expression that differ from the parental strain. These shared properties of idhD and aco1D strains are eliminated or moderated by codisruption of the CIT1 gene encoding mitochondrial citrate synthase
-
-
?
additional information
?
-
no activity with propionyl-CoA
-
-
?
additional information
?
-
-
yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase or aconitase share several growth phenotypes as well as patterns of specific protein expression that differ from the parental strain. These shared properties of idhD and aco1D strains are eliminated or moderated by codisruption of the CIT1 gene encoding mitochondrial citrate synthase
-
-
?
additional information
?
-
-
citrate synthase is essential for nodule maintenance in infection of alfalfa
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
propanoyl-CoA + H2O + oxaloacetate
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
bifunctional enzyme with 2.3-fold higher activity as a 2-methylcitrate synthase
-
-
?
propionyl-CoA + H2O + oxaloacetate
(2S,3S)-2-methylcitrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase. The enzyme is involved in the methylcitric acid cycle
-
-
?
additional information
?
-
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase. The enzyme is involved in the methylcitric acid cycle
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
bifunctional enzyme with 2.3-fold higher activity as a 2-methylcitrate synthase
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
MmgD is a bifunctional citrate synthase/2-methylcitrate synthase with 2.3fold higher activity as a 2-methylcitrate synthase. The enzyme is involved in the methylcitric acid cycle
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
-
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
the enzyme is required for fatty acid respiration and seed germination, the enzyme is not only a key enzyme of the glyoxylate cycle but also catalyzes an essential step in the respiration of fatty acids
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
contributes little to flux control in the pathway
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
contributes little to flux control in the pathway
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
high activity necessary for N2 fixation
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
key enzyme of glyoxylate cycle in fat-storing seedlings
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
involved in poly 3-hydroxybutyrate synthesis
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
key enzyme of tricarboxylic acid cycle
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
key enzyme of tricarboxylic acid cycle
-
-
r
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
only anabolic pathway
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
involved in poly 3-hydroxybutyrate synthesis
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
regulation of mitochondrial uptake and efflux by citrate synthase activity
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
regulation
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
also acting as structural protein in oral morphogenesis and conjugation
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
also acting as structural protein in oral morphogenesis and conjugation
-
-
?
additional information
?
-
-
differences in acid accumulation between acidless and acid-containing fruits may not be attributed to changes in the ativity of citrate synthase
-
-
?
additional information
?
-
-
differences in acid accumulation between acidless and acid-containing fruits may not be attributed to changes in the ativity of citrate synthase
-
-
?
additional information
?
-
-
differences in acid accumulation between acidless and acid-containing fruits may not be attributed to changes in the ativity of citrate synthase
-
-
?
additional information
?
-
-
cells with cit1 deletion show higher tendency toward glutathione depletion and subsequent accumulation of reactive oxygen species than the wild type. GSH deficiency in cit1 null cells is caused by an insufficient supply of glutamate necessary for biosynthesis of GSH rather than the depletion of reducing power required for reduction of GSSG to GSH
-
-
?
additional information
?
-
-
yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase or aconitase share several growth phenotypes as well as patterns of specific protein expression that differ from the parental strain. These shared properties of idhD and aco1D strains are eliminated or moderated by codisruption of the CIT1 gene encoding mitochondrial citrate synthase
-
-
?
additional information
?
-
-
yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase or aconitase share several growth phenotypes as well as patterns of specific protein expression that differ from the parental strain. These shared properties of idhD and aco1D strains are eliminated or moderated by codisruption of the CIT1 gene encoding mitochondrial citrate synthase
-
-
?
additional information
?
-
-
citrate synthase is essential for nodule maintenance in infection of alfalfa
-
-
?
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5,5'-dithiobis(2-nitrobenzoate)
ACMX
-
competitive inhibitor versus acetyl-CoA
Ag+
almost complete inhibition at 2 mM
Cations
-
monovalent and divalent
-
dethiaacetyl-CoA
partial substrate
dithiothreitol
2 mM, almost complete loss of activity
EDTA
2 mM, 59% residual activity
elongation factor 1alpha
-
causes polymerization of 49K protein, reduced activity
-
Guanidinium chloride
-
irreversible inactivation of recombinant wild-type at 1.6 M and of recombinant mutant G196V at 0.2 M, at 0.5 M activation of the wild-type
H2O2
about 54% inhibition at 0.4 mM
Hg2+
95% inhibition at 2 mM
MnCl2
-
56% inhibition at 10 mM
N-ethylmaleimide
-
strong
NAD+
-
10 mM, 9% inhibition
p-hydroxymercuribenzoate
-
60% inhibition at 0.1 mM, protection by oxaloacetate
Pb2+
almost complete inhibition at 2 mM
phosphoenolpyruvate
5 mM, 14% residual activity
propionyl-CoA
-
competitive against acetyl-CoA
S-carboxymethyl-CoA
competitive inhibition versus acetyl-CoA, non-competitive inhibition versus oxaloacetate; inhibits the native enzyme competitively versus acetyl-CoA and non-competitively versus oxaloacetate
succinyl-CoA
-
mixed-type inhibition
Urea
-
irreversible inactivation of recombinant wild-type at 9.3 M and of recombinant mutant G196V at 5 M, at up to 8 M activation of the wild-type
2-oxoglutarate
-
30% inhibition at 1 mM
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
competitive against oxaloacetate
2-oxoglutarate
-
wild-type and mutants
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
competitive against oxaloacetate; no inhibition
2-oxoglutarate
5 mM, 2% residual activity
5,5'-dithiobis(2-nitrobenzoate)
-
inactivation of the glyoxysomal isozyme, half-life: approx. 1 min, not mitochondrial isozyme
5,5'-dithiobis(2-nitrobenzoate)
-
no inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
inactivation, half-lifes at 0.4 mM: 2.8 min for CS 1, 50 min for CS II
acetyl-CoA
-
no inhibition
acetyl-CoA
-
no inhibition
acetyl-CoA
-
substrate inhibition at high concentration
acetyl-CoA
-
no inhibition
acetyl-CoA
-
no inhibition
ADP
-
-
ADP
5 mM, 64.8% residual activity
ADP
-
25% inhibition at 5 mM
ADP
-
10 mM, 64% inhibition; 64% inhibition at 10 mM
ADP
-
30% inhibition at 1 mM, only CS II
ADP
-
CS II insensitive, CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
ADP
14% inhibition at 5 mM
AMP
-
-
AMP
5 mM, 60% residual activity
AMP
-
8% inhibition at 5 mM
AMP
-
10 mM, 36% inhibition; 36% inhibition at 10 mM
AMP
-
CS II insensitive, CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
ATP
-
possibly involved in enzyme regulation
ATP
-
50% inhibition at 7.5 mM, acetyl-CoA protects
ATP
10 mM, 83% inhibition
ATP
-
possibly involved in enzyme regulation
ATP
-
possibly involved in enzyme regulation
ATP
-
30% inhibition at 1 mM
ATP
-
competitive against acetyl-CoA
ATP
-
44% inhibition at 5 mM
ATP
-
25% inhibition at 10 mM
ATP
-
competitive against acetyl-CoA; no inhibition
ATP
5 mM, 89% residual activity
ATP
-
50% inhibition at 5 mM, competitive against acetyl-CoA; feed back inhibition
ATP
-
10 mM, 79% inhibition; 79% inhibition at 10 mM
ATP
-
isoenzyme CSII, 30% activity at 1 mM, isoenzyme CSI not inhibited at 1 mM
ATP
-
CS II insensitive, CS I inhibited
ATP
-
competitive against acetyl-CoA
ATP
32% inhibition at 5 mM
ATP
-
competitive against acetyl-CoA
ATP
-
competitive against acetyl-CoA, inhibition reduced by Mg2+
ATP
-
competitive against acetyl-CoA
ATP
-
20%, 40%, and 60% inhibition at 1 mM, 2 mM, and 5 mM ATP, respectively
CaCl2
-
29% inhibition at 10 mM
CaCl2
-
50% inhibition at 10 mM, not reversible by KCl
citrate
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
-
50% inhibition at 2.5 mM
citrate
product inhibition, competitive. Citrate binds tightly to the substrate binding site and its binding induces a compact closed conformation
citrate
5 mM, 1% residual activity
Co2+
2 mM, 50% residual activity
Co2+
22% inhibition at 2 mM
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
50% inhibition at 0.2 mM
Cu2+
2 mM, 12% residual activity
Cu2+
2 mM, almost complete loss of activity
Cu2+
-
87% decrease in activity
Cu2+
10% inhibition at 2 mM
HgCl2
-
-
iodoacetamide
-
10% inhibition at 0.002 mM
KCl
at 0.2 M KCl, approximately 60% of its maximal activity
KCl
-
9% inhibition at 50 mM
KCl
-
CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
Mg2+
2 mM, 0.29% residual activity
MgCl2
-
32% inhibition at 10 mM
MgCl2
-
50% inhibition at 7 mM, not reversible by KCl
Mn2+
2 mM, 72% residual activity
Mn2+
40% inhibition at 2 mM
Mn2+
100 mM, 48% residual activity
NaCl
-
15% inhibition at 50 mM
NADH
-
12% inhibition at 1 mM
NADH
-
not, only gram-negative facultative methylotrophs
NADH
-
70% inhibition at 2 mM, completely reversed by 0.17 mM 5'-AMP
NADH
-
reactivation by AMP
NADH
-
reactivation by AMP
NADH
allosteric; CS II, strong and specific allosteric inhibition
NADH
-
inhibition of wild-type enzyme. Inhibition is extremenly weak in mutant enzymes Y145A, R163L, and K167A
NADH
about 95% inhibition at 0.1 mM
NADH
-
0.1 M, 92% inhibition of wild-type, 25% inhibition of K283 acetylated variant, 88% inhibition of K295 acetylated variant, 7% inhibition of K168 acetylated variant
NADH
-
not, only gram-negative facultative methylotrophs
NADH
-
complete inhibition at 1 mM, completely reversible by NAD+
NADH
-
not, only gram-negative facultative methylotrophs
NADH
5 mM, 45% residual activity
NADH
-
10 mM, 31% inhibition; 1-10 mM; non-specific, 31% inhibition at 10 mM
NADH
-
78% inhibition by 0.1 mM of CS I, 15% inhibition of CS II at 1 mM; isoenzyme CSI 78% at 0.1 mM, allosteric, isoenzyme CSII 15% activity at 1 mM
NADH
-
inhibits large isoenzyme, reactivation by AMP
NADH
-
inhibits large isoenzyme, reactivation by AMP
NADH
-
inhibits the large form of the isoenzym, reactivation by AMP
NADH
-
CS II inhibited, CS II insensitive; weak inhibition, reversible by AMP, hinders the activation by AMP, CS II
NADH
-
inhibits large isoenzyme, reactivation by AMP
NADH
-
competitive against acetyl-CoA
NADH
-
51% inhibition of peroxisomal isozyme, 12% inhibition of mitochondrial isozyme at 5 mM
NADH
-
competitive against acetyl-CoA
NADH
-
competitive against acetyl-CoA
NADH
-
inhibition only with gram-negative bacterial enzymes; no effect
NADP+
-
no inhibition
NADP+
-
10 mM, 32% inhibition
NADP+
-
only CS II slightly
NADPH
-
29% inhibition at 0.25 mM
NADPH
-
10 mM, 57% inhibition; 57% inhibition at 10 mM
NADPH
-
40% inhibition by 5 mM, both isoenzymes
NADPH
-
competitive against acetyl-CoA
NADPH
-
competitive against acetyl-CoA
Ni2+
2 mM, 71% residual activity
Ni2+
2 mM, 74% residual activity
Ni2+
21% inhibition at 2 mM
oxaloacetate
-
no inhibition
oxaloacetate
-
no inhibition
oxaloacetate
-
substrate inhibition
oxaloacetate
-
no inhibition
oxaloacetate
-
no inhibition
p-chloromercuribenzoate
-
can be restored by dithiothreitol treatment
p-chloromercuribenzoate
-
6% loss at 0.002 mM
p-chloromercuribenzoate
-
strong
Zn2+
2 mM, 27% residual activity
Zn2+
2 mM, 16.8% residual activity
Zn2+
55% inhibition at 2 mM
additional information
-
the activity is not affected by O2, pCMB (0.05 mM), or EDTA (0.05 mM)
-
additional information
-
not inhibitory: NADH, AMP
-
additional information
-
tricarboxylic acid cycle intermediates
-
additional information
allosteric inhibition mechanism, structure relationship
-
additional information
-
allosteric inhibition mechanism, structure relationship
-
additional information
no inhibition by NADH or 2-oxaloacetate
-
additional information
-
low salt concentrations inactivate reversibly
-
additional information
-
isocitrate, (R)-3-hydroxybutyrate, malonate, pyruvate, acetoacetyl, NaCl, NH4Cl, CsCl, and RbCl have no effect
-
additional information
-
not affected by EDTA
-
additional information
-
NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
NADH and AMP not inhibitory for the small isoenzyme
-
additional information
-
NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
-
additional information
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
-
additional information
-
no inhibition by NAD+
-
additional information
not inhibited by EDTA
-
additional information
-
NADH and AMP are not inhibitory for isoenzyme small
-
additional information
not influenced by NADH
-
additional information
-
inhibited by a specific antibody against 49K protein
-
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Acidosis
Carbon flux through tricarboxylic acid cycle in rat renal tubules.
Adenocarcinoma
Pyruvate dehydrogenase, the citrate condensing enzyme and the utilization of 14 C-labeled lactate, pyruvate and alanine by slices of lactating mammary gland and adenocarcinoma of mouse mammary gland.
Amyotrophic Lateral Sclerosis
Enzymatic analysis of individual posterior root ganglion cells in olivopontocerebellar atrophy, amyotrophic lateral sclerosis and Duchenne muscular dystrophy.
Infections
Human skeletal muscle in bacterial infection: enzyme activities and their relationship to age.
Intermittent Claudication
Muscle enzyme adaptation in patients with peripheral arterial insufficiency: spontaneous adaptation, effect of different treatments and consequences on walking performance.
Muscular Diseases
Evidence for metabolic aberrations in asymptomatic persons with type 2 diabetes after initiation of simvastatin therapy.
Muscular Dystrophy, Duchenne
Enzymatic analysis of individual posterior root ganglion cells in olivopontocerebellar atrophy, amyotrophic lateral sclerosis and Duchenne muscular dystrophy.
Mycoplasma Infections
Human skeletal muscle in viral and mycoplasma infections: ultrastructural morphometry and its correlations to enzyme activities.
Obesity
Obesity affects mitochondrial citrate synthase in human omental adipose tissue.
Olivopontocerebellar Atrophies
Enzymatic analysis of individual posterior root ganglion cells in olivopontocerebellar atrophy, amyotrophic lateral sclerosis and Duchenne muscular dystrophy.
Pancreatitis
Cerulein-induced acute pancreatitis diminished vitamin E concentration in plasma and increased in the pancreas.
Phenylketonurias
Effect of phenylpyruvate on enzymes involved in fatty acid synthesis in rat brain.
Rickets
Mode of action of vitamin D; citrogenase and citric acid in dogs in induced rickets.
Sarcopenia
Impact of high-intensity interval training on cardiorespiratory fitness, body composition, physical fitness, and metabolic parameters in older adults: A meta-analysis of randomized controlled trials.
Spinal Cord Injuries
Sixteen weeks of testosterone with or without evoked resistance training on protein expression, fiber hypertrophy and mitochondrial health after spinal cord injury.
Starvation
Increased Fatty Acid beta-Oxidation after Glucose Starvation in Maize Root Tips.
Typhus, Epidemic Louse-Borne
Regulatory properties of citrate synthase from Rickettsia prowazekii.
Vasculitis, Central Nervous System
[Detection of a new species of Rickettsiae in the ticks of Ixodes persulcatus in Russia]
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0.002 - 90.3
oxaloacetate
0.0017 - 0.016
propionyl-CoA
additional information
additional information
-
0.00067
acetyl-CoA
-
wild-type, pH 8.0, 20°C
0.00085
acetyl-CoA
-
mutant W348Y, pH 8.0, 20°C
0.0017
acetyl-CoA
-
recombinant enzyme
0.0025
acetyl-CoA
methylcitrate synthase exhibiting also citrate synthase activity
0.003
acetyl-CoA
-
pH and temperature not specified in the publication
0.0036
acetyl-CoA
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
0.004
acetyl-CoA
-
wild-type
0.004
acetyl-CoA
-
mitochondrial isozyme CS I
0.0045
acetyl-CoA
-
recombinant mutant G196V
0.005
acetyl-CoA
-
wild-type
0.005
acetyl-CoA
-
recombinant wild-type
0.007
acetyl-CoA
-
dimeric enzyme form
0.0075
acetyl-CoA
pH and temperature not specified in the publication
0.0075
acetyl-CoA
25°C, pH and temperature not specified in the publication
0.01
acetyl-CoA
-
mutant H187Q, pH 8.0, 20°C
0.011
acetyl-CoA
-
recombinant wild-type and mutant S43C
0.011
acetyl-CoA
-
native peroxisomal isozyme CS II
0.0116
acetyl-CoA
pH 8.0, 25°C
0.012
acetyl-CoA
-
dimeric enzyme form
0.0123
acetyl-CoA
30°C, pH 8, recombinant enzyme
0.013 - 0.014
acetyl-CoA
-
recombinant peroxisomal isozyme CS II
0.014
acetyl-CoA
-
with 0.1 M KCl
0.0141
acetyl-CoA
30°C, pH 8, native enzyme
0.0165
acetyl-CoA
pH 8.0, 25°C
0.017
acetyl-CoA
-
mutant R344K, pH 8.0, 20°C
0.018
acetyl-CoA
pH 8.0, 25°C
0.032
acetyl-CoA
-
K283 acetylated variant, pH 7.8, 25°C
0.037
acetyl-CoA
-
mutant A361R/A10E
0.038
acetyl-CoA
-
mutant A361R
0.049
acetyl-CoA
-
mutant enzyme H110A, in presence of 0.1 M KCl
0.05
acetyl-CoA
-
in presence of 2.5 mM ATP
0.05
acetyl-CoA
-
isoenzyme CSII
0.056
acetyl-CoA
-
mutant enzyme Q182A, in presence of 0.1 M KCl
0.0584
acetyl-CoA
at pH 8.0 and 35°C
0.069
acetyl-CoA
-
mutant enzyme N189A, in presence of 0.1 M KCl
0.069
acetyl-CoA
-
mutant enzyme R109L, in presence of 0.1 M KCl
0.076
acetyl-CoA
pH 7.5, 37°C
0.079
acetyl-CoA
-
mutant enzyme T111A, in presence of 0.1 M KCl
0.08
acetyl-CoA
-
in presence of 5 mM ATP
0.08
acetyl-CoA
-
mutant enzyme R163L, in presence of 0.1 M KCl
0.088
acetyl-CoA
-
in presence of 100 mM KCl
0.089
acetyl-CoA
pH not specified in the publication, temperature not specified in the publication
0.098
acetyl-CoA
-
wild-type, pH 7.8, 25°C
0.11
acetyl-CoA
-
wild-type
0.12
acetyl-CoA
-
wild-type
0.12
acetyl-CoA
-
wild-type enzyme, in presence of 0.1 M KCl
0.143 - 0.161
acetyl-CoA
-
strains X and Hanham
0.145
acetyl-CoA
-
K168 acetylated variant, pH 7.8, 25°C
0.153
acetyl-CoA
presence of 5 mM ADP, pH 7.5, 37°C
0.174
acetyl-CoA
-
in absence of KCl
0.194
acetyl-CoA
presence of 5 mM phosphoenolpyruvate, pH 7.5, 37°C
0.2
acetyl-CoA
-
wild-type
0.21
acetyl-CoA
-
mutant enzyme T204A, in presence of 0.1 M KCl
0.22
acetyl-CoA
pH 7.5, 37°C
0.22
acetyl-CoA
-
mutant enzyme K167A, in presence of 0.1 M KCl
0.23
acetyl-CoA
-
mutant enzyme Y145A, in presence of 0.1 M KCl
0.26
acetyl-CoA
-
minimum at 1 M KCl
0.478
acetyl-CoA
-
K295 acetylated variant, pH 7.8, 25°C
0.69
acetyl-CoA
mutant enzyme G181E, pH and temperature not specified in the publication
0.7
acetyl-CoA
-
wild-type
0.75
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.86
acetyl-CoA
-
isoenzyme CSI
1.01
acetyl-CoA
mutant enzyme T204R, pH and temperature not specified in the publication
1.24
acetyl-CoA
-
mutant A10E
71.6
acetyl-CoA
at pH 8.0 and 20°C
123
acetyl-CoA
30°C, pH 8.0, recombinant enzyme
125
acetyl-CoA
30°C, pH 8.0, native enzyme
0.0005
citrate
-
mutant H187Q, pH 8.0, 20°C
0.0005
citrate
-
mutant W348Y, pH 8.0, 20°C
0.0007
citrate
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
0.001
citrate
-
wild-type, pH 8.0, 20°C
0.002
oxaloacetate
-
wild-type
0.002
oxaloacetate
-
mutant A361R
0.002
oxaloacetate
-
CS II
0.002
oxaloacetate
-
dimeric enzyme form with propionyl-CoA
0.002
oxaloacetate
-
isoenzyme CSII
0.003
oxaloacetate
-
mitochondrial isozyme CS I
0.003
oxaloacetate
-
dimeric enzyme form with acetyl-CoA
0.003
oxaloacetate
-
mutant enzyme H110A, in presence of 0.1 M KCl
0.003
oxaloacetate
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
0.003
oxaloacetate
-
mutant W348Y, pH 8.0, 20°C
0.003
oxaloacetate
-
wild-type, pH 8.0, 20°C
0.004
oxaloacetate
-
mutant enzyme T204A, in presence of 0.1 M KCl
0.0043
oxaloacetate
30°C, pH 8, native enzyme
0.005
oxaloacetate
-
recombinant enzyme
0.005
oxaloacetate
-
mutant enzyme R163L, in presence of 0.1 M KCl
0.0052
oxaloacetate
-
pH and temperature not specified in the publication
0.0057
oxaloacetate
-
recombinant mutant G196V
0.006
oxaloacetate
-
mutant A361R/A10E
0.006
oxaloacetate
-
hexameric enzyme form
0.006 - 0.007
oxaloacetate
-
native and recombinant peroxisomal isozyme CS II
0.0066
oxaloacetate
-
recombinant wild-type
0.007
oxaloacetate
-
wild-type
0.007
oxaloacetate
pH 7.5
0.007
oxaloacetate
-
mutant enzyme R109L, in presence of 0.1 M KCl
0.008
oxaloacetate
-
mutant A10E
0.0081
oxaloacetate
30°C, pH 8, recombinant enzyme
0.01
oxaloacetate
-
recombinant wild-type and mutant S34C
0.01
oxaloacetate
-
mutant enzyme Q182A, in presence of 0.1 M KCl
0.0105
oxaloacetate
mutant enzyme G181E, pH and temperature not specified in the publication
0.011
oxaloacetate
-
wild-type
0.011
oxaloacetate
-
in presence of KCl
0.011
oxaloacetate
wild type enzyme, pH and temperature not specified in the publication
0.0112
oxaloacetate
at pH 8.0 and 35°C
0.015
oxaloacetate
-
wild-type
0.015
oxaloacetate
-
mutant A361R
0.017
oxaloacetate
-
mutant enzyme N189A, in presence of 0.1 M KCl
0.018
oxaloacetate
-
minimum at 1 M KCl
0.018
oxaloacetate
-
mutant enzyme T111A, in presence of 0.1 M KCl
0.0183
oxaloacetate
pH and temperature not specified in the publication
0.0183
oxaloacetate
25°C, pH and temperature not specified in the publication
0.02
oxaloacetate
-
wild-type
0.02
oxaloacetate
-
mutant mutant loop/K313L/A361R
0.021
oxaloacetate
-
wild-type, pH 7.8, 25°C
0.023
oxaloacetate
-
K283 acetylated variant, pH 7.8, 25°C
0.025
oxaloacetate
-
K168 acetylated variant, pH 7.8, 25°C
0.026
oxaloacetate
-
wild-type
0.026
oxaloacetate
-
wild-type enzyme, in presence of 0.1 M KCl
0.026
oxaloacetate
30°C, pH 8.0, native enzyme
0.027
oxaloacetate
30°C, pH 8.0, recombinant enzyme
0.032
oxaloacetate
pH not specified in the publication, temperature not specified in the publication
0.032
oxaloacetate
-
K295 acetylated variant, pH 7.8, 25°C
0.037
oxaloacetate
-
mutant enzyme K167A, in presence of 0.1 M KCl
0.0414
oxaloacetate
pH 8.0, 25°C
0.05
oxaloacetate
-
CS II
0.051
oxaloacetate
-
mutant enzyme Y145A, in presence of 0.1 M KCl
0.054
oxaloacetate
-
mutant H187Q, pH 8.0, 20°C
0.073
oxaloacetate
presence of 5 mM ADP, pH 7.5, 37°C
0.091
oxaloacetate
pH 7.5, 37°C
0.103
oxaloacetate
pH 8.0, 25°C
0.108
oxaloacetate
presence of 5 mM phosphoenolpyruvate, pH 7.5, 37°C
0.138
oxaloacetate
pH 8.0, 25°C
0.22
oxaloacetate
at pH 8.1 and 28°C
0.37
oxaloacetate
-
mutant R344K, pH 8.0, 20°C
0.63
oxaloacetate
with propionyl-CoA, methylcitrate synthase exhibiting also citrate synthase activity
0.96
oxaloacetate
-
isoenzyme CSI
90.3
oxaloacetate
at pH 8.0 and 20°C
0.0017
propionyl-CoA
methylcitrate synthase exhibiting also citrate synthase activity
0.003
propionyl-CoA
-
dimeric enzyme form
0.004
propionyl-CoA
-
mutant A361R
0.008
propionyl-CoA
-
mutant loop/K313L/A361R
0.016
propionyl-CoA
-
wild-type
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km values for acetyl-CoA and oxaloacetate of mutants with a loop introduced into the active site
-
additional information
additional information
-
mutants, with and without KCl, overview
-
additional information
additional information
-
Km increases 5fold with salt concentration from 1 to 3 M, overview
-
additional information
additional information
-
influence of NADH and AMP on Km for acetyl-CoA
-
additional information
additional information
-
affinity for oxaloacetate is increased at adaption of growth temperature from 5 to 15°C
-
additional information
additional information
-
allosteric, Hill coefficient: 1.5
-
additional information
additional information
no difference in the apparent Km-value of oxaloacetate at any temperature, indicating that the substrate affinity of citrate synthase shows no adaption to changes in thermal environment
-
additional information
additional information
no difference in the apparent Km-value of oxaloacetate at any temperature, indicating that the substrate affinity of citrate synthase shows no adaption to changes in thermal environment
-
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0.0001 - 262.8
acetyl-CoA
0.0001 - 230.7
oxaloacetate
additional information
additional information
-
0.0001
acetyl-CoA
D317N mutant protein, value is very uncertain
0.0015
acetyl-CoA
D317G mutant protein
0.0133
acetyl-CoA
-
recombinant mutant G196V
0.03 - 0.55
acetyl-CoA
-
mutant W348Y, pH 8.0, 20°C
0.15
acetyl-CoA
-
recombinant wild-type
1.42
acetyl-CoA
presence of 5 mM phosphoenolpyruvate, pH 7.5, 37°C
2.51
acetyl-CoA
pH 7.5, 37°C
2.99
acetyl-CoA
presence of 5 mM ADP, pH 7.5, 37°C
3 - 6
acetyl-CoA
-
mutant enzyme Y145A, in presence of 0.1 M KCl
6.73
acetyl-CoA
-
mutant W348Y, pH 8.0, 20°C
7
acetyl-CoA
-
mutant A10E
8.3
acetyl-CoA
30°C, pH 8, native enzyme
8.51
acetyl-CoA
pH not specified in the publication, temperature not specified in the publication
8.56
acetyl-CoA
pH 8.0, 25°C
8.8
acetyl-CoA
30°C, pH 8, recombinant enzyme
9.17
acetyl-CoA
-
recombinant wild-type, pH 8.0
9.2
acetyl-CoA
wild-type protein
9.8
acetyl-CoA
-
wild-type, pH 8.0, 20°C
11
acetyl-CoA
-
mutant H187Q, pH 8.0, 20°C
11.2
acetyl-CoA
pH 7.5, 37°C
13
acetyl-CoA
-
mutant A361R/A10E
14.5
acetyl-CoA
-
mutant R344K, pH 8.0, 20°C
15
acetyl-CoA
-
mutant A361R
15.4
acetyl-CoA
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
17
acetyl-CoA
mutant enzyme T204R, pH and temperature not specified in the publication
17.1
acetyl-CoA
pH 8.0, 25°C
18
acetyl-CoA
-
wild-type
18
acetyl-CoA
mutant enzyme G181E, pH and temperature not specified in the publication
21
acetyl-CoA
-
hexameric enzyme form
22
acetyl-CoA
-
dimeric enzyme form
23
acetyl-CoA
pH 8.0, 25°C
44
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
54
acetyl-CoA
-
mutant enzyme T111A, in presence of 0.1 M KCl
67
acetyl-CoA
-
mutant enzyme H110A, in presence of 0.1 M KCl
78
acetyl-CoA
-
wild-type, + 0.1 M KCl
81
acetyl-CoA
-
wild-type, + 0.1 M KCl
81
acetyl-CoA
-
wild-type enzyme, in presence of 0.1 M KCl
84
acetyl-CoA
-
mutant enzyme K167A, in presence of 0.1 M KCl
95
acetyl-CoA
-
mutant enzyme Q182A, in presence of 0.1 M KCl
108
acetyl-CoA
-
mutant enzyme R163L, in presence of 0.1 M KCl
118
acetyl-CoA
-
mutant enzyme T204A, in presence of 0.1 M KCl
121
acetyl-CoA
-
mutant enzyme R109L, in presence of 0.1 M KCl
124
acetyl-CoA
-
mutant enzyme N189A, in presence of 0.1 M KCl
174
acetyl-CoA
-
with 0.1 M KCl
262.8
acetyl-CoA
at pH 8.0 and 35°C
0.5
citrate
-
mutant H187Q, pH 8.0, 20°C
7.75
citrate
-
mutant W348Y, pH 8.0, 20°C
9.17
citrate
-
recombinant enzyme, pH 8.0
11.4
citrate
-
wild-type, pH 8.0, 20°C
12.66
citrate
-
mutant H187Q, pH 8.0, 20°C
17.3
citrate
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
0.0001
oxaloacetate
D317N mutant protein, value is very uncertain
0.0015
oxaloacetate
D317G mutant protein
1.53
oxaloacetate
presence of 5 mM phosphoenolpyruvate, pH 7.5, 37°C
2.76
oxaloacetate
pH 7.5, 37°C
3 - 6
oxaloacetate
-
mutant enzyme Y145A, in presence of 0.1 M KCl
3.35
oxaloacetate
presence of 5 mM ADP, pH 7.5, 37°C
6.92
oxaloacetate
pH not specified in the publication, temperature not specified in the publication
7.62
oxaloacetate
pH 8.0, 25°C
8.3
oxaloacetate
30°C, pH 8, native enzyme
8.8
oxaloacetate
30°C, pH 8, recombinant enzyme
9.2
oxaloacetate
wild-type protein
24.5
oxaloacetate
pH 8.0, 25°C
31.9
oxaloacetate
pH 8.0, 25°C
54
oxaloacetate
-
mutant enzyme T111A, in presence of 0.1 M KCl
56
oxaloacetate
-
K295 acetylated variant, pH 7.8, 25°C
67
oxaloacetate
-
mutant enzyme H110A, in presence of 0.1 M KCl
81
oxaloacetate
-
wild-type enzyme, in presence of 0.1 M KCl
84
oxaloacetate
-
mutant enzyme K167A, in presence of 0.1 M KCl
89
oxaloacetate
-
K168 acetylated variant, pH 7.8, 25°C
92
oxaloacetate
-
wild-type, pH 7.8, 25°C
95
oxaloacetate
-
mutant enzyme Q182A, in presence of 0.1 M KCl
108
oxaloacetate
-
mutant enzyme R163L, in presence of 0.1 M KCl
114
oxaloacetate
-
K283 acetylated variant, pH 7.8, 25°C
118
oxaloacetate
-
mutant enzyme T204A, in presence of 0.1 M KCl
121
oxaloacetate
-
mutant enzyme R109L, in presence of 0.1 M KCl
124
oxaloacetate
-
mutant enzyme N189A, in presence of 0.1 M KCl
170
oxaloacetate
-
with 0.1 mM KCl
230.7
oxaloacetate
at pH 8.0 and 35°C
4
propionyl-CoA
-
mutant loop/K313L/A361R
6
propionyl-CoA
-
mutant A361R
8
propionyl-CoA
-
wild-type
12
propionyl-CoA
-
dimeric enzyme form
additional information
additional information
-
values for acetyl-CoA and oxaloacetate of mutants with a loop introduced into the active site
-
additional information
additional information
-
kcat is stable over pH-range 6.0-8.0
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
chimeric mutants, overview
-
additional information
additional information
-
chimeric mutants, overview
-
additional information
additional information
-
kcat with citrate and CoA
-
additional information
additional information
-
kcat with citrate and CoA
-
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malfunction
-
citrate synthase mutants exhibit altered colony morphology with enhanced pigmentation and reduced colony size and enter stationary phase early than the wild type enzyme
malfunction
-
citrate synthase mutants exhibit altered colony morphology with enhanced pigmentation and reduced colony size and enter stationary phase early than the wild type enzyme
-
metabolism
-
the enzyme is part of the tricarboxylic acid cycle
metabolism
the enzyme is involved in the methylcitric acid cycle
metabolism
-
recombinant wild-type CS has no detectable acetylation. Acetylation of lysine residues does not result in significantly different activities with that of the wild-type, except for residues K283 and K295. Acetylation at K283 increases the activity by nearly twofold, while acetylation at K295 decreased the activity by about 10fold. CS can be acetylated by acetyl-phosphate chemically, and be deacetylated by the CobB deacetylase
metabolism
-
the enzyme is involved in the methylcitric acid cycle
-
metabolism
-
the enzyme is part of the tricarboxylic acid cycle
-
physiological function
-
enzyme overexpression improves plant tolerance to iron stress in transgenic Arabidopsis, but also leads to increased fresh weight, root length, citrate synthase activity, and contents of chlorophyll, citrate acid and iron, especially when dealt with iron stress
physiological function
-
the enzyme is required for maximal virulence
physiological function
-
Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate-independently into acetyl-coenzyme A and oxaloacetate
physiological function
-
enzymatic activities of citrate synthase and isocitrate dehydrogenase IDH2 are significantly reduced in methyl 4 phenylpyridinium treatment cells, while protein acetylation of citrate synthase and IDH2 increase. Overexpressed sirtuin SIRT3 partially reverses at least, the decline of citrate synthase activity and the increase of citrate synthase protein acetylation
physiological function
expression in Arabidopsis thaliana improves Fe stress tolerance and leads to increased fresh weight, root length, CS activity, and increased contents of chlorophyll, citrate acid, Fe and Zn, especially when dealt with Fe stress. Ectopic expression of CS3 results in abnormal flowers in transgenic Arabidopsis thaliana
physiological function
loss of CitA promotes the accumulation of active CtrA, an essential cell cycle transcriptional regulator that maintains cells in G1-phase, provided that the (p)ppGpp alarmone is present. The enzymatic activity of CitA is dispensable for CtrA control, and functional citrate synthase paralogs cannot replace CitA in promoting S-phase entry. CitA is able to complement an Escherichia coli GltA mutant
physiological function
-
overexpression of CS1 in Escherichia coli enhances its growth under salt stress. Silencing of CS1 reduces fungal biomass at the middle stage of Puccinia striiformis infection, restricts fungal growth and development
physiological function
-
recombinant enzyme binds to murine macrophages, with low concentrations (5-10 microg/ml) enhancing phagocytosis and high levels (80 microg/ml) inhibiting phagocytosis. The secretion of interleukin-10, interleukin-1beta, transforming growth factor-beta1 and tumor necrosis factor-alpha of macrophages increase after the cells are incubated with CSI. Secretion of NO and cell proliferation of the macrophages are substantially reduced
physiological function
-
loss of CitA promotes the accumulation of active CtrA, an essential cell cycle transcriptional regulator that maintains cells in G1-phase, provided that the (p)ppGpp alarmone is present. The enzymatic activity of CitA is dispensable for CtrA control, and functional citrate synthase paralogs cannot replace CitA in promoting S-phase entry. CitA is able to complement an Escherichia coli GltA mutant
-
physiological function
-
the enzyme is required for maximal virulence
-
physiological function
-
Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate-independently into acetyl-coenzyme A and oxaloacetate
-
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171000
multi-angle light scattering
242000
-
sedimentation equilibrium centrifugation
249000 - 275000
-
equilibrium sedimentation
250000
-
sedimentation equilibrium centrifugation
28000
6 * 28000, SDS-PAGE
300000
-
CS II, gel filtration
33200
-
x * 33200, calculated from amino acid sequence
36500
-
2 * 36500, CS II, SDS-PAGE
37500
-
isoenzyme CSI 6 * 37500, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
41000
-
2 * 41000, SDS-PAGE
42600
-
2 * 42600, SDS-PAGE
42679
x * 42679, calculated from sequence
43000
-
2 * 43000, SDS-PAGE
43290
2 * 43290, calculated from amino acid sequence
44000
-
6 * 44000, SDS-PAGE, 6 * 49000, guanidine-HCl gel filtration
44700
-
6 * 44700, SDS-PAGE
46000
-
6 * 46000, SDS-PAGE, amino-terminal amino acid sequence
47000
-
6 * 47000, SDS-PAGE, or homopentamer
47885
6 * 47885, calculated from amino acid sequence
48700
-
2 * 48700, SDS-PAGE
49868
2 * 49868, MALDI-TOF mass spectrometry
50000
-
2 * 50000, CS II, SDS-PAGE
51100
-
x * 51100, calculated from sequence
51700
x * 51700, calculated
52000
2 * 52000, SDS-PAGE
52200
x * 52200, deduced from amino acid sequence
58500
-
4 * 58500, sedimentation equilibrium in guanidine-HCl and dithiothreitol
60000 - 70000
-
gel filtration
60000 - 95000
-
gel filtration, sedimentation equilibrium centrifugation
66000
-
4 * 66000, SDS-PAGE
69000
-
4 * 69000, sedimentation equilibrium in guanidine-HCl and dithiothreitol
100000
-
gel filtration
100000
-
dimeric enzyme form
105000
-
gel filtration
112000
-
gel filtration
150000
-
above: gram-negative methylotrophs, below: gram-positive methylotrophs
150000
-
above: gram-negative methylotrophs, below: gram-positive methylotrophs
150000
-
above: gram-negative methylotrophs, below: gram-positive methylotrophs
240000
-
gel filtration, CS I
240000
-
native CSI, gel filtration
280000
-
gel filtration
280000
-
hexameric enzyme form
40300
-
2 * 40300, SDS-PAGE, gel filtration in guanidine-HCl, amino acid composition
40300
-
2 * 40300, SDS-PAGE, gel filtration in guanidinium chloride
42000
x * 42000, SDS-PAGE
42000
-
2 * 42000, dimeric enzyme form, SDS-PAGE
42000
-
6 * 42000, CS i, SDS-PAGE
42000
-
isoenzyme CSII 2 * 42000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
45000
-
6 * 45000, hexameric enzyme form
48000
2 * 48000, SDS-PAGE
48000
-
6 * 48000, SDS-PAGE
48000
2 * 48000, mitochondrial enzyme, SDS-PAGE
48000
-
x * 48000, glyoxysomal isozyme, SDS-PAGE
49000
-
x * 49000, SDS-PAGE
49000
-
6 * 44000, SDS-PAGE, 6 * 49000, guanidine-HCl gel filtration
53000
-
2 * 53000, SDS-PAGE, CS I, reassociation to CS II possible
53000
-
6 * 53000, SDS-PAGE, CS II
80000
-
gel filtration
80300
-
CS II, gel filtration
80300
-
native CSII, gel filtration
84000
-
gel filtration
84000
-
Stokes radius, sedimentation coefficient
additional information
-
amino acid composition
additional information
-
amino acid composition
additional information
-
amino acid sequence
additional information
amino acid sequence
additional information
-
amino acid sequence alignment
additional information
amino acid sequence alignment
additional information
-
amino acid sequence alignment
additional information
-
amino acid sequence comparison
additional information
-
alignment of partial amino acid sequence
additional information
-
alignment of partial amino acid sequence
additional information
-
alignment of partial amino acid sequence
additional information
-
N-terminal protein sequence
additional information
-
N-terminal protein sequence
additional information
C-terminal amino acid sequence alignment
additional information
-
small and large enzyme
additional information
-
small and large enzyme
additional information
-
small and large enzyme
additional information
-
small and large enzyme
additional information
-
enzyme participates in multienzyme complexes of enzymes belonging to tricarbonic acid cycle, probably substrate channeling, in vivo NMR measurements
additional information
-
gram-negative bacteria: approximately 250000, gram-positive-bacteria and eucaryotes: approximately 100000
additional information
-
secondary and tertiary structure
additional information
secondary and tertiary structure
additional information
-
N-terminal protein sequence alignment
additional information
N-terminal protein sequence alignment
additional information
-
free enzyme forms various binary and ternary complexes with substrates
additional information
-
one isoenzyme, large form
additional information
-
one isoenzyme, large form
additional information
-
one isoenzyme, large form
additional information
-
one isoenzyme, small form
additional information
-
one isoenzyme, small form
additional information
-
one isoenzyme, small form
additional information
-
one isoenzyme, small form
additional information
-
two isoenzymes, a large and a small form
additional information
-
two isoenzymes, a large and a small form
additional information
-
two isoenzymes, a large and a small form
additional information
-
two isoenzymes, a large and a small form
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dimer or oligomer
the CS4 isoform is not only present as dimer but also as high-molecular-weight oligomer under native conditions
octamer
-
8 * 55001, calculated from sequence, 8 * 70000, SDS-PAGE of recombinant protein
?
x * 52200, deduced from amino acid sequence
?
-
x * 52200, deduced from amino acid sequence
-
?
-
x * 48000, glyoxysomal isozyme, SDS-PAGE
?
-
x * 51100, calculated from sequence
?
-
x * 42000, SDS-PAGE
-
?
-
x * 33200, calculated from amino acid sequence
?
x * 26300, calculated from sequence
?
x * 42679, calculated from sequence
?
-
x * 42679, calculated from sequence
-
?
-
x * 49000, SDS-PAGE
-
dimer
crystallization data
dimer
2 * 48000, mitochondrial enzyme, SDS-PAGE
dimer
-
2 * 48000, mitochondrial enzyme, SDS-PAGE
-
dimer
-
2 * 48700, SDS-PAGE
dimer
2 * 44162.7, MALDI-TOF, 2 * 43000, SDS-PAGE
dimer
-
2 * 40300, SDS-PAGE, gel filtration in guanidine-HCl, amino acid composition
dimer
-
2 * 40300, SDS-PAGE, gel filtration in guanidinium chloride
dimer
-
2 * 40300, SDS-PAGE, gel filtration in guanidine-HCl, amino acid composition
-
dimer
-
2 * 40300, SDS-PAGE, gel filtration in guanidinium chloride
-
dimer
-
2 * 36500, CS II, SDS-PAGE
dimer
-
isoenzyme CSII 2 * 42000, SDS-PAGE
dimer
-
2 * 36500, CS II, SDS-PAGE
-
dimer
-
isoenzyme CSII 2 * 42000, SDS-PAGE
-
dimer
-
2 * 53000, SDS-PAGE, CS I, reassociation to CS II possible
dimer
-
2 * 42600, SDS-PAGE
dimer
-
2 * 42000, dimeric enzyme form, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 50000, CS II, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
-
dimer
-
2 * 43000, SDS-PAGE
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
6 * 47000, SDS-PAGE, or homopentamer
hexamer
-
6 * 44000, SDS-PAGE, 6 * 49000, guanidine-HCl gel filtration
hexamer
-
6 * 46000, SDS-PAGE, amino-terminal amino acid sequence
hexamer
-
6 * 44700, SDS-PAGE
hexamer
-
6 * 44700, SDS-PAGE
-
hexamer
-
6 * 42000, CS i, SDS-PAGE
hexamer
-
isoenzyme CSI 6 * 37500, SDS-PAGE
hexamer
-
6 * 42000, CS i, SDS-PAGE
-
hexamer
-
isoenzyme CSI 6 * 37500, SDS-PAGE
-
hexamer
-
6 * 53000, SDS-PAGE, CS II
hexamer
-
6 * 45000, hexameric enzyme form
homodimer
2 * 52000, SDS-PAGE
homodimer
2 * 43290, calculated from amino acid sequence
homodimer
2 * 48000, SDS-PAGE
homodimer
2 * 49868, MALDI-TOF mass spectrometry
homodimer
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2 * 48000, SDS-PAGE
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homodimer
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2 * 49868, MALDI-TOF mass spectrometry
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homodimer
2 * about 50000
homohexamer
6 * 47885, calculated from amino acid sequence
homohexamer
6 * 28000, SDS-PAGE
tetramer
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4 * 69000, sedimentation equilibrium in guanidine-HCl and dithiothreitol
tetramer
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4 * 58500, sedimentation equilibrium in guanidine-HCl and dithiothreitol
tetramer
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4 * 58500, sedimentation equilibrium in guanidine-HCl and dithiothreitol
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tetramer
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4 * 66000, SDS-PAGE
additional information
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recombinant chimeric enzymes, domain functions, subunit organisation
additional information
subunit organization and crystal structure, amino acid residues involved in subunit interaction
additional information
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subunit organization and crystal structure, amino acid residues involved in subunit interaction
additional information
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recombinant chimeric enzymes, domain functions, subunit organisation
additional information
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CS I expressed from different structural gene than CS II
additional information
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CS I expressed from different structural gene than CS II
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additional information
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chimeric mutants with exchanged large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus, the large subunit is responsible for subunit interaction, the small subunit is responsable for catalytic activity
additional information
subunit organisation from crystal structure, dimer
additional information
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additional information
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additional information
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additional information
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chimeric mutants with exchanged large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus, the large subunit is responsible for subunit interaction, the small subunit is responsable for catalytic activity
additional information
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inter-subunit ionic network, molecular modeling
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in complex with oxaloacetate and inhibitor carboxymethyldethia-coenzyme A. The surface of citrate synthase is decoreated abundantly with basic side chains and this constellation is stable in varied pH environments
structure of apo-CSY4, at 2.69 A resolution. Dimerization of AtCSY4 is mainly mediated by alpha-helices H6, H7, H8, H12 and H13 from one molecule upon interaction with the corresponding alpha-helices from another molecule. The N-terminal (H1, H2, S1 and S2) and C-terminal (H20 and S6) regions are also important in dimerization
structural modeling and functional annotation
hanging drop vapour diffusion method, from 2-2.3 M ammonium sulfate, 2% v/v polyethylene glycol 400, 0.1 M HEPS, pH 6.0, X-ray diffraction analysis, structure determination and modeling: 3 identical dimer units arranged about a central 3-fold axis
hanging-drop vapour-diffusion method from 2.0-2.2 M ammonium sulfate, 2% PEG 400, and 0.1 M Na-HEPES at pH 6.0. the NADH-bound form of mutant R109L is obtained by soaking a variant crystal in a solution containing 1.22 mM NADH, 2.8 M ammonium sulfate, 2% polyethylene glycol 400 and 0.1 M Na-Hepes at pH 6.0
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crystal structure at 1.7 A resolution. Like other Type-I CS, citrate synthase functions as a dimer and each monomer consists of a large domain and a small domain. The oxaloacetate binding site locates at the cleft between the two domains, and the active site is more closed upon binding of the oxaloacetate substrate than binding of the citrate product
structure of the complex with acetyl-CoA, to 1.72 A resolution. Residues His218, His258, and Asp313 are located at the active site. The pantothenic acid part of acetyl-CoA is stabilized by the main chain of Gly255 and side chain of Asp313 by direct and water mediated hydrogen binding networks. The acetyl group in the acetyl-CoA tail is stabilized by two carbonyl group at the main chain of Pro216 and Gly219 through water-mediated hydrogen bonds
hanging drop vapor diffusion method, using 0.2 M magnesium chloride hexahydrate, 0.1M Tris pH 8.5, 3.4 M 1,6-hexandiol
crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus
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hanging drop vapour diffusion method, room temperature, 2 mg/ml protein concentration, precipitation by 0.1 M sodium citrate and 0.1 M ammonium phosphate, 20 mM Tris-HCl, pH 8.0, 25 mM KCl, x-ray structure analysis, structural basis of high thermostability
comparison of rigidity in citrate synthases from thermophiles to investigate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein
hanging-drop vapour diffusion method, 2.7 A resolution
wild type enzyme bound to calcium by the hanging drop vapor diffusion method, using 0.2 M calcium acetate, 0.1 M imidazole (pH 9.0), and 4-6% (w/v) PEG 8000, and an active site variant E151Q in complex with oxaloacetate by the sitting drop vapor diffusion method, using 5% (v/v) tascimate (pH 7.0), 0.1 M HEPES (pH 7.0), 10% (w/v) PEG monomethyl ether 5000 and about 40 mM guanidine hydrochloride
structure at 2.0 A resolution. Residues His184, His259, Arg268, Arg339, and Arg359', which are important residues for substrate binding, are exposed to the inner surface of the open cleft
structure at 2.7 A resolution. Putative substrate-binding residues His180, His215, His254, Arg263, Arg335, and Arg354' are structurally conserved
pH 7.8, PEG 3350, aspartame, benzamidine, cysteamine
comparison of rigidity in citrate synthases from thermophiles to investigate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein
crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus
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hanging drop vapor diffusion method, using 0.1 M CHES pH 9.5, 12% (w/v) PEG 4000, 1 mM oxaloacetate
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unliganded form and the enzyme in complex with oxaloacetate. Oxaloacetate is most likely the quencher of tryptophan fluorescence with the oxaloacetate carbonyl as the electron acceptor
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comparison of rigidity in citrate synthases from thermophiles to investgate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein
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A10E
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site-directed mutagenesis, reduced kcat, increased Km for acetyl-CoA
A361R
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site-directed mutagenesis, slightly reduced kcat , reduced Km for acetyl-CoA and increased Km for oxaloacetate, enhanced activity with propionyl-CoA
A361R/A10E
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site-directed mutagenesis, reduced kcat, reduced Km for acetyl-CoA
K313L
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site-directed mutagenesis
K313L/A361R
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site-directed mutagenesis
K313L/A361R/A10E
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site-directed mutagenesis
A10E
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site-directed mutagenesis, reduced kcat, increased Km for acetyl-CoA
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A361R
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site-directed mutagenesis, slightly reduced kcat , reduced Km for acetyl-CoA and increased Km for oxaloacetate, enhanced activity with propionyl-CoA
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A361R/A10E
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site-directed mutagenesis, reduced kcat, reduced Km for acetyl-CoA
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K313L
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site-directed mutagenesis
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D362A
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acetyl-CoA binding site mutant, reduced turnover, increased Ki for oxaloacetate and 2-oxoglutarate
F383A
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acetyl-CoA binding site mutant, reduced turnover
G181E
the mutant shows reduced activity compared to the wild type enzyme and is not inhibited by NADH
H229Q
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active site mutant, reduced turnover, increased Ki for 2-oxoglutarate
H264A
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acetyl-CoA binding site mutant, reduced turnover, increased Ki for oxaloacetate and 2-oxoglutarate
H305A
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active site mutant, reduced turnover
K167A
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extremely weak inhibition by NADH. Does not form hexamers in response to NADH, unlike the wild-type enzyme
R109L
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extremely weak inhibition by NADH. Great structural change. Both regions - residue 260-311 and 316-342 - are much less mobile than in wild-type enzyme
R163L
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extremely weak inhibition by NADH. Does not form hexamers in response to NADH, unlike the wild-type enzyme
R314L
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active site mutant, reduced turnover
R387L
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active site mutant, reduced turnover
R407L
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active site mutant, reduced turnover, increased Ki for oxaloacetate and 2-oxoglutarate
T204R
the mutant shows reduced activity compared to the wild type enzyme and is not inhibited by NADH
H309G
site-directed mutagenesis, mutant allelic strain, altered developmental phenotype
D177A
the mutant shows reduced activity compared to the wild type enzyme
E151Q
the mutant shows reduced activity compared to the wild type enzyme
E46Q
the mutant shows reduced activity compared to the wild type enzyme
H47A
the mutant shows reduced activity compared to the wild type enzyme
H96A
the mutant shows reduced activity compared to the wild type enzyme
R72A
the mutant shows reduced activity compared to the wild type enzyme
D12N
reference for pI-value analysis
D317G
D317 removes the acetyl-CoA methyl proton during catalysis
D317N
D317 removes the acetyl-CoA methyl proton during catalysis
G196V
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site-directed mutagenesis, mutation interferes with dimerization, improper dimerization or dissociation of the dimer, reduced enzyme activity and conformational stability
R344K
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analysis of tryptophan fluorescence
S43C
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site-directed mutagenesis, 5.7fold reduced activity, unaltered Km values for the substrates and unaltered thermostability
D113A
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site-directed mutagenesis, deletion of C-terminal amino acid residues which arrange the subunit contact, slightly increased Km for acetyl-CoA and oxaloacetate, slightly increased reaction velocity, reduced thermostability
D113A
mutant with reduce thermostability
D113S
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site-directed mutagenesis, deletion of C-terminal amino acid residues which arrange the subunit contact, slightly decreased Km for acetyl-CoA and oxaloacetate, slightly increased reaction velocity, reduced thermostability
D113S
mutant with reduce thermostability
H187Q
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analysis of tryptophan fluorescence
H222Q
active site
H222Q
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the mutant shows less than 0.05% of wild type activity
W245F/W115F/W17F
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analysis of tryptophan flourescence
W245F/W115F/W17F
containing a single W (W348)
W348Y
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analysis of tryptophan fluorescence, residue responsible for quenching effect
W348Y
primary emitter in fluorescence analysis
additional information
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chimeric proteins
additional information
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introduction of a loop into the active site of wild-type, mutant K313L, K313L/A361R/A10E , and mutant K313L/A361R, the latter showing increased thermostability and decreased temperature optimum for catalytic activity, Km and activities
additional information
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introduction of a loop into the active site of wild-type, mutant K313L, K313L/A361R/A10E , and mutant K313L/A361R, the latter showing increased thermostability and decreased temperature optimum for catalytic activity, Km and activities
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additional information
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whereas strain WTDELTAP1gltA still exhibits 15% of the activity of the wild type enzyme, no citrate synthase activity is detected in extracts of strain WTDELTAP12gltA
additional information
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construction of transgenic Arabidopsis thaliana plants ectopically overexpressing the Daucus carota citrate synthase gene via transformation with Agrobacterium tumefaciens, transgenic plants process the enzyme to its mature form, targeting into mitochondria, increased growth and phosphate accumulation
additional information
construction of transgenic Arabidopsis thaliana plants ectopically overexpressing the Daucus carota citrate synthase gene via transformation with Agrobacterium tumefaciens, transgenic plants process the enzyme to its mature form, targeting into mitochondria, increased growth and phosphate accumulation
additional information
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construction of transgenic Arabidopsis thaliana plants via Agrobacterium infection, functional expression and targeting to the mitochondria
additional information
construction of transgenic Arabidopsis thaliana plants via Agrobacterium infection, functional expression and targeting to the mitochondria
additional information
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chimeric proteins
additional information
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effect of active-site mutantions on substrate binding
additional information
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knockout of citrate syntase gltA or phosphoenolpyruvate carboxylase ppc decreases the maximum cell density by 10% and 7%, resp. Over-expression of gltA or ppc increases the maximum cell dry weight by 23% and 91% resp. No acetate excretion is detected at these increased cell densities
additional information
deletion mutants, altered developmental phenotypes, complete deletion reveals that the enzyme is more important for completion of meiosis than for catalytic activity
additional information
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deletion mutants, altered developmental phenotypes, complete deletion reveals that the enzyme is more important for completion of meiosis than for catalytic activity
additional information
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overexpression of Pseudomonas aeruginosa citrate synthase in transgenic alfalfa, Medicago sativa, plants leads to increased soil aluminum tolerance and increased exclusion of Al from the root tip, overview
additional information
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additional information
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construction of mutant with disrupted inter-subunit ionic network by partly eleminating the C-terminal end amino acid residues, increased Km for substrates, reduced thermostability
additional information
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construction of chimeric enzyme mutants with mix of the large and small subunits of Thermoplasma acidophilum and Pyrococcus furiosus, functional analysis of the subunits
additional information
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citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
additional information
citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
additional information
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citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
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additional information
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no channeling of oxaloacetate between malate dehydrogenase and citrate synthase in a recombinant fusion protein using a coupled assay
additional information
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construction of mutants with reduced enzymic activity by localized random PCR mutagenesis. In symbiosis with alfalfa, alfalfa plants form fully effective nodules when infected with Sinorhizobium meliloti mutants having as low as 7% of citrate synthase activity. Mutants with about 3% of wild-type citrate synthase activity form nodules with lower nitrogenase activity and a mutant with 0.5% of wild-type activity forms Fix-nodules
additional information
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construction of chimeric enzyme mutants with mix of the large and small subunits of Thermoplasma acidophilum and Pyrococcus furiosus, functional analysis of the subunits
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alfalfa is engineered by introducing the citrate synthase gene controlled by the Arabidopsis Act2 constitutive promoter or the tobacco RB7 root-specific promoter. Fifteen transgenic plants are assayed for exclusion of aluminum from the root tip, for internal citrate content, for growth in in vitro assays, or for shoot and root growth in either hydroponics or in soil assays. Based on the soil assays, two transgenic events are identified that are more aluminum-tolerant than the non-transgenic control, confirming that citrate synthase overexpression can be a useful tool to help achieve aluminum tolerance
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cloning and expression in Aspergillus nidulans, DNA sequence
cloning and expression of citA in Aspergillus niger, 11fold overexpression does not increase the citrate activity level in vivo
cloning and expression of wild-type and mutants in Escherichia coli
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cloning of His-tagged fusion protein of citrate synthase and mitochondrial malate dehydrogenase, expression in Escherichia coli
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codon-optimized expression in Escherichia coli
ectopic overexpression in Arabidopsis thaliana strain WS via infection with Agrobacterium tumefaciens, DNA sequence determination
expressed in Arabidopsis thaliana
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expressed in Bacillus subtilis
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expressed in Corynebacterium glutamicum strain ATCC 13032
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expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(lambdaDE3) cells
expressed in Escherichia coli C41(DE3) cells
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expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli Hms174(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli using the cytoplasmic expression vectors, pET3a and pET3d. The inactive enzyme is reactivated following overnight incubation in 2 M KCl
expressed in Nicotiana benthamiana
expressed in Pichia pastoris, expressed in Nicotiana tabacum
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expressed in Pseudomonas fluorescens ATCC 13525
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expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli with polyhistidine tags
expression of a chimeric protein with one Acinetobacter domain in Escherichia coli, domain interactions, subunit interactions
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expression of a chimeric protein with one Escherichia coli domain in Escherichia coli, domain interactions, subunit interactions
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expression of chimeric mutant in Escherichia coli citrate synthase deficient strain MOB154
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expression of labeled mitochondrial isozyme in Saccharomyces from plasmid, NMR measurements in vivo
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expression of wild-type and mutant in Escherichia coli
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expression of wild-type, chimeric mutant and site-directed mutants in Escherichia coli citrate synthase deficient strain MOB154
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functional expression in citrate synthase deficient Escherichia coli mutant strain K214 under control of lacZ promotor, DNA and amino acid sequence analysis
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functional expression of peroxisomal isozyme CS II in citrate synthase deficient Escherichia coli mutant and wild-type Escherichia coli strain
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in vitro translation of glyoxysomal isozyme, heterologous expression in Xenopus laevis oocytes
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overexpression in Escherichia coli
overexpression in Escherichia coli JM105, DNA and amino acid sequence analysis
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overexpression of the CS gene under control of the Arabidopsis thaliana Act2 constitutive promoter or the Nicotiana tabacum RB7 root-specific promoter in alfalfa, Medicago sativa, using the Agrobacterium tumefaciens, strain LBA4404, transformation method
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the 1195-bp fragment of the mitochondrial citrate synthase enzyme is cloned in antisense orientation into the vector pBINAR between the CaMV 35S promoter and the ocs terminator. This construct is introduced into plants by an Agrobacterium
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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