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Information on EC 4.2.3.3 - methylglyoxal synthase
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4.2.3.3 methylglyoxal synthaseIUBMB Comments
Does not act on D-glyceraldehyde 3-phosphate.
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Word Map
- 4.2.3.3
-
meibomian
-
glass
-
film
- tear
-
ocular
-
eyelid
-
gather
-
grading
-
grimace
-
saccade
- dihydroxyacetone
-
mongolian
- gerbil
-
glory
-
microgels
- monoglycerides
-
dropout
-
break-up
- 1,2-propanediol
-
ductility
-
schirmer
-
sire
- dhap
- polydactyly
-
alloy
-
phantom
-
corrosion
- microtia
-
orifice
- encephalocele
- cdt1
- orc6
-
pre-replication
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mgs, methylglyoxal synthase, methylglyoxal synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 4.2.99.11
-
-
formerly
-
methylglyoxal synthase
methylglyoxal synthetase
-
-
-
-
MGS
MgsA
msgA
synthase, methylglyoxal
-
-
-
-
MGS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycerone phosphate = 2-oxopropanal + phosphate
stereospecific deprotonation of the pro-S hydrogen at C-3 of dihydroxyacetone, the true product of the enzymatic reaction is the enol form of methylglyoxal which is ketonized in solution
-
glycerone phosphate = 2-oxopropanal + phosphate
since the enzyme accepts the trans-enediol-phosphate as a substrate, it is likely that it or the trans-enediolate is an intermediate in the catalytic reaction with dihydroxyacetone phosphate
-
glycerone phosphate = 2-oxopropanal + phosphate
does not act on D-glyceraldehyde 3-phosphate
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Does not act on D-glyceraldehyde 3-phosphate.
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CAS REGISTRY NUMBER
COMMENTARY
37279-01-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycerone phosphate
pyruvaldehyde + phosphate
-
tautomerization to methylglyoxal
-
?
dihydroxyacetone phosphate
?
-
first enzyme in the reaction sequence for the conversion of dihydroxyacetone phosphate to pyruvate, may play a role in the control of glycolysis
-
-
?
dihydroxyacetone phosphate
?
-
during elevated metabolism, the synthesis of methylglyoxal from dihydroxyacetone phosphate temporarily relieves the cells from stress caused by phosphorylated intermediates and allows the cells to grow for a limited time. If during this period the environment changes, e.g. the level of the carbon source is reduced, the cells are not only able to survive but are also able to colonize their environment
-
-
?
dihydroxyacetone phosphate
?
-
the enzyme plays an important role in the catabolism of the triose phosphates
-
-
?
dihydroxyacetone phosphate
?
-
first enzyme in the reaction sequence for the conversion of dihydroxyacetone phosphate to pyruvate, may play a role in the control of glycolysis
-
-
?
dihydroxyacetone phosphate
?
-
the enzyme is involved in the methylglyoxal by-pass
-
-
?
dihydroxyacetone phosphate
?
-
constitutive enzyme, may be involved in by-pass sequence for part of the Embden-Meyerhof glycolytic pathway
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
strictly specific for
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
the true product of the enzymatic reaction is the enol form of methylglyoxal which is ketonized in solution
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
catalyzes the elimination reaction of DHAP, which leads to phosphate and the enol of methylglyoxal, which is subsequently tautomerized to methylglyoxal in solution
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
converts dihydrocyacetone phosphate to a cis-enediolic intermediate, then catalyses the elimination of phosphate to form the enol of methylglyoxal
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
converts dihydrocyacetone phosphate to enol pyruvaldehyde, this enol then tautomerizes to methylglyoxal in solution
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
intermediate is enol pyruvaldehyde is stereospecifically formed
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
strictly specific for
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
since the enzyme accepts the trans-enediol-phosphate as a substrate, it is likely that it or the trans-enediolate is an intermediate in the catalytic reaction with dihydroxyacetone phosphate
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
strictly specific for
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
-
?
glycerone phosphate
methylglyoxal + phosphate
-
the unregulated production of methylglyoxal appears to be due to a rapid increase in the glycolysis intermediates from ribose degradation. Such a metabolic burden may result in methylglyoxal production by methylglyoxal synthase
-
-
?
additional information
?
-
enzyme dos no catalyze the elimination reaction with glyceraldehyde phosphate
-
?
additional information
?
-
enzyme is not capable of abstracting the C2 proton from glyceraldehyde phosphate, which is an absolute requirement for the function of MGS
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate
?
-
first enzyme in the reaction sequence for the conversion of dihydroxyacetone phosphate to pyruvate, may play a role in the control of glycolysis
-
-
?
dihydroxyacetone phosphate
?
-
during elevated metabolism, the synthesis of methylglyoxal from dihydroxyacetone phosphate temporarily relieves the cells from stress caused by phosphorylated intermediates and allows the cells to grow for a limited time. If during this period the environment changes, e.g. the level of the carbon source is reduced, the cells are not only able to survive but are also able to colonize their environment
-
-
?
dihydroxyacetone phosphate
?
-
the enzyme plays an important role in the catabolism of the triose phosphates
-
-
?
dihydroxyacetone phosphate
?
-
first enzyme in the reaction sequence for the conversion of dihydroxyacetone phosphate to pyruvate, may play a role in the control of glycolysis
-
-
?
dihydroxyacetone phosphate
?
-
the enzyme is involved in the methylglyoxal by-pass
-
-
?
dihydroxyacetone phosphate
?
-
constitutive enzyme, may be involved in by-pass sequence for part of the Embden-Meyerhof glycolytic pathway
-
-
?
glycerone phosphate
methylglyoxal + phosphate
-
the unregulated production of methylglyoxal appears to be due to a rapid increase in the glycolysis intermediates from ribose degradation. Such a metabolic burden may result in methylglyoxal production by methylglyoxal synthase
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-bromoacetol phosphate
-
irreversible inactivation by reacting with a nucleophilic group located in the active center, dihydroxyacetone phosphate or phosphate protects
3-iodoacetol phosphate
-
irreversible inactivation by reacting with a nucleophilic group located in the active center, dihydroxyacetone phosphate or phosphate protects
Crh protein
in the absence of preferred carbon sources, the phosphoprotein Crh is present in the nonphosphorylated state and binds to and thereby inhibits the enzyme
-
Phosphoglycolate
inhibits wild-type enzyme and activates H98Q variant
phosphoglycolohydroxamic acid
-
tight binding inhibitor, neither a strictly competitive, non-competitive, nor uncompetitive mechanism
additional information
-
no inactivation by iodoacetate or p-mercuribenzoate
-
phosphate
acts as competitive inhibitor on the H98Q variant and as an allosteric-type inhibitor on the wild-type enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
dihydroxyacetone phosphate
mutant S55K, Hill coefficient 1.3, pH 6.5, 60°C
0.21
dihydroxyacetone phosphate
mutant carrying C-terminal extension YQRYLADRLK, pH 6.0, 60°C, Hill coefficient 1.5
0.21
dihydroxyacetone phosphate
mutant carrying C-terminus of Escherichia coli enzyme, Hill coefficient 0.87, pH 6.5, 60°C
0.25
dihydroxyacetone phosphate
mutant carrying C-terminal extension YQRYLADRLK C-terminal extension YQRYLADRLK plus mutation D10N, pH 6.0, 60°C, Hill coefficient 1.5
0.41
dihydroxyacetone phosphate
mutant mutant carrying C-terminus of Escherichia coli enzyme, Hill coefficient 1.99, presence of 1.5 mM phosphate, pH 6.5, 60°C
0.5
dihydroxyacetone phosphate
wild-type, Hill coefficient 1, pH 6.5, 60°C
0.5
dihydroxyacetone phosphate
wild-type, pH 6.0, 60°C, Hill coefficient 1.5
0.6
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, presence of phosphoglycolate
0.67
dihydroxyacetone phosphate
carrying one additional His residue between residues Arg22 and His23, Hill coefficient 1.58, pH 6.2, 60°C
0.75
dihydroxyacetone phosphate
mutant D10N, pH 6.0, 60°C, Hill coefficient 1.5
0.8
dihydroxyacetone phosphate
wild-type, Hill coefficient 1.2, presence of 1 mM phosphate, pH 6.5, 60°C
0.83
dihydroxyacetone phosphate
wild-type, Hill coefficient 2.2, pH 6.2, 60°C
1.03
dihydroxyacetone phosphate
mutant V101A, Hill coefficient 1, pH 6.5, 60°C
1.17
dihydroxyacetone phosphate
wild-type, Hill coefficient 1.5, presence of 1.5 mM phosphate, pH 6.5, 60°C
1.25
dihydroxyacetone phosphate
mutant G56S, Hill coefficient 2.3, pH 6.5, 60°C
1.3
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, absence of phosphoglycolate
1.35
dihydroxyacetone phosphate
-
mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C
1.38
dihydroxyacetone phosphate
mutant S55K, Hill coefficient 1.3, presence of 1.5 mM phosphate, pH 6.5, 60°C
1.44
dihydroxyacetone phosphate
mutant V101I, Hill coefficient 1.44, pH 6.5, 60°C
1.45
dihydroxyacetone phosphate
carrying two additional His residues between residues Arg22 and His23, Hill coefficient 2.12, pH 6.2, 60°C
1.5
dihydroxyacetone phosphate
mutant R97E, Hill coefficient 3.4, pH 6.5, 60°C
1.6
dihydroxyacetone phosphate
mutant R97E, Hill coefficient 3.7, presence of 1 mM phosphate, pH 6.5, 60°C
1.65
dihydroxyacetone phosphate
mutant V101S, Hill coefficient 1.3, pH 6.5, 60°C
1.7
dihydroxyacetone phosphate
mutant DELTAR97, Hill coefficient 3.3, pH 6.5, 60°C
1.7
dihydroxyacetone phosphate
mutant DELTAR97, Hill coefficient 5.2, presence of 1 mM phosphate, pH 6.5, 60°C
1.81
dihydroxyacetone phosphate
mutant V101A, Hill coefficient 1.45, presence of 1.5 mM phosphate, pH 6.5, 60°C
2.4
dihydroxyacetone phosphate
mutant G56A, Hill coefficient 2, pH 6.5, 60°C
2.7
dihydroxyacetone phosphate
mutant V101I, Hill coefficient 1.4, presence of 1.5 mM phosphate, pH 6.5, 60°C
2.74
dihydroxyacetone phosphate
-
wild-type, Hill coefficient 1, pH 7.0, 60°C
2.76
dihydroxyacetone phosphate
mutant G56A, Hill coefficient 1.6, presence of 1.5 mM phosphate, pH 6.5, 60°C
2.76
dihydroxyacetone phosphate
mutant S55D, Hill coefficient 1, pH 6.5, 60°C
2.79
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.55, pH 6.5, 60°C
2.8
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.5, pH 6.5, 60°C
3.2
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.5, presence of 1 mM phosphate, pH 6.5, 60°C
3.27
dihydroxyacetone phosphate
mutant S55D, Hill coefficient 1.2, presence of 1.5 mM phosphate, pH 6.5, 60°C
3.5
dihydroxyacetone phosphate
mutant G56S, Hill coefficient 2.8, presence of 1.5 mM phosphate, pH 6.5, 60°C
5.03
dihydroxyacetone phosphate
mutant V101S, Hill coefficient 1.22, presence of 1.5 mM phosphate, pH 6.5, 60°C
6.3
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.55, presence of 1.5 mM phosphate, pH 6.5, 60°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00003
dihydroxyacetone phosphate
mutant G56S, Hill coefficient 2.8, presence of 1.5 mM phosphate, pH 6.5, 60°C
0.00005
dihydroxyacetone phosphate
mutant G56S, Hill coefficient 2.3, pH 6.5, 60°C
0.0001
dihydroxyacetone phosphate
mutant G56A, Hill coefficient 1.6, presence of 1.5 mM phosphate, pH 6.5, 60°C
0.00013
dihydroxyacetone phosphate
mutant G56A, Hill coefficient 2, pH 6.5, 60°C
0.00025
dihydroxyacetone phosphate
mutant DELTAR97, Hill coefficient 5.2, presence of 1 mM phosphate, pH 6.5, 60°C
0.00025
dihydroxyacetone phosphate
mutant R97E, Hill coefficient 3.7, presence of 1 mM phosphate, pH 6.5, 60°C
0.0004
dihydroxyacetone phosphate
mutant R97E, Hill coefficient 3.4, pH 6.5, 60°C
0.001
dihydroxyacetone phosphate
mutant DELTAR97, Hill coefficient 3.3, pH 6.5, 60°C
0.09
dihydroxyacetone phosphate
mutant carrying C-terminal extension YQRYLADRLK C-terminal extension YQRYLADRLK plus mutation D10N, pH 6.0, 60°C, Hill coefficient 1.5
0.37
dihydroxyacetone phosphate
mutant V101I, Hill coefficient 1.4, presence of 1.5 mM phosphate, pH 6.5, 60°C
0.41
dihydroxyacetone phosphate
mutant D10N, pH 6.0, 60°C, Hill coefficient 1.5
0.5
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.5, presence of 1 mM phosphate, pH 6.5, 60°C
0.55
dihydroxyacetone phosphate
mutant S55K, Hill coefficient 1.3, presence of 1.5 mM phosphate, pH 6.5, 60°C
0.62
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.55, presence of 1.5 mM phosphate, pH 6.5, 60°C
0.7
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.5, pH 6.5, 60°C
0.75
dihydroxyacetone phosphate
mutant R97K, Hill coefficient 1.55, pH 6.5, 60°C
0.75
dihydroxyacetone phosphate
mutant V101I, Hill coefficient 1.44, pH 6.5, 60°C
0.96
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, absence of phosphoglycolate
1
dihydroxyacetone phosphate
mutant S55K, Hill coefficient 1.3, pH 6.5, 60°C
1.1
dihydroxyacetone phosphate
mutant V101S, Hill coefficient 1.22, presence of 1.5 mM phosphate, pH 6.5, 60°C
1.4
dihydroxyacetone phosphate
mutant V101S, Hill coefficient 1.3, pH 6.5, 60°C