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L-Cysteine sulfinate
D-Cysteine sulfinate
additional information
?
-
D-aspartate
L-aspartate
JT020910
-
-
-
r
D-aspartate
L-aspartate
-
-
-
r
D-aspartate
L-aspartate
-
-
-
r
D-aspartate
L-aspartate
-
-
-
r
D-aspartate
L-aspartate
-
-
-
r
D-aspartate
L-aspartate
-
-
-
-
r
D-aspartate
L-aspartate
-
-
-
-
r
D-aspartate
L-aspartate
D-Asp is the preferred substrate
-
-
r
D-aspartate
L-aspartate
D-Asp is the preferred substrate
-
-
r
L-Ala
D-Ala
-
at half the rate of Asp
-
?
L-Ala
D-Ala
-
no racemase activity
-
-
?
L-Asp
D-Asp
-
-
-
-
?
L-Asp
D-Asp
-
enzyme exclusively acts on L-Asp and D-Asp
-
-
r
L-Asp
D-Asp
-
enzyme exclusively acts on L-Asp and D-Asp
-
-
r
L-Asp
D-Asp
-
the enzyme regulates synthesis of the endogenous D-Asp
-
-
?
L-aspartate
D-aspartate
JT020910
-
-
-
r
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
-
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
-
-
-
?
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction
-
-
r
L-aspartate
D-aspartate
-
-
-
-
r
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
-
-
-
r
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
-
-
?
L-aspartate
D-aspartate
-
cell wall synthesis
-
?
L-aspartate
D-aspartate
-
-
-
-
?
L-aspartate
D-aspartate
-
-
-
-
r
L-aspartate
D-aspartate
-
the Asp racemase reaction is reversible, and D- and L-Asp are formed from the corresponding enantiomers in the reaction mixture. In the reaction mixture, the L-Asp substrate initially binds to Asp racemase and D-Asp is released from the enzyme as the reaction product
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
56.4% of the activity in the reverse reaction direction
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
56.4% of the activity in the reverse reaction direction
-
-
r
L-aspartate
D-aspartate
-
the enzyme is highly selective for aspartate. No detectable racemase activity against Glu, Ala, Lys, Phe, or Ser in the assays incubated at 45°C. Even at 70°C, the racemase activity using Ala as a substrate is low
-
-
r
L-aspartate
D-aspartate
-
the enzyme is highly selective for aspartate. No detectable racemase activity against Glu, Ala, Lys, Phe, or Ser in the assays incubated at 45°C. Even at 70°C, the racemase activity using Ala as a substrate is low
-
-
r
L-Cysteate
D-Cysteate
-
-
-
-
?
L-Cysteate
D-Cysteate
-
at 88% of the activity relative to L-Asp
-
?
L-Cysteine sulfinate
D-Cysteine sulfinate
-
-
-
-
?
L-Cysteine sulfinate
D-Cysteine sulfinate
-
at 51% of the activity relative to L-Asp
-
?
additional information
?
-
-
SbAspR catalyzes both racemization and dehydration. Residue Arg140 recognizes the beta-carboxyl group of the substrate aspartate in SbAspR
-
-
?
additional information
?
-
the enzyme AspR also shows negligible serine racemase, SerR (EC 5.1.1.18), activity
-
-
?
additional information
?
-
-
no racemase activity with Glu
-
-
?
additional information
?
-
-
the aspartate aminotransferase, UniProt ID Q8NHS2, EC 2.6.1, exhibits low aspartate racemase activity in contrast to the murine enzyme GOT1L1
-
-
?
additional information
?
-
recombinant Got1l1 protein is a pyridoxal 5'-phosphate-dependent enzyme and synthesizes substantial D-aspartate from L-aspartate and only one-fifth as much L-glutamate, with very little D-glutamate in vitro
-
-
?
additional information
?
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-
recombinant Got1l1 protein is a pyridoxal 5'-phosphate-dependent enzyme and synthesizes substantial D-aspartate from L-aspartate and only one-fifth as much L-glutamate, with very little D-glutamate in vitro
-
-
?
additional information
?
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recombinant Got1l1 expressed in mammalian cells shows L-aspartate aminotransferase activity, but lacks aspartate racemase activity. When L-aspartate and 2-oxoglutarate are reacted with the Got1l1 purified from HEK293T cells, neither D-aspartate nor D-glutamate is generated, but a detectable amount of L-glutamate is obtained
-
-
?
additional information
?
-
-
recombinant Got1l1 expressed in mammalian cells shows L-aspartate aminotransferase activity, but lacks aspartate racemase activity. When L-aspartate and 2-oxoglutarate are reacted with the Got1l1 purified from HEK293T cells, neither D-aspartate nor D-glutamate is generated, but a detectable amount of L-glutamate is obtained
-
-
?
additional information
?
-
the enzyme AspR also shows low serine racemase, SerR (EC 5.1.1.18), activity
-
-
?
additional information
?
-
the enzyme is also active in the racemisation of L- and D-serine, EC 5.1.1.18
-
-
?
additional information
?
-
Picrophilus torridus aspartate racemase is highly specific to aspartate
-
-
?
additional information
?
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-
Picrophilus torridus aspartate racemase is highly specific to aspartate
-
-
?
additional information
?
-
PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested
-
-
?
additional information
?
-
-
PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested
-
-
?
additional information
?
-
Picrophilus torridus aspartate racemase is highly specific to aspartate
-
-
?
additional information
?
-
PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested
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-
?
additional information
?
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-
the glutamic-oxaloacetic transaminase 1-like 1, UniProt ID A0A0U1RVK4, exhibits low aspartate racemase activity in contrast to the murine enzyme GOT1L1
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-
?
additional information
?
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-
no racemase activity with Asp, Cys, Pro, and hydroxyproline
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-
?
additional information
?
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-
development of a sensitive assay method for measuring aspartate-specific amino acid racemase activity using recombinant Streptococcus thermophilus Asp racemase as a model enzyme. The coupling method (using D-Asp oxidase (DDO), a degradative enzyme that stereospecifically acts on D-Asp) is more accurate and sensitive than the other two methods analyzed, and can be used for the determination of Asp racemase activity, overview. DDO is concomitantly included in the Asp racemase reaction mixture, and the Asp racemase reaction is readily coupled to the D-Asp degradative reaction by DDO during the incubation. Human DDO is used to degrade D-Asp formed from L-Asp by the Asp racemase reaction to 2-oxoacid, the amounts of which are determined using a colorimetric assay. Methods evaluation and optimization, overview
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-
?
additional information
?
-
the enzyme also acts on L-cysteic acid and L-cysteine sulfinic acid (with below 30% activity compared to D-aspartate) in addition to D- and L-aspartic acids. No activity with D-glutamate, D-asparagine, D-glutamine, D-alanine, D-leucine, D-valine, D-proline, D-serine, D-threonine, and D-arginine
-
-
?
additional information
?
-
-
the enzyme also acts on L-cysteic acid and L-cysteine sulfinic acid (with below 30% activity compared to D-aspartate) in addition to D- and L-aspartic acids. No activity with D-glutamate, D-asparagine, D-glutamine, D-alanine, D-leucine, D-valine, D-proline, D-serine, D-threonine, and D-arginine
-
-
?
additional information
?
-
the enzyme also acts on L-cysteic acid and L-cysteine sulfinic acid (with below 30% activity compared to D-aspartate) in addition to D- and L-aspartic acids. No activity with D-glutamate, D-asparagine, D-glutamine, D-alanine, D-leucine, D-valine, D-proline, D-serine, D-threonine, and D-arginine
-
-
?
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evolution
the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate
evolution
the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate
evolution
JT020910
the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate
evolution
the essential cysteine residues are conserved as Cys83 and Cys194
evolution
-
the essential cysteine residues are conserved as Cys83 and Cys194
-
malfunction
-
depletion of aspartate racemase by retrovirus-mediated expression of short-hairpin RNA in newborn neurons of the adult hippocampus elicits profound defects in the dendritic development and survival of newborn neurons and survival
malfunction
-
retrovirus-mediated expression of short-hairpin RNA complementary to aspartate racemase in newborn neurons of the hippocampus results in a defect in dendritic development and impaired survival of the newborn neurons
malfunction
D-aspartate contents of wild-type and Got1l1 knockout mice are not significantly different in the testis and hippocampus. The recombinant Got1l1 expressed in mammalian cells shows L-aspartate aminotransferase activity, but lacks aspartate racemase activity
malfunction
-
knockdown of Got1l1 does not reduce the total D-Asp content of the cells and their culture medium
malfunction
-
knockdown of Got1l1 does not reduce the total D-Asp content of the cells and their culture medium
malfunction
substituting the triple serine loop region in AspRs enhances serine racemization
malfunction
substituting the triple serine loop region in AspRs enhances serine racemization. Single amino acid substitution mutants, H150S, P151S and N152S, reveal several effects on activity. The Ser150 substitution decreases all enzyme activities, especially the serine dehydrogenase (SDH) activity, while Ser151 dramatically increases the SerR and AspR activities with no change on SDH activity. An increase in the AspR activity is observed after introducing Ser152, while there is little or no change in the other activities
malfunction
JT020910
substituting the triple serine loop region in AspRs enhances serine racemization. Single amino acid substitution mutants, H150S, P151S and N152S, reveal several effects on activity. The Ser150 substitution decreases all enzyme activities, especially the serine dehydrogenase (SDH) activity, while Ser151 dramatically increases the SerR and AspR activities with no change on SDH activity. An increase in the AspR activity is observed after introducing Ser152, while there is little or no change in the other activities
metabolism
because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus
metabolism
enzyme Got1l1 is not the major aspartate racemase, there might be another D-aspartate-synthesizing enzyme
metabolism
-
because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus
-
physiological function
-
aspartate racemase regulates adult neurogenesis
physiological function
-
enzyme GOT1L1 contributes little, if at all, to the biosynthesis of D-Asp in human cells, relationships between the D-Asp content and expression levels of Got1l1 and Ddo mRNAs in cultured human cells
physiological function
-
enzyme GOT1L1 contributes little, if at all, to the biosynthesis of D-Asp in rat cells, relationships between the D-Asp content and expression levels of Got1l1 and Ddo mRNAs in cultured rat cells, overview
physiological function
in the hippocampus, D-aspartate strongly enhances N-methyl-D-aspartate receptor-dependent long-term potentiation and is involved in learning and memory
physiological function
-
the enzyme from the lactic acid bacterium Lactobacillus sakei NBRC 15893 is considered to be involved in D-aspartate synthesis during the brewing process of Japanese sake at low temperatures
physiological function
-
the enzyme is responsible for D-aspartate biosynthesis in vivo. Enzyme SbAspR is a type II PLP-dependent enzyme. D-Aspartate is one of the most abundant free D-amino acids present in the nervous and reproductive systems and plays important physiological roles, including regulating developmental processes, hormone secretion and steroidogenesis
physiological function
-
the enzyme from the lactic acid bacterium Lactobacillus sakei NBRC 15893 is considered to be involved in D-aspartate synthesis during the brewing process of Japanese sake at low temperatures
-
additional information
amino acid analysis of cell-free extract, overview
additional information
-
amino acid analysis of cell-free extract, overview
additional information
important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview
additional information
important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview
additional information
JT020910
important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview
additional information
-
residue Arg140 recognizes the beta-carboxyl group of the substrate aspartate in SbAspR. The aromatic proline interaction between the domains, which favours the closed form of SbAspR, might influence the arrangement of Arg140 at the active site, active site structure of SbAspR, overview
additional information
-
amino acid analysis of cell-free extract, overview
-
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Adams, E.
Amino acid racemases and epimerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
479-507
1972
Limosilactobacillus fermentum, Pseudomonas sp.
-
brenda
Lamont, H.C.; Staudenbauer, W.L.; Strominger, J.L.
Partial purification and characterization of an aspartate racemase from Streptococcus faecalis
J. Biol. Chem.
247
5103-5106
1972
Enterococcus faecalis
brenda
Yamaguchi, T.; Choi, S.Y.; Okada, H.; Yohda, M.; Kumagai, H.; Esaki, N.; Soda, K.
Properties of aspartate racemase, a pyridoxal 5'-phosphate-independent amino acid racemase
J. Biol. Chem.
267
18361-18364
1992
Streptococcus thermophilus
brenda
Okada, H.; Yohda, M.; Giga-Hama, Y.; Ueno, Y.; Ohdo, S.; Kumagai, H.
Distribution and purification of asparate racemase in lactic acid bacteria
Biochim. Biophys. Acta
1078
377-382
1991
Enterococcus faecalis, Enterococcus faecium, Levilactobacillus brevis, Lactobacillus delbrueckii subsp. bulgaricus, Lacticaseibacillus casei, Lactobacillus delbrueckii, Lactococcus lactis, no activity in Bifidobacterium bifidum, no activity in Leuconostoc mesenteroides, no activity in Pediococcus pentosaceus, Streptococcus thermophilus
brenda
Soda, K.
PLP-dependent and independent amino acid racemase
Enzymes Depend. Pyridoxal Phosphate Other Carbonyl Comp. Cofactors (Proc. Int. Symp. Vitam. B6 Carbonyl Catal. , Meeting Date 1990, Fukui T. , ed. ) Pergamon, Oxford
8
29-34
1991
Enterococcus faecalis, Streptococcus thermophilus
-
brenda
Yohda, M.; Endo, I.; Abe, Y.; Ohta, T.; Iida, T.; Maruyama, T.; Kagawa, Y.
Gene for aspartate racemase from the sulfur-dependent hyperthermophilic archaeum, Desulfurococcus strain SY
J. Biol. Chem.
271
22017-22021
1996
Desulfurococcus sp., Desulfurococcus sp. SY
brenda
Yohda, M.; Okada, H.; Kumagai, H.
Molecular cloning and nucleotide sequencing of the aspartate racemase gene from lactic acid bacteria Streptococcus thermophilus
Biochim. Biophys. Acta
1089
234-240
1991
Streptococcus thermophilus
brenda
Ohtani, S.
Estimation of age from dentin by using the racemization reaction of aspartic acid
Am. J. Forensic Med. Pathol.
16
158-161
1995
Bacteria
brenda
Liu, L.; Iwata, K.; Kawarabayasi, Y.; Kikuchi, H.; Kita, A.; Yohda, M.; Miki, K.
Crystallization and preliminary X-ray analysis of aspartate racemase from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. D
57
1674-1676
2001
Pyrococcus horikoshii OT3
brenda
Sielaff, H.; Dittmann, E.; Tandeau De Marsac, N.; Bouchier, C.; Von Dohren, H.; Borner, T.; Schwecke, T.
The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase
Biochem. J.
373
909-916
2003
Microcystis aeruginosa
brenda
Shibata, K.; Watanabe, T.; Yoshikawa, H.; Abe, K.; Takahashi, S.; Kera, Y.; Yamada, R.H.
Purification and characterization of aspartate racemase from the bivalve mollusk Scapharca broughtonii
Comp. Biochem. Physiol. B
134
307-314
2003
Anadara broughtonii
brenda
Shibata, K.; Watanabe, T.; Yoshikawa, H.; Abe, K.; Takahashi, S.; Kera, Y.; Yamada, R.H.
Nucleotides modulate the activity of aspartate racemase of Scapharca broughtonii
Comp. Biochem. Physiol. B
134
713-719
2003
Anadara broughtonii
brenda
Liu, L.; Iwata, K.; Kita, A.; Kawarabayasi, Y.; Yohda, M.; Miki, K.
Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization
J. Mol. Biol.
319
479-489
2002
Pyrococcus horikoshii OT3
brenda
D'Aniello, S.; Spinelli, P.; Ferrandino, G.; Peterson, K.; Tsesarskia, M.; Fisher, G.; D'Aniello, A.
Cephalopod vision involves dicarboxylic amino acids: D-aspartate, L-aspartate and L-glutamate
Biochem. J.
386
331-340
2005
Sepia officinalis
brenda
Yamashita, T.; Ashiuchi, M.; Ohnishi, K.; Kato, S.; Nagata, S.; Misono, H.
Molecular identification of monomeric aspartate racemase from Bifidobacterium bifidum
Eur. J. Biochem.
271
4798-4803
2004
Bifidobacterium bifidum, Bifidobacterium bifidum NBRC 14252
brenda
Raucci, F.; Santillo, A.; D'Aniello, A.; Chieffi, P.; Baccari, G.C.
D-Aspartate modulates transcriptional activity in Harderian gland of frog, Rana esculenta: Morphological and molecular evidence
J. Cell. Physiol.
204
445-454
2005
Pelophylax lessonae
brenda
Spinelli, P.; Brown, E.R.; Ferrandino, G.; Branno, M.; Montarolo, P.G.; D'Aniello, E.; Rastogi, R.K.; D'Aniello, B.; Baccari, G.C.; Fisher, G.; D'Aniello, A.
D-aspartic acid in the nervous system of Aplysia limacina: Possible role in neurotransmission
J. Cell. Physiol.
206
672-681
2006
Aplysia limacina
brenda
Abe, K.; Takahashi, S.; Muroki, Y.; Kera, Y.; Yamada, R.
Cloning and expression of the pyridoxal 5-phosphate-dependent aspartate racemase gene from the bivalve mollusk Scapharca broughtonii and characterization of the recombinant enzyme
J. Biochem.
139
235-244
2006
Anadara broughtonii
brenda
Ohtaki, A.; Nakano, Y.; Iizuka, R.; Arakawa, T.; Yamada, K.; Odaka, M.; Yohda, M.
Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism
Proteins Struct. Funct. Bioinform.
70
1167-1174
2008
Pyrococcus horikoshii (O58403), Pyrococcus horikoshii OT-3 (O58403)
brenda
Kim, P.M.; Duan, X.; Huang, A.S.; Liu, C.Y.; Ming, G.L.; Song, H.; Snyder, S.H.
Aspartate racemase, generating neuronal D-aspartate, regulates adult neurogenesis
Proc. Natl. Acad. Sci. USA
107
3175-3179
2010
Mus musculus
brenda
Topo, E.; Soricelli, A.; DAniello, A.; Ronsini, S.; DAniello, G.
The role and molecular mechanism of D-aspartic acid in the release and synthesis of LH and testosterone in humans and rats
Reprod. Biol. Endocrinol.
7
120-130
2009
Rattus norvegicus
brenda
Zhang, C.; Guo, Y.; Xue, Y.
QM/MM study on catalytic mechanism of aspartate racemase from Pyrococcus horikoshii OT3
Theoret. Chem. Accounts
129
781-791
2011
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
-
brenda
Long, Z.; Lee, J.A.; Okamoto, T.; Sekine, M.; Nimura, N.; Imai, K.; Yohda, M.; Maruyama, T.; Sumi, M.; Kamo, N.; Yamagishi, A.; Oshima, T.; Homma, H.
Occurrence of D-amino acids and a pyridoxal 5'-phosphate-dependent aspartate racemase in the acidothermophilic archaeon, Thermoplasma acidophilum
Biochem. Biophys. Res. Commun.
281
317-321
2001
Thermoplasma acidophilum, Thermoplasma acidophilum HO-62
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D-Amino acid metabolism in mammals: biosynthesis, degradation and analytical aspects of the metabolic study
J. Chromatogr. B
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3162-3168
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Mus musculus, Rattus norvegicus
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Fujii, T.; Yamauchi, T.; Ishiyama, M.; Gogami, Y.; Oikawa, T.; Hata, Y.
Crystallographic studies of aspartate racemase from Lactobacillus sakei NBRC 15893
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1012-1016
2015
Latilactobacillus sakei, Latilactobacillus sakei NBRC 15893
brenda
Mizobuchi, T.; Nonaka, R.; Yoshimura, M.; Abe, K.; Takahashi, S.; Kera, Y.; Goto, M.
Crystal structure of a pyridoxal 5'-phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca broughtonii
Acta Crystallogr. Sect. F
73
651-656
2017
Anadara broughtonii
brenda
Tanaka-Hayashi, A.; Hayashi, S.; Inoue, R.; Ito, T.; Konno, K.; Yoshida, T.; Watanabe, M.; Yoshimura, T.; Mori, H.
Is D-aspartate produced by glutamic-oxaloacetic transaminase-1 like 1 (Got1l1) a putative aspartate racemase?
Amino Acids
47
79-86
2015
Mus musculus (Q7TSV6), Mus musculus
brenda
Matsuda, S.; Katane, M.; Maeda, K.; Kaneko, Y.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.
Biosynthesis of D-aspartate in mammals the rat and human homologs of mouse aspartate racemase are not responsible for the biosynthesis of D-aspartate
Amino Acids
47
975-985
2015
Homo sapiens, Rattus norvegicus
brenda
Uda, K.; Abe, K.; Dehara, Y.; Mizobata, K.; Edashige, Y.; Nishimura, R.; Radkov, A.D.; Moe, L.A.
Triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family
Amino Acids
49
1743-1754
2017
Penaeus monodon (A0A0U5A554), Acropora millepora (JT020910), Crassostrea gigas (K1QH67)
brenda
Aihara, T.; Ito, T.; Yamanaka, Y.; Noguchi, K.; Odaka, M.; Sekine, M.; Homma, H.; Yohda, M.
Structural and functional characterization of aspartate racemase from the acidothermophilic archaeon Picrophilus torridus
Extremophiles
20
385-393
2016
Picrophilus torridus (Q6L2R8), Picrophilus torridus, Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 (Q6L2R8)
brenda
Washio, T.; Kato, S.; Oikawa, T.
Molecular cloning and enzymological characterization of pyridoxal 5'-phosphate independent aspartate racemase from hyperthermophilic archaeon Thermococcus litoralis DSM 5473
Extremophiles
20
711-721
2016
Thermococcus litoralis (H3ZNI2), Thermococcus litoralis, Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C (H3ZNI2)
brenda
Katane, M.; Nakayama, K.; Kawata, T.; Yokoyama, Y.; Matsui, Y.; Kaneko, Y.; Matsuda, S.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.
A sensitive assay for measuring aspartate-specific amino acid racemase activity
J. Pharm. Biomed. Anal.
116
109-115
2015
Streptococcus thermophilus
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