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Information on EC 5.1.1.13 - aspartate racemase
for references in articles please use BRENDA:EC5.1.1.13
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EC Tree 5 Isomerases
5.1 Racemases and epimerases
5.1.1 Acting on amino acids and derivatives
5.1.1.13 aspartate racemase
IUBMB Comments
Also acts, at half the rate, on L-alanine.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 5.1.1.13
- l-aspartate
-
d-amino
-
racemization
- asprs
-
5'-phosphate-dependent
- horikoshii
-
scapharca
- d-serine
- broughtonii
-
d-forms
-
d-enantiomer
- serrs
-
plp-dependent
- d-glutamate
-
mirror-symmetric
- food industry
- analysis
showSynonyms
aspartate racemase, asp racemase, got1l1, d-aspartate racemase, phaspr, sbaspr, pyridoxal 5'-phosphate-independent aspartate racemase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Asp racemase
Asp/GluR
Aspartate racemase
AspR
D-Aspartate racemase
GOT1L1
LsAspR
OCC_11152
PhAspR
PLP-independent AspR
PTO0149
PtoAspR
pyridoxal 5'-phosphate independent aspartate racemase
pyridoxal 5'-phosphate-independent aspartate racemase
Racemase, aspartate
-
-
-
-
Tl-AspR
Asp/GluR
-
Asp/GluR gene is the result of AspR gene duplication and several amino acid substitutions including that of the 156th serine residue with alanine
Aspartate racemase
-
-
-
-
D-Aspartate racemase
-
-
-
-
pyridoxal 5'-phosphate independent aspartate racemase
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
-
pyridoxal 5'-phosphate-independent aspartate racemase
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate = D-aspartate
removal of alpha-hydrogen of the substrate is at least partially rate-determining
-
L-aspartate = D-aspartate
the enzyme racemizes only aspartate and no other amino acids but the enzyme also shows a dehydratase activity toward L-threo-3-hydroxyaspartate
-
L-aspartate = D-aspartate
one-base mechanism, residue C194 plays the role of the base for not only L-aspartate but also D-aspartate
L-aspartate = D-aspartate
one-base mechanism, residue C194 plays the role of the base for not only L-aspartate but also D-aspartate
-
-
L-aspartate = D-aspartate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
aspartate racemase
Also acts, at half the rate, on L-alanine.
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CAS REGISTRY NUMBER
COMMENTARY
37237-56-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-aspartate
L-aspartate
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: -
Products: -
Products: -
r
D-aspartate
L-aspartate
-
Substrates: bifunctional enzyme Asp/GluR shows comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate, cf. EC 5.1.1.3. AspR shows very low glutamate racemase activity
Products: -
Products: -
r
D-aspartate
L-aspartate
-
Substrates: the bifunctional enzyme Asp/GluR shows comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate, cf. EC 5.1.1.3. AspR shows very low glutamate racemase activity
Products: -
Products: -
r
D-aspartate
L-aspartate
-
Substrates: comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate
Products: -
Products: -
r
D-aspartate
L-aspartate
Substrates: D-Asp is the preferred substrate
Products: -
Products: -
r
D-aspartate
L-aspartate
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
Substrates: D-Asp is the preferred substrate
Products: -
Products: -
r
D-glutamate
L-glutamate
-
Substrates: comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate
Products: -
Products: -
r
L-Asp
D-Asp
-
Substrates: enzyme exclusively acts on L-Asp and D-Asp
Products: -
Products: -
r
L-Asp
D-Asp
-
Substrates: enzyme exclusively acts on L-Asp and D-Asp
Products: -
Products: -
r
L-Asp
D-Asp
-
Substrates: the enzyme regulates synthesis of the endogenous D-Asp
Products: -
Products: -
?
L-aspartate
D-aspartate
Substrates: the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction
Products: -
Products: -
r
L-aspartate
D-aspartate
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: -
Products: -
Products: -
r
L-aspartate
D-aspartate
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction
Products: -
Products: -
r
L-aspartate
D-aspartate
-
Substrates: cell wall synthesis
Products: -
Products: -
?
L-aspartate
D-aspartate
-
Substrates: the bifunctional enzyme Asp/GluR shows comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate, cf. EC 5.1.1.3. AspR shows very low glutamate racemase activity
Products: -
Products: -
r
L-aspartate
D-aspartate
-
Substrates: comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate
Products: -
Products: -
r
L-aspartate
D-aspartate
-
Substrates: 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
Products: -
Products: -
r
L-aspartate
D-aspartate
Substrates: 56.4% of the activity in the reverse reaction direction
Products: -
Products: -
r
L-aspartate
D-aspartate
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
Substrates: -
Products: -
Products: -
r
L-aspartate
D-aspartate
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
Substrates: 56.4% of the activity in the reverse reaction direction
Products: -
Products: -
r
L-aspartate
D-aspartate
-
Substrates: 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
Products: -
Products: -
r
L-aspartate
D-aspartate
-
Substrates: 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
Products: -
Products: -
r
L-Cysteate
D-Cysteate
-
Substrates: at 88% of the activity relative to L-Asp
Products: -
Products: -
?
L-Cysteine sulfinate
D-Cysteine sulfinate
-
Substrates: at 51% of the activity relative to L-Asp
Products: -
Products: -
?
L-Cysteine sulfinate
D-Cysteine sulfinate
-
Substrates: -
Products: -
Products: -
?
L-glutamate
D-glutamate
-
Substrates: comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate
Products: -
Products: -
r
additional information
?
-
-
Substrates: SbAspR catalyzes both racemization and dehydration. Residue Arg140 recognizes the beta-carboxyl group of the substrate aspartate in SbAspR
Products: -
Products: -
?
additional information
?
-
-
Substrates: no racemase activity with Glu
Products: -
Products: -
?
additional information
?
-
-
Substrates: the aspartate aminotransferase, UniProt ID Q8NHS2, EC 2.6.1, exhibits low aspartate racemase activity in contrast to the murine enzyme GOT1L1
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme AspR also shows negligible serine racemase, SerR (EC 5.1.1.18), activity
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme AspR also shows low serine racemase, SerR (EC 5.1.1.18), activity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is also active in the racemisation of L- and D-serine, EC 5.1.1.18
Products: -
Products: -
?
additional information
?
-
Substrates: Picrophilus torridus aspartate racemase is highly specific to aspartate
Products: -
Products: -
?
additional information
?
-
Substrates: PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested
Products: -
Products: -
?
additional information
?
-
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: Picrophilus torridus aspartate racemase is highly specific to aspartate
Products: -
Products: -
?
additional information
?
-
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glutamic-oxaloacetic transaminase 1-like 1, UniProt ID A0A0U1RVK4, exhibits low aspartate racemase activity in contrast to the murine enzyme GOT1L1
Products: -
Products: -
?
additional information
?
-
-
Substrates: no racemase activity with Asp, Cys, Pro, and hydroxyproline
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Asp
D-Asp
-
Substrates: the enzyme regulates synthesis of the endogenous D-Asp
Products: -
Products: -
?
D-aspartate
L-aspartate
-
Substrates: bifunctional enzyme Asp/GluR shows comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate, cf. EC 5.1.1.3. AspR shows very low glutamate racemase activity
Products: -
Products: -
r
L-aspartate
D-aspartate
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: -
Products: -
Products: -
r
L-aspartate
D-aspartate
-
Substrates: cell wall synthesis
Products: -
Products: -
?
L-aspartate
D-aspartate
-
Substrates: the bifunctional enzyme Asp/GluR shows comparable substrate affinity and high catalytic efficiency (kcat/Km) for both aspartate and glutamate, cf. EC 5.1.1.3. AspR shows very low glutamate racemase activity
Products: -
Products: -
r
L-aspartate
D-aspartate
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme AspR also shows low serine racemase, SerR (EC 5.1.1.18), activity
Products: -
Products: -
?
additional information
?
-
Substrates: Picrophilus torridus aspartate racemase is highly specific to aspartate
Products: -
Products: -
?
additional information
?
-
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Substrates: Picrophilus torridus aspartate racemase is highly specific to aspartate
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
this enzyme is the first aspartate racemase purified from animal tissues and unique in its pyridoxal 5'-phosphate (PLP)dependence in contrast to microbial aspartate racemases characterized so far
pyridoxal 5'-phosphate
-
dependent on. Enzyme activity is very low in the absence of pyridoxal 5'-phosphate
additional information
a pyridoxal 5'-phosphate-independent aspartate racemase. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains
-
additional information
the enzyme does not require pyridoxal 5'-phosphate as a coenzyme
-
additional information
-
the enzyme does not require pyridoxal 5'-phosphate as a coenzyme
-
additional information
pyridoxal 5'-phosphate independent amino acid racemase
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme contains no significant amount of metal
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
1 mM, complete inhibition, pH 7.0, 30°C, 30 min
hydroxylamine
-
inclusion of hydroxylamine (1.0 mM and 10 mM) in the assay results in complete loss in the activity at 45°C, and also at 70°C where higher levels of activity are observed than at 45°C
additional information
-
enzyme is not influenced by high concentrations of aspartate up to 500 mM
-
additional information
-
enzyme is not influenced by high concentrations of aspartate up to 500 mM; no inhibition by: hydroxylamine, sodium borohydride
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SH-protecting reagents
-
e.g., 2-mercaptoethanol and dithiothreitol increase activity 2fold
-
additional information
-
removal of some divalent cation by EDTA gives slight increase in activity
-
additional information
-
enzyme contains no bound pyridoxal phosphate
-
additional information
-
enzyme contains no bound pyridoxal phosphate
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Crystal structure of a pyridoxal 5'-phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca broughtonii.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.37
D-Aspartate
JT020910
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
2.97
D-Aspartate
pH 8.0, temperature not specified in the publication
4.36
D-Aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme
4.43
D-Aspartate
-
pH 8.0, temperature not specified in the publication
4.55
D-Aspartate
JT020910
recombinant His-tagged mutant P150S, pH 8.0, 30°C
5
D-Aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme
5
D-Aspartate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
6.21
D-Aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
7.49
D-Aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme
9.86
D-Aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
23.3
D-Aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme
23.3
D-Aspartate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
80.6
D-Aspartate
recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C
39.8
D-glutamate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
85
D-glutamate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
242
D-serine
pH 8.0, temperature not specified in the publication
2.23
L-aspartate
pH 8.0, temperature not specified in the publication
3.11
L-aspartate
JT020910
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
3.2
L-aspartate
JT020910
recombinant His-tagged mutant P150S, pH 8.0, 30°C
3.27
L-aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme
3.27
L-aspartate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
3.52
L-aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme
4.75
L-aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
6.37
L-aspartate
-
recombinant enzyme, pH 8.3, 37°C, coupling method assay
9.57
L-aspartate
-
pH 8.0, temperature not specified in the publication
10.4
L-aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme
14.9
L-aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
15.4
L-aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme
15.4
L-aspartate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
48.6
L-aspartate
recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C
2 - 3
L-glutamate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
101
L-glutamate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
64.2
L-serine
pH 8.0, temperature not specified in the publication
additional information
additional information
-
steady-state kinetics of all assay methods, overview
-
additional information
additional information
kinetics of enzyme AspR with L-Ser and D-Ser as substrates, comparison to the serine racemase enzyme of Penaeus monodon, EC 5.1.1.18, overview
-
additional information
additional information
kinetics of wild-type and mutant enzymes AspR with L-Ser and D-Ser as substrates, comparison to the serine racemase enzyme of Crassostrea gigas, EC 5.1.1.18, overview
-
additional information
additional information
JT020910
kinetics of wild-type and mutant enzymes AspR with L-Ser and D-Ser as substrates, comparison to the serine racemase enzyme of Acropora millepora, overview
-
additional information
additional information
the activation energy of Tl-AspR is calculated to be 51.8 kJ/mol by Arrhenius plots
-
additional information
additional information
-
the activation energy of Tl-AspR is calculated to be 51.8 kJ/mol by Arrhenius plots
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.09
D-glutamic acid
-
pH 8.0, temperature not specified in the publication
0.721
L-Glutamic acid
-
pH 8.0, temperature not specified in the publication
0.0322
D-Aspartate
recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C
2.96
D-Aspartate
-
pH 8.0, temperature not specified in the publication
7.47
D-Aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme
7.47
D-Aspartate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
7.56
D-Aspartate
pH 8.0, temperature not specified in the publication
10
D-Aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme
10
D-Aspartate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
13.1
D-Aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
17.8
D-Aspartate
JT020910
recombinant His-tagged mutant P150S, pH 8.0, 30°C
19.9
D-Aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme AS56A, AspR enzyme
25.3
D-Aspartate
JT020910
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
27.6
D-Aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
45.1
D-Aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme
11.3
D-glutamate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
15.6
D-glutamate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.175
D-serine
pH 8.0, temperature not specified in the publication
0.0228
L-aspartate
recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C
3.63
L-aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme
3.63
L-aspartate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
6.19
L-aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme
6.19
L-aspartate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
7.52
L-aspartate
-
pH 8.0, temperature not specified in the publication
7.64
L-aspartate
pH 8.0, temperature not specified in the publication
8.65
L-aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
14.5
L-aspartate
JT020910
recombinant His-tagged mutant P150S, pH 8.0, 30°C
17.9
L-aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme
33
L-aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
39.6
L-aspartate
-
recombinant enzyme, pH 8.3, 37°C, coupling method assay
41.6
L-aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme
57.7
L-aspartate
JT020910
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
6.7
L-glutamate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
18.1
L-glutamate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.0631
L-serine
pH 8.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00601
D-glutamic acid
-
pH 8.0, temperature not specified in the publication
0.00547
L-Glutamic acid
-
pH 8.0, temperature not specified in the publication
0.0004
D-Aspartate
recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C
0.321
D-Aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme
0.321
D-Aspartate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.667
D-Aspartate
-
pH 8.0, temperature not specified in the publication
2
D-Aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme
2
D-Aspartate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
2.12
D-Aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
2.57
D-Aspartate
pH 8.0, temperature not specified in the publication
2.65
D-Aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme
2.8
D-Aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
3.9
D-Aspartate
JT020910
recombinant His-tagged mutant P150S, pH 8.0, 30°C
10.4
D-Aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme
18.4
D-Aspartate
JT020910
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
0.183
D-glutamate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.284
D-glutamate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.000721
D-serine
pH 8.0, temperature not specified in the publication
0.00132
D-serine
-
pH 8.0, temperature not specified in the publication
0.0005
L-aspartate
recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C
0.236
L-aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme
0.236
L-aspartate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.79
L-aspartate
-
pH 8.0, temperature not specified in the publication
1.72
L-aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme
1.82
L-aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
1.89
L-aspartate
-
pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme
1.89
L-aspartate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
2.22
L-aspartate
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
3.43
L-aspartate
pH 8.0, temperature not specified in the publication
4.7
L-aspartate
JT020910
recombinant His-tagged mutant P150S, pH 8.0, 30°C
6.22
L-aspartate
-
recombinant enzyme, pH 8.3, 37°C, coupling method assay
11.8
L-aspartate
-
pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme
18.7
L-aspartate
JT020910
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
0.18
L-glutamate
-
mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.291
L-glutamate
-
wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
0.000986
L-serine
pH 8.0, temperature not specified in the publication
0.00186
L-serine
-
pH 8.0, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.8
-
substrate: D-aspartate, mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
1590
purified recombinant enzyme after complete purification procedure, pH 8.0, 90°C
19.5
-
crude recombinant enzyme in Escherichia coli cell extract, coupled assay method, pH 8.3, 37°C
2.4
-
substrate: L-aspartate, wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
3.25
-
substrate: L-glutamate, wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
3.7
-
substrate: D-glutamate, wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
3870
partially purified recombinant enzyme, after the first anion exchange chromatographic step, pH 8.0, 90°C
4
-
substrate: D-aspartate, wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
4.03
-
substrate: D-glutamate, mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
4.23
-
substrate: L-glutamate, mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
460
-
Vmax of recombinant enzyme, activity is assayed in 500 nl of pyrydoxal 5'-phosphate (100 nM), 0.49 ml of recombinant enzyme (0.5 mg/ml), and 0.01 mL of 1 mM L-aspartate at 37°C for 1 h in 10 mM Tris (pH 7.5)
7.65
-
substrate: L-aspartate, mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme
additional information
-
the pituitary gland is the tissue which contains the highest enzymatic activity, with 20.0 EU/mg protein, followed by: testis; brain, liver, kidney and serum, 1 enzyme unit (EU) is defined as the amount of the enzyme capable of generating 1 nmol of D-Asp in 60 min of incubation at 37°C and in the assay conditions (0.1 M Tris-HCl,10 mM EDTA, 0.1 M sodium L-aspartate)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 6.5
recombinant enzyme, the activity at pH 4.6 is approximately 6times lower than that at the optimal pH 5.5. The activity is completely lost at approximately pH 4.0, 50% of maximal actiivty at pH 6.5, profile overview
6.5 - 8.5
-
pH 6.5: 59% of maximal activity, pH 8.5: 74% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
95
the activity of Tl-AspR increases gradually and shows a maximum activity at 95°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
recombinant enzyme, about 20% of maximal activity at 30°C and 70°C, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 9790, strain IAM 10065, no activity in strain IAM 10067
-
-
brenda
isolated from a hot spring of a shallow sea in Naples, Italy
UniProt
brenda
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
isolated from a hot spring of a shallow sea in Naples, Italy
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme is purified from foot muscle of Scapharca broughtonii
brenda
-
no significant seasonal differences in racemase concentration
brenda
-
concentration of the enzyme in optic lobe is 6fold higher than in the retina
brenda
-
activity in the pyloric ceca is approximately 30-60 nmol/min per g tissue, regardless of the season in both sexes
brenda
additional information
-
high expression level, D-aspartate is abundant in the embryonic brain, but drastically decreases during postnatal development. The enzyme is located in the paraventricular and supraoptic nuclei, the cerebral cortex, the hippocampus, the dentate gyrus, the pineal gland, and the posterior pituitary gland
brenda
-
no significant seasonal differences in racemase concentration
brenda
-
seasonal change of aspartate racemase activity, activity is significantly higher in August compared with April
brenda
additional information
-
highest aspartate racemase activity is observed in tissues where D-aspartate is present at high concentrations
brenda
additional information
no expression of Got1l1 mRNA in the brain and submandibular gland, where D-aspartate is abundant
brenda
additional information
-
no expression of Got1l1 mRNA in the brain and submandibular gland, where D-aspartate is abundant
brenda
additional information
the optimal growth temperature is about 60°C
brenda
additional information
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
the optimal growth temperature is about 60°C
-
brenda
additional information
-
highest aspartate racemase activity is observed in tissues where D-aspartate is present at high concentrations
brenda
additional information
the organism is able to grow at 55-98°C in pH 4.0-8.0, optimally at 88°C and pH 6.0
brenda
additional information
-
the organism is able to grow at 55-98°C in pH 4.0-8.0, optimally at 88°C and pH 6.0
brenda
additional information
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
the organism is able to grow at 55-98°C in pH 4.0-8.0, optimally at 88°C and pH 6.0
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
plant aspartate racemase genes independently evolved from serine racemase in each ancestral lineage of plant species by gene duplication and acquisition of two serine residues at position 150 to 152
evolution
-
the animal aspartate racemase (AspR) gene has evolved from the serine racemase (SerR) gene by acquisition of three consecutive serine residues (Ser155-Ser156-Ser157) involved in the strong AspR activity, and this event has occurred independently and frequently during animal evolution. Phylogenetic analysis suggests that the Saccoglossus kowalevskii AspR gene has evolved from the SerR gene after the divergence of hemichordata and vertebrate lineages by acquisition of the three serine residues at position 155 to 157 as in the case of other animal AspR genes. The Saccoglossus kowalevskii Asp/GluR gene is the result of AspR gene duplication and several amino acid substitutions including that of the 156th serine residue with alanine
evolution
plant aspartate racemase genes independently evolved from serine racemase in each ancestral lineage of plant species by gene duplication and acquisition of two serine residues at position 150 to 152
evolution
-
plant aspartate racemase genes independently evolved from serine racemase in each ancestral lineage of plant species by gene duplication and acquisition of two serine residues at position 150 to 152
evolution
-
invertebrate animal serine racemase (SerR) and aspartate racemase (AspR) evolved from a common ancestral gene and are widely distributed. Invertebrate AspR genes arose through parallel evolution by duplication of the SerR gene followed by substitution of amino acid residues necessary for substrate recognition in multiple lineages
evolution
-
invertebrate animal serine racemase (SerR) and aspartate racemase (AspR) evolved from a common ancestral gene and are widely distributed. Invertebrate AspR genes arose through parallel evolution by duplication of the SerR gene followed by substitution of amino acid residues necessary for substrate recognition in multiple lineages
evolution
-
invertebrate animal serine racemase (SerR) and aspartate racemase (AspR) evolved from a common ancestral gene and are widely distributed. Invertebrate AspR genes arose through parallel evolution by duplication of the SerR gene followed by substitution of amino acid residues necessary for substrate recognition in multiple lineages
evolution
-
invertebrate animal serine racemase (SerR) and aspartate racemase (AspR) evolved from a common ancestral gene and are widely distributed. Invertebrate AspR genes arose through parallel evolution by duplication of the SerR gene followed by substitution of amino acid residues necessary for substrate recognition in multiple lineages
evolution
-
plant aspartate racemase genes independently evolved from serine racemase in each ancestral lineage of plant species by gene duplication and acquisition of two serine residues at position 150 to 152
evolution
-
plant aspartate racemase genes independently evolved from serine racemase in each ancestral lineage of plant species by gene duplication and acquisition of two serine residues at position 150 to 152
evolution
-
plant aspartate racemase genes independently evolved from serine racemase in each ancestral lineage of plant species by gene duplication and acquisition of two serine residues at position 150 to 152
evolution
-
the evolution of Saccoglossus kowalevskii AspR and Asp/GluR genes is thought to have occurred as follows. First Saccoglossus kowalevskii AspR gene has evolved from the ancestral SerR gene by acquisition of the triple serine loop region at its recent ancestral species, then Asp/GluR has arisen by gene duplication, which is followed by an increase of GluR activity
evolution
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
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
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
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
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
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
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus
-
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
-
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
aspartate racemase and the transporter encoded in the Shigella resistance locus pathogenicity island are important for bacterial survival in environments rich in D-aspartate
physiological function
the enzyme produces the substrate D-aspartate for the biosynthesis of microcystin in the cyanobacterium Microcystis aeruginosa PCC7806
physiological function
-
possible involvement of aspartate racemase and D-aspartate in testicular maturation in echinoderm starfish
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
Shigella flexneri 2a YSH6000
-
aspartate racemase and the transporter encoded in the Shigella resistance locus pathogenicity island are important for bacterial survival in environments rich in D-aspartate
-
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
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
amino acid analysis of cell-free extract, overview
additional information
-
amino acid analysis of cell-free extract, overview
additional information
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
amino acid analysis of cell-free extract, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). YGEA_ECOBD
Escherichia coli (strain B / BL21-DE3)
230
0
25308
Swiss-Prot
-
RACD_ENTFU
Enterococcus faecium (strain Aus0004)
243
0
27940
Swiss-Prot
other Location (Reliability: 4)
RACD_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
228
0
25158
Swiss-Prot
-
RACD_THEK8
232
0
25428
Swiss-Prot
other Location (Reliability: 5)
H3ZNI2_THELN
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
225
0
25636
TrEMBL
-
Q6L2R8_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)
232
0
25930
TrEMBL
-
AATC2_MOUSE
404
0
45458
Swiss-Prot
other Location (Reliability: 5)
Q93F34_SHIFL
229
0
25364
TrEMBL
other Location (Reliability: 1)
Q9RNB4_MICA7
Microcystis aeruginosa (strain PCC 7806)
251
0
28065
TrEMBL
-
Q2L695_ANABR
338
0
37096
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
45500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
homodimer
comparisons of Picrophilus torridus enzyme structure with the Pyrococcus aspartate racemase structure. The dimerization interface is composed of three interaction surfaces, including an inter-subunit disulfide bond and contacts through the beta-sheets and alpha-helix. The interface between two molecules (Mol-A and Mol-B) of Picrophilus torridus PtoAspR looks similar to that of Pyrococcus aspartate racemase, except that there is no cysteine disulfide bond between two molecules of PtoAspR. Each subunit is composed of two homologous domains, the N-terminal domain with residues 1-101 and 207-232, and the C-terminal domain with residues 106-206. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains
homodimer
Picrophilus oshimae ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
comparisons of Picrophilus torridus enzyme structure with the Pyrococcus aspartate racemase structure. The dimerization interface is composed of three interaction surfaces, including an inter-subunit disulfide bond and contacts through the beta-sheets and alpha-helix. The interface between two molecules (Mol-A and Mol-B) of Picrophilus torridus PtoAspR looks similar to that of Pyrococcus aspartate racemase, except that there is no cysteine disulfide bond between two molecules of PtoAspR. Each subunit is composed of two homologous domains, the N-terminal domain with residues 1-101 and 207-232, and the C-terminal domain with residues 106-206. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains
-
homodimer
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
2 * 25000-30000, recombinant enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.006 ml of 2.5 mg/ml protein in 10 mM Tris-HCl, 20 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, pH 8.8, with 0.003 ml of reservoir solution containing 27% w/v PEG 4000, 50 mM sodium acetate, pH 5.0, 200 mM ammonium acetate, and 15% v/v glycerol, and equilibration against 0.1 ml of reservoir solution, 14°C, X-ray diffraction structure determination and analysis at 1.90 A resolution
-
purified enzyme, sitting drop vapour diffusion method with microseeding, mixing of 0.002 ml of 20 mg/ml protein in 50 mM MES, pH 6.5, and 4 mM dithiothreitol, with 0.002 ml of reservoir solution containing 25% v/v PEG MME 550, and 5% v/v 2-propanol, and 0.1 M sodium acetate, pH 4.8, equilibration againat 0.1 ml reservoir solution, 20°C, single rod-shaped crystals, X-ray diffraction structure determination and analysis at 2.55 A resolution, molecular replacement calculations are carried out using the coordinates of PhAspR, PDB ID 1jfl, as a starting model
-
hanging drop vapor-diffusion method at 16°C, crystal structures of McyF in complex with citrate, L-Asp and D-Asp at 2.35 A, 2.63 A and 2.80 A, respectively
purified recombinant enzyme, vapour diffusion method, mixing of 8-12 mg/ml protein in 50 mM Tris-HCl, pH 8.0, with reservoir solution containing 20-25% w/v PEG 3400, 200 mM potassium/sodium tartrate, and 1 mM L-aspartate, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement method using the structure of aspartate racemase from Salmonella typhimurium, PDB ID 3S81, as a probe model
catalytically inactive mutant C82A in complex with citric acid, 2.0 A resolution. Citric acid binds to the catalytic site, which induces a conformational change to close the active site. Residue R48 is responsible for recognizing carboxyl groups of the substrates L-/D-aspartates and stabilizing a reaction intermediate, and L164 is responsible for stabilizing a closed state structure
sitting drop vapour diffusion method at 293 K, space group P21 with a: 65.5 A, b: 58.7 A, c: 67 A and beta 109.6°
-
sitting drop vapour diffusion method at 293 K, space groups: P21 with a: 65.5 A, b: 58.7 A, c: 67.0 A, and beta: 109.6°, P212121 with a: 68.1 A, b: 135 A and c: 151.5 A, and P3121 with a and b: 80.6 A and c: 70.3 A
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P150S
JT020910
PCR-based site-directed mutagenesis, the mutant shows reduced aspartate and serine racemase activities compared to the wild-type enzyme
S151P/S152F
JT020910
PCR-based site-directed mutagenesis, the mutant is inactive as aspartate racemase, but shows serine racemase activity, EC 5.1.1.18
S150P/S151P/S152Y
PCR-based site-directed mutagenesis, the SSS to PPY mutation of Crassostrea AspR triple serine loop region drastically decreases the specific AspR activity to below 0.04% compared to wild-type, whereas it significantly increases the specific SerR and SDH activities by 6-13fold. The large change in the AspR activity in the mutant enzyme is caused by approximately 400fold decrease in kcat rather than by 22-32fold decrease in Km
C195S
kcat/Km for L-aspartate is about 70fold lower than the wild-type value
E197Q
little racemization activity towards either L-aspartate or D-aspartate
K136W
-
the importance of lysine-136, the presumed proton donor, is highlighted by its mutation to tryptophan, which virtually abolishes racemase activity
C82A
A156S
-
the Asp/GluR mutant enzyme shows 1.3-2.7fold increase in kcat values for both aspartate racemase and glutamate racemase activity compared with wild-type. The A156S mutant Asp/GluR shows approximately 10fold higher catalytic efficiency for L- and D-aspartate as compared with L- and D-glutamate
S156A
-
the AspR mutant enzyme shows 1.7-3fold increase in Km value and 2.3fold decrease in kcat value for L- and D-aspartate
C194A
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
site-directed mutagenesis, inactive mutant
-
C83A
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
site-directed mutagenesis, inactive mutant
-
C83A/C194A
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
-
site-directed mutagenesis, inactive mutant
-
additional information
C82A
catalytically inactive. Crystallization data in complex with citric acid
C82A
-
catalytically inactive. Crystallization data in complex with citric acid
-
additional information
JT020910
substituting the triple serine loop region in AspRs enhances serine racemization
additional information
-
the cDNA included an open reading frame of 1017 bp encoding a protein of 338 amino acids, and the deduced amino acid sequence contains a pyridoxal 5'-phosphate-binding motif
additional information
substituting the triple serine loop region in AspRs enhances serine racemization
additional information
generation of Got1l1 knockout mice. Got1l1 mRNA is highly expressed in the testis in wild-type mice, but is not detected in Got1l1 knockout mice. The D-aspartate contents of knockout and Got1l1 knockout mice are not significantly different in the testis and hippocampus
additional information
-
generation of Got1l1 knockout mice. Got1l1 mRNA is highly expressed in the testis in wild-type mice, but is not detected in Got1l1 knockout mice. The D-aspartate contents of knockout and Got1l1 knockout mice are not significantly different in the testis and hippocampus
additional information
substituting the triple serine loop region in AspRs enhances serine racemization
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
purified enzyme, min. 50% activity remaining within this range
6 - 9
-
thermal stability shows a bimodal dependence on pH, with minimum stability at pH 7.5, and remarkably stability at pH 6 and pH 8-9. 10 min, pH 8, 66% loss of activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
thermal stability shows a bimodal dependence on pH, with minimum stability at pH 7.5, and remarkably stability at pH 6 and pH 8-9. 10 min, pH 8, 66% loss of activity
30
-
30 min, stable up to 30°C in 0.1 M Tes buffer, pH 6.5 containing 4 mM dithiothreitol and 1 mM EDTA
37
90
purified enzyme, approximately 50% of initial activity remains after incubation for 11 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aspartate racemase is purified from the Scapharca broughtonii foot muscle by a procedure that includes sodium sulfate fractionation and blue sepharose column chromatography. The purified enzyme (225 mg) is digested at 25°C for 12 h with 80 mg of lysyl endopeptidase in a reaction mixture comprising 50 mM Tris-HCl, pH 8.0, containing 2 M guanidine hydrochloride, and the resulting peptides is resolved by reverse phase high performance liquid chromatography on a capcell Pac C-8 column (0.2 mm x 15 cm) using an acetonitrile gradient in 0.06% trifluoroacetic acid
-
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and desalting gel filtration
-
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
recombinant C-terminally His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, hydrophobic interaction chromatography, dialysis anion change chromatography, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
-
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21 and HEK-293T cells by nickel affinity chromatography and desalting gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain Rosetta (DE3) by heat treatment of cell-free extract at 70°C for 30 min, centrifugation, dialysis, and anion exchange chromatography, dialysis, hydrophobic interaction chromatography, and another different anion exchange chromatography, followed by dialysis
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
JT020910
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is cloned into pET vector, which is transformed into BL21 Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
gene Got1l1, real-time PCR expression analysis, relationships between the D-Asp content and expression levels of Got1l1 and Ddo mRNAs in cultured rat cells
-
gene Got1l1, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21 and in HEK-293T cells
gene OCC_11152, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta (DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
-
sequence comparisons and phylogenetic tree of serine and aspartate racemases, recombinant expression of C-terminally His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
the coding sequence of McyF is amplified from the genomic DNA of Microcystis aeruginosa PCC 7806, cloned into a pET-28a-derived expression vector with an N-terminal 6 x His tag and overexpressed in Escherichia coli strain BL21 (DE3)
recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
JT020910
recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
seasonal change of aspartate racemase activity, activity is significantly higher in August compared with April
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
food industry
-
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
food industry
-
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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adams, E.
Amino acid racemases and epimerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
479-507
1972
Pseudomonas sp., Limosilactobacillus fermentum
-
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
no activity in Leuconostoc mesenteroides, no activity in Pediococcus pentosaceus, no activity in Bifidobacterium bifidum, Enterococcus faecalis, Streptococcus thermophilus, Enterococcus faecium, Lactococcus lactis, Levilactobacillus brevis, Lactobacillus delbrueckii subsp. bulgaricus, Lacticaseibacillus casei, Lactobacillus delbrueckii
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
brenda
Ohide, H.; Miyoshi, Y.; Maruyama, R.; Hamase, K.; Konno, R.
D-Amino acid metabolism in mammals: biosynthesis, degradation and analytical aspects of the metabolic study
J. Chromatogr. B
879
3162-3168
2011
Rattus norvegicus, Mus musculus
brenda
Fujii, T.; Yamauchi, T.; Ishiyama, M.; Gogami, Y.; Oikawa, T.; Hata, Y.
Crystallographic studies of aspartate racemase from Lactobacillus sakei NBRC 15893
Acta Crystallogr. Sect. F
71
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), Magallana gigas (K1QH67), Acropora millepora (JT020910)
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 oshimae (Q6L2R8), Picrophilus oshimae 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
brenda
Cao, D.D.; Zhang, C.P.; Zhou, K.; Jiang, Y.L.; Tan, X.F.; Xie, J.; Ren, Y.M.; Chen, Y.; Zhou, C.Z.; Hou, W.T.
Structural insights into the catalysis and substrate specificity of cyanobacterial aspartate racemase McyF
Biochem. Biophys. Res. Commun.
514
1108-1114
2019
Microcystis aeruginosa (Q9RNB4)
brenda
Shibata, K.; Sugaya, N.; Kuboki, Y.; Matsuda, H.; Abe, K.; Takahashi, S.; Kera, Y.
Aspartate racemase and D-aspartate in starfish; possible involvement in testicular maturation
Biosci. Biotechnol. Biochem.
84
95-102
2020
Patiria pectinifera
brenda
Uda, K.; Ishizuka, N.; Edashige, Y.; Kikuchi, A.; Radkov, A.D.; Moe, L.A.
Cloning and characterization of a novel aspartate/glutamate racemase from the acorn worm Saccoglossus kowalevskii
Comp. Biochem. Physiol. B
232
87-92
2019
Saccoglossus kowalevskii
brenda
Uda, K.; Moe, L.
Distribution and evolution of the serine/aspartate racemase family in invertebrates. II. Frequent and widespread parallel evolution of aspartate racemase
J. Biochem.
172
303-311
2022
Aplysia californica, Macrostomum lignano, Anneissia japonica, Anadara broughtonii
brenda
Uda, K.; Edashige, Y.; Nishimura, R.; Shikano, Y.; Matsui, T.; Radkov, A.D.; Moe, L.A.
Distribution and evolution of the serine/aspartate racemase family in plants
Phytochemistry
169
112164
2020
Solanum lycopersicum (A0A3Q7FTJ5), Manihot esculenta, Sphagnum girgensohnii, Spirogyra pratensis, Medicago truncatula, Arabidopsis thaliana
brenda
Henriquez, T.; Salazar, J.C.; Marvasi, M.; Shah, A.; Corsini, G.; Toro, C.S.
SRL pathogenicity island contributes to the metabolismof D-aspartate via an aspartate racemase in Shigella flexneri YSH6000
PLoS ONE
15
e0228178
2020
Shigella flexneri 2a (Q93F34), Shigella flexneri 2a YSH6000 (Q93F34)
brenda
EXTERNAL LINKS (specific for EC-Number 5.1.1.13)
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