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Information on EC 5.1.1.13 - aspartate racemase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58403

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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.
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This record set is specific for:
Pyrococcus horikoshii
UNIPROT: O58403
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
aspartate racemase, asp racemase, got1l1, d-aspartate racemase, phaspr, sbaspr, pyridoxal 5'-phosphate-independent aspartate racemase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aspartate racemase
-
-
-
-
D-Aspartate racemase
-
-
-
-
Racemase, aspartate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate = D-aspartate
show the reaction diagram
one-base mechanism, residue C194 plays the role of the base for not only L-aspartate but also D-aspartate
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
aspartate racemase
Also acts, at half the rate, on L-alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
37237-56-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate
D-aspartate
show the reaction diagram
-
-
-
?
D-aspartate
L-aspartate
show the reaction diagram
-
-
-
-
r
L-aspartate
D-aspartate
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
pyridoxal 5'-phosphate-independent
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Citric acid
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
L-aspartate
pH 8.0, 70°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.4
Citric acid
pH 8.0, 70°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain OT3
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C82A
catalytically inactive. Crystallization data in complex with citric acid
C82A
-
inactive
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team