5.1.1.13: aspartate racemase
This is an abbreviated version!
For detailed information about aspartate racemase, go to the full flat file.
Word Map on EC 5.1.1.13
-
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
- 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
Reaction
Synonyms
Asp racemase, Aspartate racemase, AspR, D-Asp racemase, D-Aspartate racemase, GOT1L1, LsAspR, OCC_11152, P. AspR, PhAspR, PLP-independent AspR, PTO0149, PtoAspR, pyridoxal 5'-phosphate independent aspartate racemase, pyridoxal 5'-phosphate-independent aspartate racemase, Racemase, aspartate, SbAspR, Tl-AspR
ECTree
Advanced search results
Substrates Products
Substrates Products on EC 5.1.1.13 - aspartate racemase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
D-aspartate
L-aspartate
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
-
-
r
D-aspartate
L-aspartate
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
D-Asp is the preferred substrate
-
-
r
L-Asp
D-Asp
-
enzyme exclusively acts on L-Asp and D-Asp
-
-
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
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
-
-
r
L-aspartate
D-aspartate
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction
-
-
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
56.4% of the activity in the reverse reaction direction
-
-
r
L-aspartate
D-aspartate
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
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
-
at 88% of the activity relative to L-Asp
-
?
L-Cysteine sulfinate
D-Cysteine sulfinate
-
at 51% of the activity relative to L-Asp
-
?
?
-
-
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
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 ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
Picrophilus torridus aspartate racemase is highly specific to aspartate
-
-
?
additional information
?
-
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested
-
-
?
additional information
?
-
-
the glutamic-oxaloacetic transaminase 1-like 1, UniProt ID A0A0U1RVK4, exhibits low aspartate racemase activity in contrast to the murine enzyme GOT1L1
-
-
?
additional information
?
-
-
no racemase activity with Asp, Cys, Pro, and hydroxyproline
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
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
-
-
?