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
Subunits
Subunits 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.
dimer
homodimer
monomer
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 torridus 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
-