EC number:5.1.1.13

Enzyme

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EC Tree
     5. Isomerases
        5.1 Racemases and epimerases
            5.1.1 Acting on amino acids and derivatives
ID:5.1.1.13
Description:Aspartate racemase.
Prosite: PDOC00714;
PDB:
PDBScop
Cath: 3.40.50.1860;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 5.1.1.13
BRENDA Enzyme Link: BRENDA 5.1.1.13
KEGG Enzyme Link: KEGG5.1.1.13
BioCyc Enzyme Link: BioCyc 5.1.1.13
ExPASy Enzyme Link: ExPASy5.1.1.13
EC2PDB Enzyme Link: EC2PDB 5.1.1.13
ExplorEnz Enzyme Link: ExplorEnz 5.1.1.13
PRIAM enzyme-specific profiles Link: PRIAM 5.1.1.13
IntEnz Enzyme Link: IntEnz 5.1.1.13
MEDLINE Enzyme Link: MEDLINE 5.1.1.13

EC number:5.1.1.13

MSA:

5.1.1.13;
Phylogenetic Tree:

5.1.1.13;
Uniprot:
M-CSA:
RHEA:14973 L-aspartate = D-aspartate
RULE(radius=1)
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular identification of monomeric aspartate racemase from Bifidobacterium bifidum.Yamashita T, Ashiuchi M, Ohnishi K, Kato S, Nagata S, Misono H2004 Dec15606767
The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase.Sielaff H, Dittmann E, Tandeau De Marsac N, Bouchier C, Von Döhren H, Börner T, Schwecke T2003 Aug 112713441
Purification and characterization of aspartate racemase from the bivalve mollusk Scapharca broughtonii.Shibata K, Watanabe T, Yoshikawa H, Abe K, Takahashi S, Kera Y, Yamada RH2003 Feb12568809
Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization.Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K2002 May 3112051922