DB code: D00272

CATH domain 3.40.50.1860 : Rossmann fold Catalytic domain
3.40.50.1860 : Rossmann fold Catalytic domain
E.C. 5.1.1.3
CSA 1b73
M-CSA 1b73
MACiE M0001

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P56868 Glutamate racemase
EC 5.1.1.3
PF01177 (Asp_Glu_race)
[Graphical View]

KEGG enzyme name
glutamate racemase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P56868 MURI_AQUPY L-glutamate = D-glutamate. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00251 Glutamate metabolism
MAP00471 D-Glutamine and D-glutamate metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00025 C00217
E.C.
Compound L-Glutamate D-Glutamate
Type amino acids,carboxyl group amino acids,carboxyl group
ChEBI 16015
15966
PubChem 33032
44272391
88747398
23327
1b73A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1b74A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:DGN
1b73A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1b74A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [5] & [6]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b73A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 7;CYS 70
1b74A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 7;CYS 70
1b73A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 147;CYS 178
1b74A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 147;CYS 178

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
[2]
Fig.2
[3]
p.4005
[4]
Fig.1, p.4110-4112
[5]
Fig.3, p.425
[6]
Fig.1, Fig.4, p.6202-6204
[7]
Fig.7, p.239
[9]
Scheme 1, Fig.7

References
[1]
Resource
Comments
Medline ID
PubMed ID 1358877
Journal J Biochem (Tokyo)
Year 1992
Volume 112
Pages 139-42
Authors Choi SY, Esaki N, Yoshimura T, Soda K
Title Reaction mechanism of glutamate racemase, a pyridoxal phosphate-independent amino acid racemase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8097109
Journal Biochemistry
Year 1993
Volume 32
Pages 3991-7
Authors Gallo KA, Tanner ME, Knowles JR
Title Mechanism of the reaction catalyzed by glutamate racemase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8097110
Journal Biochemistry
Year 1993
Volume 32
Pages 3998-4006
Authors Tanner ME, Gallo KA, Knowles JR
Title Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10194325
Journal Biochemistry
Year 1999
Volume 38
Pages 4106-13
Authors Glavas S, Tanner ME
Title Catalytic acid/base residues of glutamate racemase.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 99260734
PubMed ID 10331867
Journal Nat Struct Biol
Year 1999
Volume 6
Pages 422-6
Authors Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y
Title Structure and mechanism of glutamate racemase from Aquifex pyrophilus.
Related PDB 1b73 1b74
Related UniProtKB P56868
[6]
Resource
Comments
Medline ID
PubMed ID 11371180
Journal Biochemistry
Year 2001
Volume 40
Pages 6199-204
Authors Glavas S, Tanner ME
Title Active site residues of glutamate racemase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11955052
Journal Acc Chem Res
Year 2002
Volume 35
Pages 237-46
Authors Tanner ME
Title Understanding nature's strategies for enzyme-catalyzed racemization and epimerization.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12238935
Journal J Med Chem
Year 2002
Volume 45
Pages 4559-70
Authors de Dios A, Prieto L, Martin JA, Rubio A, Ezquerra J, Tebbe M, Lopez de Uralde B, Martin J, Sanchez A, LeTourneau DL, McGee JE, Boylan C, Parr TR Jr, Smith MC
Title 4-Substituted D-glutamic acid analogues: the first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 15274623
Journal Biochemistry
Year 2004
Volume 43
Pages 9685-94
Authors Mobitz H, Bruice TC
Title Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: a molecular dynamics study.
Related PDB
Related UniProtKB

Comments
Although many racemase enzymes adopts pyridoxal phosphate (PLP) as cofactor, this enzyme does not utilize such cofactor in the catalytic reaction.
According to the literature [5] & [6], the racemization occurs by two consecutive reactions (shift of double-bond; Isomeriation), forming a carbanionic intermediate.

Created Updated
2005-04-11 2009-02-26