EzCatDB: D00272
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DB codeD00272
CATH domainDomain 13.40.50.1860 : Rossmann foldCatalytic domain
Domain 23.40.50.1860 : Rossmann foldCatalytic domain
E.C.5.1.1.3
CSA1b73
MACiEM0001


Enzyme Name
UniProtKBKEGG

P56868
Protein nameGlutamate racemaseglutamate racemase
SynonymsEC 5.1.1.3
PfamPF01177 (Asp_Glu_race)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00251Glutamate metabolism
MAP00471D-Glutamine and D-glutamate metabolism

UniProtKB:Accession NumberP56868
Entry nameMURI_AQUPY
ActivityL-glutamate = D-glutamate.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00025C00217
CompoundL-GlutamateD-Glutamate
Typeamino acids,carboxyl groupamino acids,carboxyl group
ChEBI16015
15966
PubChem88747398
44272391
33032
23327
          
1b73A01UnboundUnbound
1b74A01UnboundAnalogue:DGN
1b73A02UnboundUnbound
1b74A02UnboundUnbound

Active-site residues
resource
literature [5] & [6]
pdbCatalytic residues
         
1b73A01ASP 7;CYS 70  
1b74A01ASP 7;CYS 70  
1b73A02GLU 147;CYS 178
1b74A02GLU 147;CYS 178

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
PubMed ID1358877
JournalJ Biochem (Tokyo)
Year1992
Volume112
Pages139-42
AuthorsChoi SY, Esaki N, Yoshimura T, Soda K
TitleReaction mechanism of glutamate racemase, a pyridoxal phosphate-independent amino acid racemase.
[2]
PubMed ID8097109
JournalBiochemistry
Year1993
Volume32
Pages3991-7
AuthorsGallo KA, Tanner ME, Knowles JR
TitleMechanism of the reaction catalyzed by glutamate racemase.
[3]
PubMed ID8097110
JournalBiochemistry
Year1993
Volume32
Pages3998-4006
AuthorsTanner ME, Gallo KA, Knowles JR
TitleIsotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase.
[4]
PubMed ID10194325
JournalBiochemistry
Year1999
Volume38
Pages4106-13
AuthorsGlavas S, Tanner ME
TitleCatalytic acid/base residues of glutamate racemase.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID99260734
PubMed ID10331867
JournalNat Struct Biol
Year1999
Volume6
Pages422-6
AuthorsHwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y
TitleStructure and mechanism of glutamate racemase from Aquifex pyrophilus.
Related PDB1b73,1b74
Related UniProtKBP56868
[6]
PubMed ID11371180
JournalBiochemistry
Year2001
Volume40
Pages6199-204
AuthorsGlavas S, Tanner ME
TitleActive site residues of glutamate racemase.
[7]
PubMed ID11955052
JournalAcc Chem Res
Year2002
Volume35
Pages237-46
AuthorsTanner ME
TitleUnderstanding nature's strategies for enzyme-catalyzed racemization and epimerization.
[8]
PubMed ID12238935
JournalJ Med Chem
Year2002
Volume45
Pages4559-70
Authorsde 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
Title4-Substituted D-glutamic acid analogues: the first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity.
[9]
PubMed ID15274623
JournalBiochemistry
Year2004
Volume43
Pages9685-94
AuthorsMobitz H, Bruice TC
TitleMultiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: a molecular dynamics study.

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.

createdupdated
2005-04-112009-02-26


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