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 16015	15966 15966
PubChem						33032 44272391 88747398 33032 44272391 88747398	23327 23327
1b73A01						Unbound	Unbound
1b74A01						Unbound	Analogue:DGN
1b73A02						Unbound	Unbound
1b74A02						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						ASP 7;CYS 70
1b74A01						ASP 7;CYS 70
1b73A02						GLU 147;CYS 178
1b74A02						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