EzCatDB: S00810
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DB codeS00810
RLCP classification4.12.642300.465 : Addition
5.201.1660000.464 : Elimination
CATH domainDomain 13.40.140.10 : Cytidine Deaminase; domain 2Catalytic domain
E.C.3.5.4.3

CATH domainRelated DB codes (homologues)
3.40.140.10 : Cytidine Deaminase; domain 2S00808,D00406

Enzyme Name
UniProtKBKEGG

O34598
Protein nameGuanine deaminaseGuanine deaminase
Guanase
Guanine aminase
GAH
SynonymsGDEase
Guanase
Guanine aminase
EC 3.5.4.3
Guanine aminohydrolase
GAH
RefSeqNP_389200.1 (Protein)
NC_000964.3 (DNA/RNA sequence)
PfamPF00383 (dCMP_cyt_deam_1)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism

UniProtKB:Accession NumberO34598
Entry nameGUAD_BACSU
ActivityGuanine + H(2)O = xanthine + NH(3).
Subunit
Subcellular location
CofactorZinc (By similarity).

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00038C00242C00001C00385C00014I00149
CompoundZincguanineH2OxanthineNH32-hydroxy-guanine
Typeheavy metalamide group,amine group,aromatic ring (with nitrogen atoms)H2Oamide group,aromatic ring (with nitrogen atoms)amine group,organic ion
ChEBI29105
16235
15377
17712
48517
16134

PubChem32051
764
962
22247451
1188
222

              
1tiyA00Bound:_ZNUnbound UnboundUnboundUnbound
1tiyB00Bound:_ZNUnbound UnboundUnboundUnbound
1wkqA00Bound:_ZNUnbound UnboundUnboundUnbound
1wkqB00Bound:_ZNUnbound UnboundUnboundUnbound

Active-site residues
resource
PDB;1wkq & literature[5]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1tiyA00GLU 55
HIS 53;CYS 83;CYS 86
GLU 81
1tiyB00GLU 55
HIS 53;CYS 83;CYS 86
GLU 81
1wkqA00GLU 55
HIS 53;CYS 83;CYS 86
GLU 81
1wkqB00GLU 55
HIS 53;CYS 83;CYS 86
GLU 81

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Scheme 1, p.35481-35483
[5]Fig. 4, Fig. 6, p. 4200, p. 4203-4209

references
[1]
PubMed ID8289286
JournalJ Mol Biol
Year1994
Volume235
Pages635-56
AuthorsBetts L, Xiang S, Short SA, Wolfenden R, Carter CW Jr
TitleCytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex.
[2]
PubMed ID11101664
JournalMicrobiology
Year2000
Volume146 Pt 12
Pages3061-9
AuthorsNygaard P, Bested SM, Andersen KA, Saxild HH
TitleBacillus subtilis guanine deaminase is encoded by the yknA gene and is induced during growth with purines as the nitrogen source.
Related UniProtKBO34598
[3]
PubMed ID12637534
JournalJ Biol Chem
Year2003
Volume278
Pages19111-7
AuthorsKo TP, Lin JJ, Hu CY, Hsu YH, Wang AH, Liaw SH
TitleCrystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
PubMed ID15180998
JournalJ Biol Chem
Year2004
Volume279
Pages35479-85
AuthorsLiaw SH, Chang YJ, Lai CT, Chang HC, Chang GG
TitleCrystal structure of Bacillus subtilis guanine deaminase: the first domain-swapped structure in the cytidine deaminase superfamily.
Related PDB1wkq
Related UniProtKBO34598
[5]
PubMed ID17394305
JournalJ Phys Chem B
Year2007
Volume111
Pages4200-10
AuthorsYao L, Cukier RI, Yan H
TitleCatalytic mechanism of guanine deaminase: an ONIOM and molecular dynamics study.
[6]
PubMed ID17803218
JournalProteins
Year2008
Volume70
Pages873-81
AuthorsFernandez JR, Welsh WJ, Firestein BL
TitleStructural characterization of the zinc binding domain in cytosolic PSD-95 interactor (cypin): Role of zinc binding in guanine deamination and dendrite branching.

comments
This enzyme is homologous to cytidine deaminase (EC 3.5.4.5; D00406 in EzCatDB) and deoxycytidylate deaminase (EC 3.5.4.12; S00808 in EzCatDB), sharing a similar active site with them.
According to the literature [4], this enzyme seems to have a similar reaction mechanism to those by the homolgous enzymes. This enzyme catalyzes two successive reactions (rather than hydrolysis) as follows:

createdupdated
2008-07-042012-10-16


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