EzCatDB: S00544
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DB codeS00544
CATH domainDomain 13.40.50.1820 : Rossmann foldCatalytic domain
E.C.1.11.1.-
CSA1a8q

CATH domainRelated DB codes (homologues)
3.40.50.1820 : Rossmann foldS00344,S00517,S00525,S00526,S00720,S00723,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
UniProtKB

P33912P29715
Protein nameNon-haem bromoperoxidase BPO-A1Non-haem bromoperoxidase BPO-A2
SynonymsEC 1.11.1.-
Bromide peroxidase
BPO1
EC 1.11.1.-
Bromide peroxidase
BPO2
MEROPSS33.992 (Serine)

Pfam
PF00561 (Abhydrolase_1)
[Graphical view]


UniProtKB:Accession NumberP33912P29715
Entry nameBPA1_STRAUBPOA2_STRAU
Activity

SubunitHomodimer.Homotrimer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01371C01324C00708C00027C00720C01321C00001
CompoundRHBr-I-H2O2RBrRIH2O
TypelipidhalidehalideothershalidehalideH2O
ChEBI
15858
16382
16240


15377
PubChem
259
30165
784
22326046


962
22247451
               
1a8qAUnboundUnboundUnboundUnboundUnboundUnbound 
1broAUnboundUnboundUnboundUnboundUnboundUnbound 
1broBUnboundUnboundUnboundUnboundUnboundUnbound 
1brtAUnboundAnalogue:_CLUnboundUnboundUnboundUnbound 

Active-site residues
resource
PDB;1a7u, 1a88, 1a8q, 1a8s, 1a8u, 1brt & Swiss-prot;P33912, P29715, O31158, O31168, P49323
pdbCatalytic residuescomment
          
1a8qASER 94;ASP 223;HIS 252
 
1broASER 98;ASP 228;HIS 257
 
1broBSER 98;ASP 228;HIS 257
 
1brtASER 98;ASP 228;HIS 257
mutant M99T

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.535-536
[3]p.155-156
[4]Fig.5, p.895-898
[5]p.222

references
[1]
PubMed ID786162
JournalAnnu Rev Biochem
Year1976
Volume45
Pages861-88
AuthorsMorrison M, Schonbaum GR
TitlePeroxidase-catalyzed halogenation.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
Medline ID95393196
PubMed ID7664081
JournalNat Struct Biol
Year1994
Volume1
Pages532-7
AuthorsHecht HJ, Sobek H, Haag T, Pfeifer O, van Pee KH
TitleThe metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
Related PDB1bro
Related UniProtKBP29715
[3]
PubMed ID7632719
JournalBiochim Biophys Acta
Year1995
Volume1250
Pages149-57
AuthorsPelletier I, Altenbuchner J, Mattes R
TitleA catalytic triad is required by the non-heme haloperoxidases to perform halogenation.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
Medline ID98307994
PubMed ID9642069
JournalJ Mol Biol
Year1998
Volume279
Pages889-900
AuthorsHofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ
TitleStructural investigation of the cofactor-free chloroperoxidases.
Related PDB1a7u,1a88,1a8q,1a8s,1a8u,1brt
Related UniProtKBP33912,P29715,O31158,O31168,P49323
[5]
PubMed ID12369917
JournalCurr Protein Pept Sci
Year2000
Volume1
Pages209-35
AuthorsHolmquist M
TitleAlpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
[7]
PubMed ID12447906
JournalJ Mol Recognit
Year2002
Volume15
Pages291-6
AuthorsLittlechild J, Garcia-Rodriguez E, Dalby A, Isupov M
TitleStructural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.


createdupdated
2004-07-132009-02-26


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