EzCatDB: S00344

DB codeS00344
CATH domainDomain 13.40.50.1820Catalytic domain
E.C.1.11.1.10
CSA1a7u
MACiEM0248

CATH domainRelated DB codes (homologues)
3.40.50.1820S00544,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
Swiss-protKEGG

P49323O31158O31168
Protein nameNon-heme chloroperoxidaseNon-heme chloroperoxidaseNon-heme chloroperoxidasechloride peroxidase
chloroperoxidase
SynonymsEC 1.11.1.10
Chloride peroxidase
Chloroperoxidase L
CPO-L
EC 1.11.1.10
Chloride peroxidase
Chloroperoxidase F
CPO-F
EC 1.11.1.10
Chloride peroxidase
Chloroperoxidase T
CPO-T


Swiss-prot:Accession NumberP49323O31158O31168
Entry namePRXC_STRLIPRXC_PSEFLPRXC_STRAU
ActivityRH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
SubunitHomodimer.Homodimer.Homodimer.
Subcellular location


Cofactor




SubstratesProducts
KEGG-idC01371C00698C00027C01334C00001
CompoundRHCl-H2O2RClH2O
TypelipidhalideothershalideH2O
1a88AUnboundUnboundUnboundUnbound
1a88BUnboundUnboundUnboundUnbound
1a88CUnboundUnboundUnboundUnbound
1a8sABound:PPIUnboundUnboundUnbound
1a7uAUnboundUnboundUnboundUnbound
1a7uBUnboundUnboundUnboundUnbound
1a8uABound:BEZUnboundUnboundUnbound
1a8uBBound:BEZUnboundUnboundUnbound

Active-site residues
resource
PDB;1a7u, 1a88, 1a8q, 1a8s, 1a8u, 1brt & Swiss-prot;P33912, P29715, O31158, O31168, P49323
pdbCatalytic residues
1a88ASER 96;ASP 226;HIS 255
1a88BSER 96;ASP 226;HIS 255
1a88CSER 96;ASP 226;HIS 255
1a8sASER 94;ASP 224;HIS 253
1a7uASER 98;ASP 228;HIS 257
1a7uBSER 98;ASP 228;HIS 257
1a8uASER 98;ASP 228;HIS 257
1a8uBSER 98;ASP 228;HIS 257

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
[7]Fig. 5
[8]Figure 3
[9]FIGURE 1a

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 Swiss-protP29715
[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 Swiss-protP33912,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.
[6]
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.
[7]
PubMed ID15381402
JournalBioorg Chem
Year2004
Volume32
Pages367-75
AuthorsBugg TD
TitleDiverse catalytic activities in the alphabeta-hydrolase family of enzymes: activation of H2O, HCN, H2O2, and O2.
[8]
PubMed ID15803517
JournalAngew Chem Int Ed Engl
Year2005
Volume44
Pages2742-6
AuthorsBernhardt P, Hult K, Kazlauskas RJ
TitleMolecular basis of perhydrolase activity in serine hydrolases.
[9]
PubMed ID20112920
JournalBiochemistry
Year2010
Volume49
Pages1931-42
AuthorsYin de LT, Bernhardt P, Morley KL, Jiang Y, Cheeseman JD, Purpero V, Schrag JD, Kazlauskas RJ
TitleSwitching catalysis from hydrolysis to perhydrolysis in Pseudomonas fluorescens esterase.
Related PDB3hea,3hi4
Related Swiss-protP22862

comments
This enzyme is closely related to arylesterase (EC 3.1.1.2; S00720 in EzCatDB), which has got a classical catalytic triad composed of Ser/His/Asp.

createdupdated
2004-07-132012-03-28
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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