EzCatDB: D00059

DB codeD00059
CATH domainDomain 11.20.144.10
Domain 21.10.606.10Catalytic domain
E.C.1.11.1.10
CSA1vnc
MACiEM0014


Enzyme Name
Swiss-protKEGG

P49053
Protein nameVanadium chloroperoxidasechloride peroxidase
chloroperoxidase
SynonymsEC 1.11.1.10
Vanadium chloride peroxidase
VCPO


Swiss-prot:Accession NumberP49053
Entry namePRXC_CURIN
ActivityRH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
Subunit
Subcellular locationSecreted.
CofactorVanadium.


CofactorsSubstratesProducts
KEGG-idC06267C01371C00698C00027C01334C00001
CompoundVanadiumRHCl-H2O2RClH2O
Typeheavy metallipidhalideothershalideH2O
1idqA01UnboundUnboundUnboundUnboundUnbound
1iduA01UnboundUnboundUnboundUnboundUnbound
1vncA01UnboundUnboundUnboundUnboundUnbound
1vneA01UnboundUnboundUnboundUnboundUnbound
1vnfA01UnboundUnboundUnboundUnboundUnbound
1vngA01UnboundUnboundUnboundUnboundUnbound
1vnhA01UnboundUnboundUnboundUnboundUnbound
1vniA01UnboundUnboundUnboundUnboundUnbound
1vnsA01UnboundUnboundUnboundUnboundUnbound
1idqA02Bound:VO4UnboundUnboundUnboundUnbound
1iduA02Bound:VO4UnboundUnboundUnboundUnbound
1vncA02Bound:VO4UnboundUnboundUnboundUnbound
1vneA02Bound:VO4UnboundUnboundUnboundUnbound
1vnfA02Bound:VO4UnboundUnboundUnboundUnbound
1vngA02Bound:VO4UnboundUnboundUnboundUnbound
1vnhA02Bound:VO4UnboundUnboundUnboundUnbound
1vniA02Bound:VO4UnboundUnboundUnboundUnbound
1vnsA02Analogue:SO4UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P49053 & literature [4], [6], [10]
pdbCatalytic residuesCofactor-binding residuescomment
1idqA01


1iduA01


1vncA01


1vneA01


1vnfA01


1vngA01


1vnhA01


1vniA01


1vnsA01


1idqA02LYS 353;ARG 360;HIS 404;ARG 490
HIS 496(Vanadium binding)

1iduA02LYS 353;ARG 360;HIS 404;ARG 490
HIS 496(Vanadium binding)

1vncA02LYS 353;ARG 360;HIS 404;ARG 490
HIS 496(Vanadium binding)

1vneA02LYS 353;ARG 360;HIS 404;ARG 490
HIS 496(Vanadium binding)
mutant D292A
1vnfA02LYS 353;       ;HIS 404;ARG 490
HIS 496(Vanadium binding)
mutant R360A
1vngA02LYS 353;ARG 360;       ;ARG 490
HIS 496(Vanadium binding)
mutant H404A
1vnhA02LYS 353;ARG 360;HIS 404;ARG 490
                         
mutant H496A
1vniA02LYS 353;ARG 360;HIS 404;ARG 490
HIS 496(Vanadium binding)

1vnsA02LYS 353;ARG 360;HIS 404;ARG 490
HIS 496(Vanadium binding)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.395-396
[2]Fig.7, p.314
[5]Fig.2a, p.30-31
[6]Fig.5, p.23825-23826
[8]Fig.10, p.603-604
[9]Fig.8, p.11656
[12]Fig.1, p.294

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID96133943
PubMed ID8552646
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages392-6
AuthorsMesserschmidt A, Wever R
TitleX-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
Related PDB1vnc
Related Swiss-protP49053
[2]
CommentsX-ray crystallography
PubMed ID9165086
JournalBiol Chem
Year1997
Volume378
Pages309-15
AuthorsMesserschmidt A, Prade L, Wever R
TitleImplications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form.
Related PDB1idu,1idq,1vne,1vnf
[3]
PubMed ID9224681
JournalFEBS Lett
Year1997
Volume409
Pages317-9
AuthorsHemrika W, Wever R
TitleA new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in von Gierke disease.
[4]
PubMed ID9260289
JournalProtein Sci
Year1997
Volume6
Pages1764-7
AuthorsNeuwald AF
TitleAn unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
[5]
PubMed ID10021409
JournalCurr Opin Chem Biol
Year1999
Volume3
Pages28-34
AuthorsLittlechild J
TitleHaloperoxidases and their role in biotransformation reactions.
[6]
PubMed ID10446144
JournalJ Biol Chem
Year1999
Volume274
Pages23820-7
AuthorsHemrika W, Renirie R, Macedo-Ribeiro S, Messerschmidt A, Wever R
TitleHeterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His(496), Lys(353), Arg(360), and Arg(490).
[7]
CommentsX-ray crystallography
PubMed ID10499093
JournalJ Biol Inorg Chem
Year1999
Volume4
Pages209-19
AuthorsMacedo-Ribeiro S, Hemrika W, Renirie R, Wever R, Messerschmidt A
TitleX-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
Related PDB1vng,1vnh,1vni,1vns
[8]
PubMed ID10543953
JournalJ Mol Biol
Year1999
Volume293
Pages595-611
AuthorsWeyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D
TitleX-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution.
[9]
PubMed ID10766783
JournalJ Biol Chem
Year2000
Volume275
Pages11650-7
AuthorsRenirie R, Hemrika W, Wever R
TitlePeroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms.
[10]
PubMed ID10843856
JournalJ Mol Biol
Year2000
Volume299
Pages1035-49
AuthorsIsupov MN, Dalby AR, Brindley AA, Izumi Y, Tanabe T, Murshudov GN, Littlechild JA
TitleCrystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.
[11]
PubMed ID11800602
JournalInorg Chem
Year2002
Volume41
Pages161-3
AuthorsKimblin C, Bu X, Butler A
TitleModeling the catalytic site of vanadium bromoperoxidase: synthesis and structural characterization of intramolecularly H-bonded vanadium(V) oxoperoxo complexes, [VO(O(2))((NH)2pyg(2))]K and [VO(O(2))((BrNH)2pyg(2))]K.
[12]
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
2004-06-212009-02-26
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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