D00059
type: Enzyme
cath: Vanadium-containing Chloroperoxidase; domain 1
cath: Vanadium-containing Chloroperoxidase; domain 2
ec: https://purl.uniprot.org/enzyme/1.11.1.10
csa: 1vnc
macie: M0014
uniprot: P49053
kegg enzyme: chloride peroxidase
kegg enzyme: chloroperoxidase
kegg cofactor: Vanadium
kegg substrate: RH
kegg substrate: Cl-
kegg substrate: H2O2
kegg product: RCl
kegg product: H2O
pdb: 1idqA01
pdb: 1iduA01
pdb: 1vncA01
pdb: 1vneA01
pdb: 1vnfA01
pdb: 1vngA01
pdb: 1vnhA01
pdb: 1vniA01
pdb: 1vnsA01
pdb: 1idqA02
pdb: 1iduA02
pdb: 1vncA02
pdb: 1vneA02
pdb: 1vnfA02
pdb: 1vngA02
pdb: 1vnhA02
pdb: 1vniA02
pdb: 1vnsA02
pdb bound state: Unbound
  compound: RH
  pdb: 1idqA01
pdb bound state: Unbound
  compound: RH
  pdb: 1iduA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vncA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vneA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vnfA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vngA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vnhA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vniA01
pdb bound state: Unbound
  compound: RH
  pdb: 1vnsA01
pdb bound state: Unbound
  compound: RH
  pdb: 1idqA02
pdb bound state: Unbound
  compound: RH
  pdb: 1iduA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vncA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vneA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vnfA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vngA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vnhA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vniA02
pdb bound state: Unbound
  compound: RH
  pdb: 1vnsA02
pdb bound state: Unbound
  compound: Cl-
  pdb: 1idqA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1iduA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vncA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vneA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vnfA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vngA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vnhA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vniA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vnsA01
pdb bound state: Unbound
  compound: Cl-
  pdb: 1idqA02
pdb bound state: Unbound
  compound: Cl-
  pdb: 1iduA02
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vncA02
pdb bound state: Unbound
  compound: Cl-
  pdb: 1vneA02
active site residues resources: Haloperoxidases and their role in biotransformation reactions.
active site residues resources: X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00059#11
active site residues resources: P49053
references: X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
references: Implications 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.
references: A new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in von Gierke disease.
references: An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
references: Haloperoxidases and their role in biotransformation reactions.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00059#6
references: X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
references: X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution.
references: Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms.
references: Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00059#11
references: Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.

Vanadium-containing Chloroperoxidase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.144.10

Vanadium-containing Chloroperoxidase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.606.10
catalytic domain: index.html

Vanadium
type: KeggCofactor
references: KEGG:C06267
compound type: heavy metal

RH
type: KeggSubstrate
references: KEGG:C01371
compound type: lipid

Cl-
type: KeggSubstrate
references: KEGG:C00698
compound type: halide
references: CHEBI:17996
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H2O2
type: KeggSubstrate
references: KEGG:C00027
compound type: others
references: CHEBI:16240
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

RCl
type: KeggProduct
references: KEGG:C01334
compound type: halide

H2O
type: KeggProduct
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1idqA02
type: Pdb
references: 1idq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1idq
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)

1iduA02
type: Pdb
references: 1idu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1idu
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)

1vncA02
type: Pdb
references: 1vnc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vnc
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)

1vneA02
type: Pdb
references: 1vne
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vne
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)
comment: mutant D292A

1vnfA02
type: Pdb
references: 1vnf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vnf
catalytic residue: LYS 353; ;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)
comment: mutant R360A

1vngA02
type: Pdb
references: 1vng
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vng
catalytic residue: LYS 353;ARG 360; ;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)
comment: mutant H404A

1vnhA02
type: Pdb
references: 1vnh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vnh
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
comment: mutant H496A

1vniA02
type: Pdb
references: 1vni
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vni
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)

1vnsA02
type: Pdb
references: 1vns
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vns
catalytic residue: LYS 353;ARG 360;HIS 404;ARG 490
cofactor binding residue: HIS 496(Vanadium binding)

X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
medline id: 96133943
references: http://www.ncbi.nlm.nih.gov/pubmed/8552646
journal: Proc Natl Acad Sci U S A
volume: 93
pages: 392-6
published year: 1996
authors:
  item: Messerschmidt A
  item: Wever R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P49053

Implications 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.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9165086
journal: Biol Chem
volume: 378
pages: 309-15
published year: 1997
authors:
  item: Messerschmidt A
  item: Prade L
  item: Wever R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

A new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in von Gierke disease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9224681
journal: FEBS Lett
volume: 409
pages: 317-9
published year: 1997
authors:
  item: Hemrika W
  item: Wever R

An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9260289
journal: Protein Sci
volume: 6
pages: 1764-7
published year: 1997
authors:
  item: Neuwald AF

Haloperoxidases and their role in biotransformation reactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10021409
journal: Curr Opin Chem Biol
volume: 3
pages: 28-34
published year: 1999
authors:
  item: Littlechild J

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00059#6
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10446144
journal: J Biol Chem
volume: 274
pages: 23820-7
published year: 1999
authors:
  item: Hemrika W
  item: Renirie R
  item: Macedo-Ribeiro S
  item: Messerschmidt A
  item: Wever R
title: Heterologous 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).

X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10499093
journal: J Biol Inorg Chem
volume: 4
pages: 209-19
published year: 1999
authors:
  item: Macedo-Ribeiro S
  item: Hemrika W
  item: Renirie R
  item: Wever R
  item: Messerschmidt A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10543953
journal: J Mol Biol
volume: 293
pages: 595-611
published year: 1999
authors:
  item: Weyand M
  item: Hecht H
  item: Kiess M
  item: Liaud M
  item: Vilter H
  item: Schomburg D

Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10766783
journal: J Biol Chem
volume: 275
pages: 11650-7
published year: 2000
authors:
  item: Renirie R
  item: Hemrika W
  item: Wever R

Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10843856
journal: J Mol Biol
volume: 299
pages: 1035-49
published year: 2000
authors:
  item: Isupov MN
  item: Dalby AR
  item: Brindley AA
  item: Izumi Y
  item: Tanabe T
  item: Murshudov GN
  item: Littlechild JA

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00059#11
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11800602
journal: Inorg Chem
volume: 41
pages: 161-3
published year: 2002
authors:
  item: Kimblin C
  item: Bu X
  item: Butler A
title: Modeling 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.

Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12447906
journal: J Mol Recognit
volume: 15
pages: 291-6
published year: 2002
authors:
  item: Littlechild J
  item: Garcia-Rodriguez E
  item: Dalby A
  item: Isupov M

Analogue
compound: Vanadium
pdb: 1vnsA02
ligand het code: SO4

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.395-396

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.7, p.314

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.2a, p.30-31

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.5, p.23825-23826

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.10, p.603-604

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.8, p.11656

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.1, p.294