spacer

Overview for MACiE Entry M0014

Version history

General Information

EC Number: 1.11.1.10 (A member of the Oxidoreductases, Acting on a peroxide as acceptor, Peroxidases)

Enzyme Name: chloride peroxidase

Biological Species: Curvularia inaequalis (Fungus)

Catalytic Chain UniprotKB Accession Codes:

  • P49053 - Vanadium chloroperoxidase

Representative PDB Code: 1vnc - CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS (Resolution = 2.10 Å).

Catalytic CATH Codes:

  • 1.10.606.10 - Vanadium-containing Chloroperoxidase, domain 2

"Other" CATH Codes:

  • 1.20.144.10 - Vanadium-containing Chloroperoxidase, domain 1

Display structure information

Overall Reaction:

Image of chloride ion

Image of hydrogen peroxide

Image of proton

Image of alkane

right arrow

Image of water

Image of chlorinated alkane

chloride ion
C00698
CHEBI:17996
hydrogen peroxide
C00027
CHEBI:16240
proton
C00080
CHEBI:24636
alkane
C01371
CHEBI:18310
2 water
C00001
CHEBI:15377
chlorinated alkane
C01334
CHEBI:23128

It is unknown whether this reaction is reversible or not.

Overall Comment: Enzyme also oxidises bromide and iodide. The vanadate cofactor is covalently bound to the enzyme via the side chain nitrogen of His496.


View similar reactions


Stepwise Description of the Reaction

Step 1The axial hydroxide of the vanadate cofactor deprotonates hydrogen peroxide.
Step 2The activated hydrogen peroxide initiates a nucleophilic attack on the vanadate in a substitution reaction, eliminating water.
Step 3One of the equatorial oxo groups deprotonates the attached hydrogen peroxide.
Step 4The peroxide initiates a nucleophilic attack on the vanadate in a substitution reaction, eliminating hydroxide and forming a three membered ring.
Step 6The dioxygen bond undergoes rearrangement to eliminate hypochloroate with concomitant deprotonation of water, which initiates a nucleophilic attack on the vanadate in a coordination reaction to regenerate the cofactor.
Step 7The hypohalous acid chlorinates an organic substrate.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Lys 353 A Side Chain
Arg 360 A Side Chain
Ser 402 A Side Chain
Gly 403 A Main Chain Amide
His 404 A Side Chain
Arg 490 A Side Chain
His 496 A Side Chain

Metal Cofactors for M0014

Type Het group Number Chain
vanadium VO4 579 x Overview

References

  1. W. Hemrika et al. (1999), J. Biol. Chem., 274, 23820-23827. 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).
    Medline: 10446144
  2. A. Messerschmidt et al. (1996), Proc. Natl Acad. Sci. USA, 93, 392-396. X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
    Medline: 8552646
  3. A. Messerschmidt et al. (1997), Biol. Chem., 378, 309-315. 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.
    Medline: 9165086
  4. O. Bortolini et al. (2005), J. Inorg. Biochem., 99, 1549-1557. Vanadium (V) peroxocomplexes: structure, chemistry and biological implications.
    Medline: 15964077

Homologue information for M0014 (1vnc)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with the same EC number (different mechanisms):

MACiE Entry Enzyme Name PDB code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0248 chloride peroxidase 1a7u 0.303 0.2076 Compare
M0250 chloride peroxidase 2cpo 0.4848 0.1509 Compare

View a comparison of the other reactions in MACiE with EC number 1.11.1.10


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
catalytic activity (molecular function)
peroxidase activity (molecular function)
extracellular region (cellular component)
membrane (cellular component)
oxidoreductase activity (molecular function)
chloride peroxidase activity (molecular function)
metal ion binding (molecular function)
oxidation-reduction process (biological process)
spacer
spacer