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PROSITE documentation PDOC51405

Heme haloperoxidase family profile





Description

Heme haloperoxidase or chloroperoxidase (CPO) is an ~250 residue heme-containing glycoprotein that is secreted by various fungi. CPO was first identified in Caldariomyces fumago where it catalyzes the hydrogen peroxide-dependent chlorination of cyclopentanedione during the biosynthesis of the antibiotic caldarioymcin. Additionally, heme haloperoxidase catalyzes the iodination and bromination of a wide range of substrates. Besides performing H2O2-dependent halogenation reactions, the enzyme catalyzes dehydrogenation reactions. CPO also functions as a catalase, facilitating the decomposition of hydrogen peroxide to oxygen and water. Furthermore, heme haloperoxidase catalyzes P450-like oxygen insertion reactions. The capability of heme haloperoxidase to perform these diverse reactions makes it one of the most versatile of all known heme proteins [1,2].

Despite functional similarities with other heme enzymes, heme haloperoxidase folds into a novel tertiary structure dominated by eight helical segments (see <PDB: 1CPO>) [3]. Structurally, heme haloperoxidase is unique, but it shares features with both peroxidases and P450 enzymes. As in cytochrome P450 enzymes, the proximal heme ligand of the heme haloperoxidase is a cysteine, but similar to peroxidases, the distal side of the heme is polar. However, unlike other peroxidases, the normally conserved distal arginine is lacking and the catalytic acid base is a glutamic acid and not a histidine [4].

The profile we developed covers the whole conserved region of the heme haloperoxidase family.

Last update:

September 2008 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

HEME_HALOPEROXIDASE, PS51405; Heme haloperoxidase family profile  (MATRIX)


References

1AuthorsHofrichter M. Ullrich R.
TitleHeme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance.
SourceAppl. Microbiol. Biotechnol. 71:276-288(2006).
PubMed ID16628447
DOI10.1007/s00253-006-0417-3

2AuthorsManoj K.M. Hager L.P.
TitleChloroperoxidase, a janus enzyme.
SourceBiochemistry 47:2997-3003(2008).
PubMed ID18220360
DOI10.1021/bi7022656

3AuthorsSundaramoorthy M. Terner J. Poulos T.L.
TitleThe crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
SourceStructure 3:1367-1377(1995).
PubMed ID8747463

4AuthorsKuhnel K. Blankenfeldt W. Terner J. Schlichting I.
TitleCrystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.
SourceJ. Biol. Chem. 281:23990-23998(2006).
PubMed ID16790441
DOI10.1074/jbc.M603166200



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