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PROSITE documentation PDOC51405Heme haloperoxidase family profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51405
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Hofrichter M. Ullrich R. |
| Title | Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance. | |
| Source | Appl. Microbiol. Biotechnol. 71:276-288(2006). | |
| PubMed ID | 16628447 | |
| DOI | 10.1007/s00253-006-0417-3 |
| 2 | Authors | Manoj K.M. Hager L.P. |
| Title | Chloroperoxidase, a janus enzyme. | |
| Source | Biochemistry 47:2997-3003(2008). | |
| PubMed ID | 18220360 | |
| DOI | 10.1021/bi7022656 |
| 3 | Authors | Sundaramoorthy M. Terner J. Poulos T.L. |
| Title | The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid. | |
| Source | Structure 3:1367-1377(1995). | |
| PubMed ID | 8747463 |
| 4 | Authors | Kuhnel K. Blankenfeldt W. Terner J. Schlichting I. |
| Title | Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. | |
| Source | J. Biol. Chem. 281:23990-23998(2006). | |
| PubMed ID | 16790441 | |
| DOI | 10.1074/jbc.M603166200 |
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