| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.11.1.- |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.11.-.- |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "Enzymes of this type are either heme-thiolate proteins, or contain vanadate."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18)."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "Also oxidizes bromide and iodide."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "It catalyzes the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2000/01/rdf-schema#comment | "At a separate site it catalyzes the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://www.w3.org/2004/02/skos/core#prefLabel | "chloride peroxidase"xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8747463 |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1056179 |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10885468 |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11670813 |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16790441 |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16870515 |
| http://purl.uniprot.org/enzyme/1.11.1.10 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17777960 |