Haloperoxidase
From Proteopedia
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'''Haloperoxidases''' catalyze the oxidation of halides by hydrogen peroxide while adding a halide to hydrocarbons. They are classified as '''chloroperoxldase''' (CPO), '''bromoperoxidase''' (BPO) and '''iodoperoxidase''' (IPO) according to the halide which they oxidize. | '''Haloperoxidases''' catalyze the oxidation of halides by hydrogen peroxide while adding a halide to hydrocarbons. They are classified as '''chloroperoxldase''' (CPO), '''bromoperoxidase''' (BPO) and '''iodoperoxidase''' (IPO) according to the halide which they oxidize. | ||
*'''CPO''' is heme-containing, vanadium-containing or metal-free. | *'''CPO''' is heme-containing, vanadium-containing or metal-free. | ||
| - | *'''BPO''' from marine algae is vanadium-containing<ref>PMID:19363038</ref>. | + | *'''BPO''' is from marine algae is vanadium-containing<ref>PMID:19363038</ref>. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 09:12, 30 June 2024
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3D structures of haloperoxidase
Updated on 30-June-2024
References
- ↑ Winter JM, Moore BS. Exploring the chemistry and biology of vanadium-dependent haloperoxidases. J Biol Chem. 2009 Jul 10;284(28):18577-81. doi: 10.1074/jbc.R109.001602. Epub, 2009 Apr 10. PMID:19363038 doi:http://dx.doi.org/10.1074/jbc.R109.001602
- ↑ Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D. X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution. J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:10543953 doi:10.1006/jmbi.1999.3179
