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Haloperoxidase

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{{STRUCTURE_1qi9| PDB=1qi9 | SIZE=400| SCENE= |right|CAPTION=Bromoperoxidase complex with VO4 and Br- (purple) ions, [[1qi9]] }}
{{STRUCTURE_1qi9| PDB=1qi9 | SIZE=400| SCENE= |right|CAPTION=Bromoperoxidase complex with VO4 and Br- (purple) ions, [[1qi9]] }}
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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. CPO is heme-containing, vanadium-containing or metal-free. BPO from marine algae is vanadium-containing<ref>PMID:19363038</ref>.
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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. CPO is heme-, vanadium-containing or metal-free. BPO from marine algae is vanadium-containing.
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==3D structures of haloperoxidase==
==3D structures of haloperoxidase==
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== References ==
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[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:55, 20 March 2016

Template:STRUCTURE 1qi9


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. BPO from marine algae is vanadium-containing[1].

3D structures of haloperoxidase

Updated on 20-March-2016

References

  1. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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