Haloperoxidase
From Proteopedia
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| - | {{STRUCTURE_1qi9| PDB=1qi9 | SIZE=400| SCENE= |right|CAPTION=Bromoperoxidase complex with VO4 and | + | {{STRUCTURE_1qi9| PDB=1qi9 | SIZE=400| SCENE= |right|CAPTION=Bromoperoxidase complex with VO4 and I- (purple) ions, [[1qi9]] }} |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The vanadate | + | The vanadate ion shows a trigonal bipyramidal coordination. The iodine atoms are coordinated to tyrosine residues<ref>PMID:10543953</ref>. |
==3D structures of haloperoxidase== | ==3D structures of haloperoxidase== | ||
Revision as of 10:15, 20 March 2016
Contents |
Function
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].
Structural highlights
The vanadate ion shows a trigonal bipyramidal coordination. The iodine atoms are coordinated to tyrosine residues[2].
3D structures of haloperoxidase
Updated on 20-March-2016
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
