Haloperoxidase: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The <scene name='48/486480/Cv/ | The <scene name='48/486480/Cv/5'>vanadate ion shows a trigonal bipyramidal coordination</scene>. The iodine atoms are coordinated to tyrosine residues: <scene name='48/486480/Cv/6'>first coordination site</scene> and <scene name='48/486480/Cv/7'>second coordination site</scene> <ref>PMID:10543953</ref>. Water molecules shown as red spheres. | ||
</StructureSection> | </StructureSection> | ||
==3D structures of haloperoxidase== | ==3D structures of haloperoxidase== | ||
Revision as of 16:03, 14 May 2019
FunctionHaloperoxidases 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 highlightsThe . The iodine atoms are coordinated to tyrosine residues: and [2]. Water molecules shown as red spheres. |
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3D structures of haloperoxidase3D structures of haloperoxidase
Updated on 14-May-2019
ReferencesReferences
- ↑ 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