Haloperoxidase
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 2: | Line 2: | ||
== Function == | == 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<ref>PMID:19363038</ref>. | + | '''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''' is from marine algae is vanadium-containing<ref>PMID:19363038</ref>. | ||
== 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== | ||
| Line 19: | Line 21: | ||
**[[3w35]] – StCPO – ''Streptomyces''<br /> | **[[3w35]] – StCPO – ''Streptomyces''<br /> | ||
**[[3w36]] – StCPO + VO4<br /> | **[[3w36]] – StCPO + VO4<br /> | ||
| - | **[[5lpc]] – | + | **[[5lpc]] – AmCPO – ''Acaryochloris marina''<br /> |
*Heme-containing chloroperoxidase | *Heme-containing chloroperoxidase | ||
| Line 52: | Line 54: | ||
**[[1qi9]] – AnBPO + I + VO4 – ''Ascophyllum nodosum''<br /> | **[[1qi9]] – AnBPO + I + VO4 – ''Ascophyllum nodosum''<br /> | ||
**[[5aa6]] – AnBPO-2 + VO4<br /> | **[[5aa6]] – AnBPO-2 + VO4<br /> | ||
| - | **[[1up8]], [[1qhb]] – | + | **[[1up8]], [[1qhb]], [[7qyy]] – CpBPO – ''Corallina pilulifera''<br /> |
| + | **[[8vgx]] – CpBPO – Cryo EM<br /> | ||
| + | **[[7qvw]] – CpBPO (mutant) <br /> | ||
| + | **[[7qwi]] – CpBPO + VO4<br /> | ||
| + | **[[8vh0]] – CpBPO + VO4 – Cryo EM<br /> | ||
| + | **[[7qw3]] – CpBPO (mutant) + Br<br /> | ||
| + | **[[8vjq]] – CpBPO + VO4 + Br – Cryo EM<br /> | ||
| + | **[[8vix]] – CpBPO + VO4 + O2 – Cryo EM<br /> | ||
| + | **[[8q20]], [[8q21]], [[8q22]] – AmBPO (mutant)<br /> | ||
*Vanadium-containing iodoperoxidase | *Vanadium-containing iodoperoxidase | ||
Current revision
| |||||||||||
3D structures of haloperoxidase
Updated on 07-August-2025
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
