Haloperoxidase: Difference between revisions
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<StructureSection load='1qi9' size='400' side='right' scene='48/486480/Cv/1' caption='Bromoperoxidase complex with VO4 and I- (purple) ions, [[1qi9]]'> | |||
== 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''' is 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-, vanadium-containing or metal-free. BPO from marine algae is vanadium-containing. | |||
== Structural highlights == | |||
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> | |||
==3D structures of haloperoxidase== | ==3D structures of haloperoxidase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | |||
*Vanadium-dependent chloroperoxidase | |||
[[1vnc]], [[1vni]], [[1idq]], [[1idu]] – CiCPO – ''Curvularia inaequalis''<br /> | **[[1vnc]], [[1vni]], [[1idq]], [[1idu]] – CiCPO + VO4 – ''Curvularia inaequalis''<br /> | ||
[[1vne]], [[1vnf]], [[1vng]], [[1vnh]] – CiCPO (mutant)<br /> | **[[1vne]], [[1vnf]], [[1vng]], [[1vnh]] – CiCPO (mutant) + VO4<br /> | ||
[[1vns]] – CiCPO | **[[1vns]], [[3bb0]] – CiCPO <br /> | ||
**[[3w35]] – StCPO – ''Streptomyces''<br /> | |||
**[[3w36]] – StCPO + VO4<br /> | |||
**[[5lpc]] – CPO – ''Acaryochloris marina''<br /> | |||
*Heme-containing chloroperoxidase | |||
[[1cpo]], [[2cpo]] – LfCPO – ''Leptoxyphium fumago''<br /> | **[[1cpo]], [[2cpo]] – LfCPO – ''Leptoxyphium fumago''<br /> | ||
[[2civ]] – LfCPO + Br<br /> | **[[2civ]], [[2j18]], [[2j19]] – LfCPO + Br<br /> | ||
[[2ciw]] – LfCPO + I<br /> | **[[2ciw]] – LfCPO + I<br /> | ||
[[2cix]] – LfCPO + cyclopentane-dione + Br<br /> | **[[2cix]] – LfCPO + cyclopentane-dione + Br<br /> | ||
[[2ciy]] – LfCPO + CN + DMSO + Br<br /> | **[[2ciy]] – LfCPO + CN + DMSO + Br<br /> | ||
[[2ciz]] – LfCPO + acetate + Br<br /> | **[[2ciz]] – LfCPO + acetate + Br<br /> | ||
[[2cj0]] – LfCPO + nitrate<br /> | **[[2cj0]] – LfCPO + nitrate<br /> | ||
[[2cj1]], [[2cj2]] – LfCPO + formate<br /> | **[[2cj1]], [[2cj2]] – LfCPO + formate<br /> | ||
[[2j5m]] – LfCPO + H2O2 | **[[2j5m]] – LfCPO + H2O2 | ||
*Metal-free chloroperoxidase | |||
[[1a7u]] - SaCPO T – ''Streptomyces aureofaciens''<br /> | **[[1a7u]] - SaCPO T – ''Streptomyces aureofaciens''<br /> | ||
[[1a8s]] – PfCPO F + propanoic acid – ''Pseudomonas fluorescens''<br /> | **[[1a8s]] – PfCPO F + propanoic acid – ''Pseudomonas fluorescens''<br /> | ||
[[1a8u]] – PfCPO T + benzoic acid<br /> | **[[1a8u]] – PfCPO T + benzoic acid<br /> | ||
[[1a88]] - CPO L – ''Streptomyces lividans'' | **[[1a88]] - CPO L – ''Streptomyces lividans''<br /> | ||
**[[4dgq]] – CPO – ''Burkholderia cenocepacia''<br /> | |||
*Metal-free bromoperoxidase | |||
[[1a8q]] – SaBPO A1<br /> | **[[1a8q]] – SaBPO A1<br /> | ||
[[1bro]] - SaBPO A2<br /> | **[[1bro]] - SaBPO A2<br /> | ||
[[1brt]] – SaBPO A2 (mutant)<br /> | **[[1brt]], [[4iq4]], [[4itv]], [[4ivj]], [[4qes]], [[4qf0]], [[4qff]] – SaBPO A2 (mutant)<br /> | ||
[[3fob]] – BPO – ''Bacillus anthracis'' | **[[3fob]] – BPO – ''Bacillus anthracis'' | ||
*Vanadium-containing bromoperoxidase | |||
[[1qi9]] – | **[[1qi9]] – AnBPO + I + VO4 – ''Ascophyllum nodosum''<br /> | ||
[[1up8]] – | **[[5aa6]] – AnBPO-2 + VO4<br /> | ||
**[[1up8]], [[1qhb]], [[7qyy]] – CpBPO – ''Corallina pilulifera''<br /> | |||
**[[7qvw]] – CpBPO (mutant) <br /> | |||
**[[7qwi]] – CpBPO + VO4<br /> | |||
**[[7qw3]] – CpBPO (mutant) + Br<br /> | |||
*Vanadium-containing iodoperoxidase | |||
**[[4cit]], [[4usz]] – IPO + VO4 – ''Zobellia galactanivorans''<br /> | |||
}} | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 12:12, 30 June 2024
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.
Structural highlightsThe . The iodine atoms are coordinated to tyrosine residues: and [2]. Water molecules shown as red spheres. |
| ||||||||||
3D structures of haloperoxidase3D structures of haloperoxidase
Updated on 30-June-2024
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