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| Line 21: |
Line 21: |
| **[[3w35]] – StCPO – ''Streptomyces''<br /> | | **[[3w35]] – StCPO – ''Streptomyces''<br /> |
| **[[3w36]] – StCPO + VO4<br /> | | **[[3w36]] – StCPO + VO4<br /> |
| **[[5lpc]] – CPO – ''Acaryochloris marina''<br /> | | **[[5lpc]] – AmCPO – ''Acaryochloris marina''<br /> |
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| *Heme-containing chloroperoxidase | | *Heme-containing chloroperoxidase |
| Line 55: |
Line 55: |
| **[[5aa6]] – AnBPO-2 + VO4<br /> | | **[[5aa6]] – AnBPO-2 + VO4<br /> |
| **[[1up8]], [[1qhb]], [[7qyy]] – CpBPO – ''Corallina pilulifera''<br /> | | **[[1up8]], [[1qhb]], [[7qyy]] – CpBPO – ''Corallina pilulifera''<br /> |
| | **[[8vgx]] – CpBPO – Cryo EM<br /> |
| **[[7qvw]] – CpBPO (mutant) <br /> | | **[[7qvw]] – CpBPO (mutant) <br /> |
| **[[7qwi]] – CpBPO + VO4<br /> | | **[[7qwi]] – CpBPO + VO4<br /> |
| | **[[8vh0]] – CpBPO + VO4 – Cryo EM<br /> |
| **[[7qw3]] – CpBPO (mutant) + Br<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 /> |
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| *Vanadium-containing iodoperoxidase | | *Vanadium-containing iodoperoxidase |
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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[1].
Structural highlights
The vanadate ion shows a trigonal bipyramidal coordination. The iodine atoms are coordinated to tyrosine residues: first coordination site and second coordination site [2]. Water molecules shown as red spheres.
- ↑ 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:https://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
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3D structures of haloperoxidase
Updated on 07-August-2025
{"openlevels":0}
- Vanadium-dependent chloroperoxidase
- Heme-containing chloroperoxidase
- Metal-free chloroperoxidase
- 1a7u - SaCPO T – Streptomyces aureofaciens
- 1a8s – PfCPO F + propanoic acid – Pseudomonas fluorescens
- 1a8u – PfCPO T + benzoic acid
- 1a88 - CPO L – Streptomyces lividans
- 4dgq – CPO – Burkholderia cenocepacia
- Metal-free bromoperoxidase
- Vanadium-containing bromoperoxidase
- 1qi9 – AnBPO + I + VO4 – Ascophyllum nodosum
- 5aa6 – AnBPO-2 + VO4
- 1up8, 1qhb, 7qyy – CpBPO – Corallina pilulifera
- 8vgx – CpBPO – Cryo EM
- 7qvw – CpBPO (mutant)
- 7qwi – CpBPO + VO4
- 8vh0 – CpBPO + VO4 – Cryo EM
- 7qw3 – CpBPO (mutant) + Br
- 8vjq – CpBPO + VO4 + Br – Cryo EM
- 8vix – CpBPO + VO4 + O2 – Cryo EM
- 8q20, 8q21, 8q22 – AmBPO (mutant)
- Vanadium-containing iodoperoxidase
- 4cit, 4usz – IPO + VO4 – Zobellia galactanivorans
References