Biology:Pentachlorophenol monooxygenase
| Pentachlorophenol monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.50 | ||||||||
| CAS number | 136111-57-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pentachlorophenol monooxygenase (EC 1.14.13.50, pentachlorophenol dechlorinase, pentachlorophenol dehalogenase, pentachlorophenol 4-monooxygenase, PCP hydroxylase, pentachlorophenol hydroxylase, PcpB, PCB 4-monooxygenase, PCB4MO) is an enzyme with systematic name pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating). It catalyses two different chemical reactions, depending on its substrate. In each case, the starting material is a phenol.[1][2]
Pentachlorophenol monooxygenase is a flavoprotein.[3]
Reactions catalysed
The enzyme acts only on phenols with halogens in the position next to the hydroxy group on the benzene ring, the 2-position.[4]
With hydrogen at the 4-position
In this case, a typical reaction converts 2,3,5,6-tetrachlorophenol to tetrachlorohydroquinone:[5]
- REDIRECT Template:Chemical reaction
With a halogen at the 4-position
In this case, a typical reaction converts pentachlorophenol to chloranil:[6]
- REDIRECT Template:Chemical reaction
References
- ↑ "Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790". Journal of Bacteriology 171 (10): 5487–91. October 1989. doi:10.1128/jb.171.10.5487-5491.1989. PMID 2793827.
- ↑ "Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1700 (2): 151–9. August 2004. doi:10.1016/j.bbapap.2004.04.008. PMID 15262224.
- ↑ "Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase". Journal of Bacteriology 174 (17): 5745–7. September 1992. doi:10.1128/jb.174.17.5745-5747.1992. PMID 1512208.
- ↑ Enzyme 1.14.13.50 at KEGG Pathway Database.
- ↑ "Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries". Journal of Bacteriology 174 (9): 2898–902. May 1992. doi:10.1128/jb.174.9.2898-2902.1992. PMID 1569020.
- ↑ "Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723". Biochemical and Biophysical Research Communications 219 (1): 146–9. February 1996. doi:10.1006/bbrc.1996.0196. PMID 8619798. Bibcode: 1996BBRC..219..146L.
External links
- Pentachlorophenol+monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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