Pentachlorophenol monooxygenase
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| Pentachlorophenol monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.50 | ||||||||
| CAS no. | 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).[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- (1) pentachlorophenol + 2 NADPH + H+ + O2 2,3,5,6-tetrachlorohydroquinone + 2 NADP+ + chloride + H2O
- (2) 2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O
Pentachlorophenol monooxygenase is a flavoprotein (FAD).
References
- ^ Schenk T, Müller R, Mörsberger F, Otto MK, Lingens F (October 1989). "Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790". Journal of Bacteriology. 171 (10): 5487–91. doi:10.1128/jb.171.10.5487-5491.1989. PMC 210388. PMID 2793827.
- ^ Xun L, Topp E, Orser CS (May 1992). "Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries". Journal of Bacteriology. 174 (9): 2898–902. doi:10.1128/jb.174.9.2898-2902.1992. PMC 205942. PMID 1569020.
- ^ Xun L, Topp E, Orser CS (September 1992). "Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase". Journal of Bacteriology. 174 (17): 5745–7. doi:10.1128/jb.174.17.5745-5747.1992. PMC 206524. PMID 1512208.
- ^ Lange CC, Schneider BJ, Orser CS (February 1996). "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. doi:10.1006/bbrc.1996.0196. PMID 8619798.
- ^ Nakamura T, Motoyama T, Hirono S, Yamaguchi I (August 2004). "Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1700 (2): 151–9. doi:10.1016/j.bbapap.2004.04.008. PMID 15262224.
External links
- Pentachlorophenol+monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
