Pentachlorophenol monooxygenase

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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

\rightleftharpoons

2,3,5,6-tetrachlorohydroquinone + 2 NADP⁺ + chloride + H₂O

(2) 2,3,5,6-tetrachlorophenol + NADPH + H⁺ + O2

\rightleftharpoons

2,3,5,6-tetrachlorohydroquinone + NADP⁺ + H₂O

Pentachlorophenol monooxygenase is a flavoprotein (FAD).

References

↑ Schenk, T., Müller, R., Mörsberger, F., Otto, M.K. and Lingens, F. (1989). "Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790". J. Bacteriol. 171 (10): 5487–5491. PMC 210388. PMID 2793827.
↑ Xun, L., Topp, E. and Orser, C.S. (1992). "Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries". J. Bacteriol. 174 (9): 2898–2902. PMC 205942. PMID 1569020.
↑ Xun, L., Topp, E. and Orser, C.S. (1992). "Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase". J. Bacteriol. 174 (17): 5745–5747. PMC 206524. PMID 1512208.
↑ Lange, C.C., Schneider, B.J. and Orser, C.S. (1996). "Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723". Biochem. Biophys. Res. Commun. 219 (1): 146–149. doi:10.1006/bbrc.1996.0196. PMID 8619798.
↑ Nakamura, T., Motoyama, T., Hirono, S. and Yamaguchi, I. (2004). "Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase". Biochim. Biophys. Acta 1700 (2): 151–159. doi:10.1016/j.bbapap.2004.04.008. PMID 15262224.

External links

Pentachlorophenol monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase

1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase

1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1

1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1

1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase

1.14.17: reduced ascorbate	Dopamine beta-hydroxylase

1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1

1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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