Pentachlorophenol monooxygenase

Pentachlorophenol monooxygenase
Identifiers
EC no.1.14.13.50
CAS no.136111-57-4
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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]

+ NADPH + H+
 
 
O2
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27102186.
Tetrachlorohydroquinone
 

With a halogen at the 4-position

In this case, a typical reaction converts pentachlorophenol to chloranil:[6]

+ NADPH + H+
 
 
O2
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
+ NADP+ + Cl−
 

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ Enzyme 1.14.13.50 at KEGG Pathway Database.
  5. ↑ 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.
  6. ↑ 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. Bibcode:1996BBRC..219..146L. doi:10.1006/bbrc.1996.0196. PMID 8619798.