The Enzyme Database

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EC 1.14.13.244     
Accepted name: phenol 2-monooxygenase (NADH)
Reaction: phenol + NADH + H+ + O2 = catechol + NAD+ + H2O
Other name(s): dmpLMNOP (gene names)
Systematic name: phenol,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nordlund, I., Powlowski, J. and Shingler, V. Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 172 (1990) 6826–6833. [PMID: 2254258]
2.  Powlowski, J. and Shingler, V. In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 172 (1990) 6834–6840. [PMID: 2254259]
3.  Powlowski, J., Sealy, J., Shingler, V. and Cadieux, E. On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Biol. Chem 272 (1997) 945–951. [PMID: 8995386]
4.  Qian, H., Edlund, U., Powlowski, J., Shingler, V. and Sethson, I. Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. Biochemistry 36 (1997) 495–504. [PMID: 9012665]
5.  Cadieux, E., Vrajmasu, V., Achim, C., Powlowski, J. and Munck, E. Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600. Biochemistry 41 (2002) 10680–10691. [PMID: 12186554]
[EC 1.14.13.244 created 2019]
 
 


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