Nomenclature
EC number
1.14.13.7
Systematic name
phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)
Recommended name
phenol 2-monooxygenase
Synonyms
oxygenase, phenol 2-mono-
phenol hydroxylase
phenol o-hydroxylase
CAS registry number
37256-84-1
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Neujahr, H.Y.; Gaal, A.: Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum. Eur. J. Biochem., 35, 386–400 (1973)
Nakagawa, H.; Takeda, Y.: Phenol hydroxylase. Biochim. Biophys. Acta, 62, 423–426 (1962)
Neujahr, H.Y.; Gaal, A.: Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum. Eur. J. Biochem., 58, 351–357 (1975)
Kjellen, K.G.; Neujahr, N.Y.: Immobilization of phenol hydroxylase. Biotechnol. Bioeng., 21, 715–719 (1979)
Detmer, K.; Massey, V.: Effect of monovalent anions on the mechanism of phenol hydroxylase. J. Biol. Chem., 259, 11265–11272 (1984)
Detmer, K.; Massey, V.: Effect of substrate and pN on the oxidative half-reaction of phenol hydroxylase. J. Biol. Chem., 260, 5998–6005 (1985)
Neujahr, N.Y.; Kjellen, K.G.: Phenol hydroxylase from yeast. Reaction with phenol derivatives. J. Biol. Chem., 253, 8835–8841 (1978)
Neujahr, N.Y.: Effect of anions, chaotropes, and phenol on the attachment of flavin adenine dinucleotide to phenol hydroxylase. Biochemistry, 22, 580–584 (1983)
Neujahr, H.Y.; Kjellen, K.G.: Phenol hydroxylase from yeast: a lysyl residue essential for binding of reduced nicotinamide adenine dinucleotide phosphate. Biochemistry, 19, 4967–4972 (1980)
Selitz, T.; Neujahr, H.Y.: Phenol hydroxylase from yeast. A model for phenol binding and an improved purification procedure. Eur. J. Biochem., 170, 343–349 (1987)
Krug, M.; Straube, G.: Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathway. J. Basic Microbiol., 26, 271–281 (1986)
Straube, G.: Phenol hydroxylase from Rhodococcus sp. P 1. J. Basic Microbiol., 27, 229–232 (1987)
Mörtberg, M.; Neujahr, H.Y.: In situ and in vitro kinetics of phenol hydroxylase. Biochem. Biophys. Res. Commun., 146, 41–46 (1987)
Cadieux, E.; Vrajmasu, V.; Achim, C.; Powlowski, J.; Muenck, E.: Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600. Biochemistry, 41, 10680–10691 (2002)
Enroth, C.; Neujahr, H.; Schneider, G.; Lindqvist, Y.: The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. Structure, 6, 605–617 (1998)
Hino, S.; Watanabe, K.; Takahashi, N.: Phenol hydroxylase cloned from Ralstonia eutropha strain E2 exhibits novel kinetic properties. Microbiology, 144, 1765–1772 (1998)
Kaelin, M.; Neujahr, H.Y.; Weissmahr, R.N.; Sejlitz, T.; Joehl, R.; Fiechter, A.; Reiser, J.: Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coil. J. Bacteriol., 174, 7112–7120 (1992)
Maeda-Yorita, K.; Massey, V.: On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studies. J. Biol. Chem., 268, 4134–4144 (1993)
Peelen, S.; Rietjens, LM.C.M.; Boersma, M.G.; Vervoort, J.: Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics. Eur. J. Biochem., 227, 284–291 (1995)
Peelen, S.; Rietjens, I.M.C.M.; van Berkel, W.J.H.; van Workum, W.A.T.; Vervoort, J.: Fluorine-19 NMR study on the pH-dependent regioselectivity and rate of the ortho-hydroxylation of 3-fluorophenol by phenol hydroxylase from Trichosporon cutaneum. Implications for the reaction mechanism. Eur. J. Biochem., 218, 345–353 (1993)
Pessione, E.; Divari, S.; Griva, E.; Cavaletto, M.; Rossi, G.L.; Gilardi, G.; Giunta, C.: Phenol hydroxylase from Acinetobacter radioresistens is a multicomponent enzyme. Purification and characterization of the reductase moiety. Eur. J. Biochem., 265, 549–555 (1999)
Waters, S.; Neujahr, H.Y.: A fermentor culture for production of recombinant phenol hydroxylase. Protein Expr. Purif., 5, 534–540 (1994)
Waters, S.; Neujahr, H.Y.: Sources and nature of heterogeneity in recombinant phenol hydroxylase derived from the basidiomycetous soil yeast Trichosporon cutaneum. Biotechnol. App1. Biochem., 25, 235–242 (1997)
Xu, D.; Ballou, D.P.; Massey, V.: Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met. Biochemistry, 40, 12369–12378 (2001)
Xu, D.; Enroth, C.; Lindqvist, Y.; Ballou, D.P.; Massey, V.: Studies of the mechanism of phenol hydroxylase: Effect of mutation of proline 364 to serine. Biochemistry, 41, 13627–13636 (2002)
Rights and permissions
Copyright information
© 2006 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2006). Phenol 2-monooxygenase. In: Class 1 Oxidoreductases XI. Springer Handbook of Enzymes, vol 26. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37708-5_46
Download citation
DOI: https://doi.org/10.1007/3-540-37708-5_46
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-26586-3
Online ISBN: 978-3-540-37708-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)