1foh

Structural highlights

Function

PHHY_CUTCT Hydroxylates phenol to catechol (PubMed:1429434, PubMed:4146224, PubMed:3203745, PubMed:2022646, PubMed:7858421, PubMed:7851397, PubMed:11591156). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols (PubMed:4146224, PubMed:17425111, PubMed:7851397).^{[1] [2] [3] [4] [5] [6] [7] [8]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Monooxygenase 3D structures

References

1. ↑ Xu D, Ballou DP, Massey V. Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met. Biochemistry. 2001 Oct 16;40(41):12369-78. PMID:11591156 doi:10.1021/bi010962y
2. ↑ Kälin M, Neujahr HY, Weissmahr RN, Sejlitz T, Jöhl R, Fiechter A, Reiser J. Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli. J Bacteriol. 1992 Nov;174(22):7112-20. PMID:1429434 doi:10.1128/jb.174.22.7112-7120.1992
3. ↑ Gerginova M, Manasiev J, Shivarova N, Alexieva Z. Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain. Z Naturforsch C J Biosci. 2007 Jan-Feb;62(1-2):83-6. PMID:17425111 doi:10.1515/znc-2007-1-215
4. ↑ Taylor MG, Massey V. Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase. J Biol Chem. 1991 May 5;266(13):8291-301 PMID:2022646
5. ↑ Mörtberg M, Neujahr HY. Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ. FEBS Lett. 1988 Dec 19;242(1):75-8. PMID:3203745 doi:10.1016/0014-5793(88)80988-8
6. ↑ Neujahr HY, Gaal A. Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum. Eur J Biochem. 1973 Jun;35(2):386-400. PMID:4146224 doi:10.1111/j.1432-1033.1973.tb02851.x
7. ↑ Peelen S, Rietjens IM, Boersma MG, 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. 1995 Jan 15;227(1-2):284-91. PMID:7851397 doi:10.1111/j.1432-1033.1995.tb20386.x
8. ↑ Waters S, Neujahr HY. A fermentor culture for production of recombinant phenol hydroxylase. Protein Expr Purif. 1994 Dec;5(6):534-40. PMID:7858421 doi:10.1006/prep.1994.1073