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.
Publication Abstract from PubMed
The crystal structure model of phenol hydroxylase has been corrected for 11 sequence errors and refined against new data to 1.7 A resolution. The higher resolution data together with careful exploitation of non-crystallographic symmetry restraints and the use of many small groups for refinement of anisotropic displacement parameters resulted in a large decrease in the crystallographic R factor. The final crystallographic free R factor is 18.0%, which should be compared with the values of 27.8% for the previously published model (PDB code 1foh). The rebuilding and re-refinement procedure is described. A comparison with the previously published model was performed and possible biochemical implications are discussed. No large differences suggesting gross errors in the earlier model were found. The actual differences between these two models give an indication of the level of ambiguity and inaccuracy that may be found in a well refined protein model at 2.4 A resolution.
High-resolution structure of phenol hydroxylase and correction of sequence errors.,Enroth C Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Enroth C. High-resolution structure of phenol hydroxylase and correction of sequence errors. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790
