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- | {{Seed}} | |
- | [[Image:1foh.png|left|200px]] | |
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- | <!-- | + | ==PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM== |
- | The line below this paragraph, containing "STRUCTURE_1foh", creates the "Structure Box" on the page.
| + | <StructureSection load='1foh' size='340' side='right'caption='[[1foh]], [[Resolution|resolution]] 2.40Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | + | <table><tr><td colspan='2'>[[1foh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cutaneotrichosporon_cutaneum Cutaneotrichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOH FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
- | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene></td></tr> |
- | {{STRUCTURE_1foh| PDB=1foh | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1foh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foh OCA], [https://pdbe.org/1foh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1foh RCSB], [https://www.ebi.ac.uk/pdbsum/1foh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1foh ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/PHHY_CUTCT 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).<ref>PMID:11591156</ref> <ref>PMID:1429434</ref> <ref>PMID:17425111</ref> <ref>PMID:2022646</ref> <ref>PMID:3203745</ref> <ref>PMID:4146224</ref> <ref>PMID:7851397</ref> <ref>PMID:7858421</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1foh_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1foh ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | ===PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM=== | + | ==See Also== |
- | | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
- | | + | == References == |
- | <!--
| + | <references/> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_9634698}}, adds the Publication Abstract to the page
| + | __TOC__ |
- | (as it appears on PubMed at http://www.pubmed.gov), where 9634698 is the PubMed ID number.
| + | </StructureSection> |
- | -->
| + | [[Category: Cutaneotrichosporon cutaneum]] |
- | {{ABSTRACT_PUBMED_9634698}}
| + | [[Category: Large Structures]] |
- | | + | [[Category: Enroth C]] |
- | ==About this Structure==
| + | [[Category: Lindqvist Y]] |
- | 1FOH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOH OCA].
| + | [[Category: Neujahr H]] |
- | | + | [[Category: Schneider G]] |
- | ==Reference== | + | |
- | 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., Enroth C, Neujahr H, Schneider G, Lindqvist Y, Structure. 1998 May 15;6(5):605-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9634698 9634698]
| + | |
- | [[Category: Phenol 2-monooxygenase]] | + | |
- | [[Category: Single protein]] | + | |
- | [[Category: Trichosporon cutaneum]]
| + | |
- | [[Category: Enroth, C.]] | + | |
- | [[Category: Lindqvist, Y.]] | + | |
- | [[Category: Neujahr, H.]] | + | |
- | [[Category: Schneider, G.]] | + | |
- | [[Category: Flavin]]
| + | |
- | [[Category: Monooxygenase]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Phenol hydroxylase]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:41:01 2008''
| + | |
| 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
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
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