1foh: Difference between revisions

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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]] 2.40&Aring;' 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]] 2.4&#8491;</td></tr>
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<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
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(as it appears on PubMed at http://www.pubmed.gov), where 9634698 is the PubMed ID number.
</StructureSection>
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[[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''

Latest revision as of 10:16, 7 February 2024

PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUMPHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM

Structural highlights

1foh is a 4 chain structure with sequence from Cutaneotrichosporon cutaneum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  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

1foh, resolution 2.40Å

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