4urf
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ure|4ure]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ure|4ure]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(S)-1-phenylethanol_dehydrogenase (S)-1-phenylethanol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.311 1.1.1.311] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(S)-1-phenylethanol_dehydrogenase (S)-1-phenylethanol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.311 1.1.1.311] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4urf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4urf RCSB], [http://www.ebi.ac.uk/pdbsum/4urf PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4urf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urf OCA], [http://pdbe.org/4urf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4urf RCSB], [http://www.ebi.ac.uk/pdbsum/4urf PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The dehydrogenation of 1-(4-hydroxyphenyl)-ethanol to 4-hydroxyacetophenone represents the second reaction step during anaerobic degradation of p-ethylphenol in the denitrifying bacterium 'Aromatoleum aromaticum' EbN1. Previous proteogenomic studies identified two different proteins (ChnA and EbA309) as possible candidates for catalyzing this reaction [Wohlbrand et al: J Bacteriol 2008;190:5699-5709]. Physiological-molecular characterization of newly generated unmarked in-frame deletion and complementation mutants allowed defining ChnA (renamed here as Hped) as the enzyme responsible for 1-(4-hydroxyphenyl)-ethanol oxidation. Hped [1-(4-hydroxyphenyl)-ethanol dehydrogenase] belongs to the 'classical' family within the short-chain alcohol dehydrogenase/reductase (SDR) superfamily. Hped was overproduced in Escherichia coli, purified and crystallized. The X-ray structures of the apo- and NAD+-soaked form were resolved at 1.5 and 1.1 A, respectively, and revealed Hped as a typical homotetrameric SDR. Modeling of the substrate 4-hydroxyacetophenone (reductive direction of Hped) into the active site revealed the structural determinants of the strict (R)-specificity of Hped (Phe187), contrasting the (S)-specificity of previously reported 1-phenylethanol dehydrogenase (Ped; Tyr93) from strain EbN1 [Hoffken et al: Biochemistry 2006;45:82-93]. | ||
| + | |||
| + | Molecular Genetic and Crystal Structural Analysis of 1-(4-Hydroxyphenyl)-Ethanol Dehydrogenase from 'Aromatoleum aromaticum' EbN1.,Busing I, Hoffken HW, Breuer M, Wohlbrand L, Hauer B, Rabus R J Mol Microbiol Biotechnol. 2015;25(5):327-39. doi: 10.1159/000439113. Epub 2015 , Oct 22. PMID:26488297<ref>PMID:26488297</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4urf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:08, 13 January 2016
Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1
| |||||||||||
