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4fr2

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Revision as of 16:48, 5 August 2016

Alcohol dehydrogenase from Oenococcus oeni

Structural highlights

4fr2 is a 1 chain structure with sequence from Oenococcus oeni atcc baa-1163. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	dhaT, OENOO_49030 (Oenococcus oeni ATCC BAA-1163)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Alcohol dehydrogenases are highly diverse enzymes catalysing the interconversion of alcohols and aldehydes or ketones. Due to their versatile specificities, these biocatalysts are of great interest for industrial applications. The adh3-gene encoding a group III alcohol dehydrogenase was isolated from the gram-positive bacterium Oenococcus oeni and was characterised after expression in the heterologous host Escherichia coli. Adh3 has been identified by genome BLASTP analyses using the amino acid sequence of 1,3-propanediol dehydrogenase DhaT from Klebsiella pneumoniae and group III alcohol dehydrogenases with known activity towards 1,3-propanediol as target sequences. The recombinant protein was purified in a two-step column chromatography approach. Crystal structure determination and biochemical characterisation confirmed that Adh3 forms a Ni(2+)-containing homodimer in its active form. Adh3 catalyses the interconversion of ethanol and its corresponding aldehyde acetaldyhyde and is also capable of using other alcoholic compounds as substrates, such as 1,3-propanediol, 1,2-propanediol and 1-propanol. In the presence of Ni(2+), activity increases towards 1,3-propanediol and 1,2-propanediol. Adh3 is strictly dependent on NAD(+)/NADH, whereas no activity has been observed with NADP(+)/NADPH as co-factor. The enzyme exhibits a specific activity of 1.1 U/mg using EtOH as substrate with an optimal pH value of 9.0 for ethanol oxidation and 8.0 for aldehyde reduction. Moreover, Adh3 exhibits tolerance to several metal ions and organic solvents, but is completely inhibited in the presence of Zn(2+). The present study demonstrates that O. oeni is a group III alcohol dehydrogenase with versatile substrate specificity, including Ni(2+)-dependent activity towards 1,3-propanediol.

Structural and biochemical characterisation of a NAD(+)-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications.,Elleuche S, Fodor K, Klippel B, von der Heyde A, Wilmanns M, Antranikian G Appl Microbiol Biotechnol. 2013 Feb 6. PMID:23385476^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Elleuche S, Fodor K, Klippel B, von der Heyde A, Wilmanns M, Antranikian G. Structural and biochemical characterisation of a NAD(+)-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications. Appl Microbiol Biotechnol. 2013 Feb 6. PMID:23385476 doi:10.1007/s00253-013-4725-0

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4fr2"

@@ Line 1: / Line 1: @@
 ==Alcohol dehydrogenase from Oenococcus oeni==
 <StructureSection load='4fr2' size='340' side='right' caption='[[4fr2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaT, OENOO_49030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=379360 Oenococcus oeni ATCC BAA-1163])</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=4fr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fr2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fr2 RCSB], [http://www.ebi.ac.uk/pdbsum/4fr2 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=4fr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fr2 OCA], [http://pdbe.org/4fr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fr2 RCSB], [http://www.ebi.ac.uk/pdbsum/4fr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fr2 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4fr2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4fr2

From Proteopedia

Revision as of 16:48, 5 August 2016

Alcohol dehydrogenase from Oenococcus oeni

Structural highlights

Publication Abstract from PubMed

References

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