4cmf: Difference between revisions
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==The (R)-selective transaminase from Nectria haematococca with inhibitor bound== | ==The (R)-selective transaminase from Nectria haematococca with inhibitor bound== | ||
<StructureSection load='4cmf' size='340' side='right' caption='[[4cmf]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='4cmf' size='340' side='right' caption='[[4cmf]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmd|4cmd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmd|4cmd]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=4cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cmf RCSB], [http://www.ebi.ac.uk/pdbsum/4cmf 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=4cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmf OCA], [http://pdbe.org/4cmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cmf RCSB], [http://www.ebi.ac.uk/pdbsum/4cmf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cmf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4cmf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminotransferase|Aminotransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:13, 11 August 2016
The (R)-selective transaminase from Nectria haematococca with inhibitor boundThe (R)-selective transaminase from Nectria haematococca with inhibitor bound
Structural highlights
Publication Abstract from PubMedDuring the last decade the use of transaminases for the production of pharmaceutical and fine chemical intermediates has attracted a great deal of attention. Transaminases are versatile biocatalysts for the efficient production of amine intermediates and many have (S)-enantiospecificity. Transaminases with (R)-specificity are needed to expand the applications of these enzymes in biocatalysis. In this work we have identified a fungal putative (R)-specific transaminase from the Eurotiomycetes Nectria haematococca, cloned a synthetic version of this gene, demonstrated (R)-selective deamination of several substrates including (R)-alpha-methylbenzylamine, as well as production of (R)-amines, and determined its crystal structure. The crystal structures of the holoenzyme and the complex with an inhibitor gabaculine offer the first detailed insight into the structural basis for substrate specificity and enantioselectivity of the industrially important class of (R)-selective amine:pyruvate transaminases. This article is protected by copyright. All rights reserved. STRUCTURED DIGITAL ABSTRACT: TAm and TAm bind by x-ray crystallography (View interaction). The substrate specificity, enantioselectivity and structure of the (R)-selective amine:pyruvate transaminase from Nectria haematococca.,Sayer C, Martinez-Torres RJ, Richter N, Isupov MN, Hailes HC, Littlechild JA, Ward JM FEBS J. 2014 Mar 11. doi: 10.1111/febs.12778. PMID:24618038[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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