6itl
From Proteopedia
(Difference between revisions)
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<StructureSection load='6itl' size='340' side='right'caption='[[6itl]], [[Resolution|resolution]] 1.97Å' scene=''> | <StructureSection load='6itl' size='340' side='right'caption='[[6itl]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6itl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITL OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6itl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mansm Mansm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ITL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdh, MS1266 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=221988 MANSM])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6itl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itl OCA], [http://pdbe.org/6itl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6itl RCSB], [http://www.ebi.ac.uk/pdbsum/6itl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6itl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MDH_MANSM MDH_MANSM]] Catalyzes the reversible oxidation of malate to oxaloacetate. | [[http://www.uniprot.org/uniprot/MDH_MANSM MDH_MANSM]] Catalyzes the reversible oxidation of malate to oxaloacetate. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Succinic acid (SA), a dicarboxylic acid of industrial importance, can be efficiently produced by metabolically engineered Mannheimia succiniciproducens. Malate dehydrogenase (MDH) is one of the key enzymes for SA production, but has not been well characterized. Here we report biochemical and structural analyses of various MDHs and development of hyper-SA producing M. succiniciproducens by introducing the best MDH. Corynebacterium glutamicum MDH (CgMDH) shows the highest specific activity and least substrate inhibition, whereas M. succiniciproducens MDH (MsMDH) shows low specific activity at physiological pH and strong uncompetitive inhibition toward oxaloacetate (ki of 67.4 and 588.9 muM for MsMDH and CgMDH, respectively). Structural comparison of the two MDHs reveals a key residue influencing the specific activity and susceptibility to substrate inhibition. A high-inoculum fed-batch fermentation of the final strain expressing cgmdh produces 134.25 g L(-1) of SA with the maximum productivity of 21.3 g L(-1) h(-1), demonstrating the importance of enzyme optimization in strain development. | ||
| + | |||
| + | Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase.,Ahn JH, Seo H, Park W, Seok J, Lee JA, Kim WJ, Kim GB, Kim KJ, Lee SY Nat Commun. 2020 Apr 23;11(1):1970. doi: 10.1038/s41467-020-15839-z. PMID:32327663<ref>PMID:32327663</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6itl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Malate dehydrogenase]] | [[Category: Malate dehydrogenase]] | ||
| + | [[Category: Mansm]] | ||
[[Category: Kim, K J]] | [[Category: Kim, K J]] | ||
[[Category: Seo, H]] | [[Category: Seo, H]] | ||
Revision as of 06:33, 10 June 2020
Crystal strcuture of malate dehydrogenase from Mannheimia succiniciproducens in complex with NAD
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