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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 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> | + | <table><tr><td colspan='2'>[[6itl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mannheimia_succiniciproducens_MBEL55E Mannheimia succiniciproducens MBEL55E]. 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 [https://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" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97Å</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='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='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'>[https://proteopedia.org/fgij/fg.htm?mol=6itl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itl OCA], [https://pdbe.org/6itl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6itl RCSB], [https://www.ebi.ac.uk/pdbsum/6itl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6itl ProSAT]</span></td></tr> |
| - | <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. | + | [https://www.uniprot.org/uniprot/MDH_MANSM MDH_MANSM] Catalyzes the reversible oxidation of malate to oxaloacetate. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Malate dehydrogenase]]
| + | [[Category: Kim K-J]] |
| - | [[Category: Mansm]]
| + | [[Category: Seo H]] |
| - | [[Category: Kim, K J]] | + | |
| - | [[Category: Seo, H]] | + | |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
MDH_MANSM Catalyzes the reversible oxidation of malate to oxaloacetate.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ahn JH, Seo H, Park W, Seok J, Lee JA, Kim WJ, Kim GB, Kim KJ, Lee SY. Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase. Nat Commun. 2020 Apr 23;11(1):1970. doi: 10.1038/s41467-020-15839-z. PMID:32327663 doi:http://dx.doi.org/10.1038/s41467-020-15839-z
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