6itk: Difference between revisions
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==Crystal | ==Crystal structure of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malate== | ||
<StructureSection load='6itk' size='340' side='right'caption='[[6itk]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6itk' size='340' side='right'caption='[[6itk]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6itk]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6itk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ITK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=6itk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itk OCA], [https://pdbe.org/6itk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6itk RCSB], [https://www.ebi.ac.uk/pdbsum/6itk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6itk ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MDH_CORGL MDH_CORGL] Catalyzes the reversible oxidation of malate to oxaloacetate. Exhibits higher catalytic efficiency for oxaloacetate reduction than for malate oxidation in vitro. Almost equally active both for NADH and NADPH on the bases of the kcat values at pH 6.5, but catalytic efficiency for oxaloacetate reduction is 50-fold higher with NADH.<ref>PMID:16233457</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6itk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6itk" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Corynebacterium glutamicum ATCC 13032]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kim K-J]] | |||
[[Category: Kim | [[Category: Seo H]] | ||
[[Category: Seo | |||
Latest revision as of 12:52, 22 November 2023
Crystal structure of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malateCrystal structure of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malate
Structural highlights
FunctionMDH_CORGL Catalyzes the reversible oxidation of malate to oxaloacetate. Exhibits higher catalytic efficiency for oxaloacetate reduction than for malate oxidation in vitro. Almost equally active both for NADH and NADPH on the bases of the kcat values at pH 6.5, but catalytic efficiency for oxaloacetate reduction is 50-fold higher with NADH.[1] Publication Abstract from PubMedSuccinic 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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