6ITK

Crystal structure of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malate

6ITK の概要

• エントリーDOI: 10.2210/pdb6itk/pdb
• 分子名称: Malate dehydrogenase, (2S)-2-hydroxybutanedioic acid, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: dehydrogenase, oxidoreductase
• 由来する生物種: Corynebacterium glutamicum ATCC 13032
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73617.19

構造登録者

Seo, H.,Kim, K.-J. (登録日: 2018-11-23, 公開日: 2019-11-27, 最終更新日: 2023-11-22)

主引用文献

Ahn, J.H.,Seo, H.,Park, W.,Seok, J.,Lee, J.A.,Kim, W.J.,Kim, G.B.,Kim, K.J.,Lee, S.Y.
Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase.
Nat Commun, 11:1970-1970, 2020

PubMed Abstract: 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 μM 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 of SA with the maximum productivity of 21.3 g L h, demonstrating the importance of enzyme optimization in strain development.

PubMed: 32327663
DOI: 10.1038/s41467-020-15839-z

実験手法

X-RAY DIFFRACTION (2 Å)