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Journal of Zhejiang University SCIENCE B 2016 Vol.17 No.4 P.247-261

http://doi.org/10.1631/jzus.B1500219


Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase


Author(s):  Tóshiko Takahashi-Íñiguez, Nelly Aburto-Rodríguez, Ana Laura Vilchis-González, María Elena Flores

Affiliation(s):  Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, México, D.F. 04510, México

Corresponding email(s):   mflores@biomedicas.unam.mx

Key Words:  Malate dehydrogenase, Carbon metabolism, Tricarboxylic acid cycle


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Tóshiko Takahashi-Íñiguez, Nelly Aburto-Rodríguez, Ana Laura Vilchis-González, María Elena Flores. Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase[J]. Journal of Zhejiang University Science B, 2016, 17(4): 247-261.

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publisher="Zhejiang University Press & Springer",
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%A Nelly Aburto-Rodríguez
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DOI - 10.1631/jzus.B1500219


Abstract: 
malate dehydrogenase (MDH) is an enzyme widely distributed among living organisms and is a key protein in the central oxidative pathway. It catalyzes the interconversion between malate and oxaloacetate using NAD+ or NADP+ as a cofactor. Surprisingly, this enzyme has been extensively studied in eukaryotes but there are few reports about this enzyme in prokaryotes. It is necessary to review the relevant information to gain a better understanding of the function of this enzyme. Our review of the data generated from studies in bacteria shows much diversity in their molecular properties, including weight, oligomeric states, cofactor and substrate binding affinities, as well as differences in the direction of the enzymatic reaction. Furthermore, due to the importance of its function, the transcription and activity of this enzyme are rigorously regulated. Crystal structures of MDH from different bacterial sources led to the identification of the regions involved in substrate and cofactor binding and the residues important for the dimer-dimer interface. This structural information allows one to make direct modifications to improve the enzyme catalysis by increasing its activity, cofactor binding capacity, substrate specificity, and thermostability. A comparative analysis of the phylogenetic reconstruction of MDH reveals interesting facts about its evolutionary history, dividing this superfamily of proteins into two principle clades and establishing relationships between MDHs from different cellular compartments from archaea, bacteria, and eukaryotes.

微生物苹果酸脱氢酶的功能、动力学特征、晶体结构以及调控

概要:苹果酸脱氢酶(MDH)广泛存在于动物、植物以及微生物体内,是生物体进行糖代谢的关键酶之一。在辅酶I(NAD+)或辅酶II(NADP+)的作用下,能够催化草酰乙酸和苹果酸之间相互转化。虽然目前真核微生物中MDH已被广泛研究,但是对原核生物中的这种酶却鲜有报道。因此,有必要对MDH的相关研究信息进行综述,以期更好地了解这种酶的功能。本文综述了细菌相关研究的各种数据信息,进一步挖掘MDH的分子多样性,包括分子量、低聚态、辅因子与底物的结合力,以及酶反应方向的差异等。通过对不同细菌来源的MDH的晶体结构的分析,可鉴别底物与辅因子结合的部位以及形成二聚体的重要残基。对这些结构信息的了解将有利于指导研究人员对酶的结构进行修饰从而提高其催化能力,比如增加酶的活性、辅助因子的结合能力、底物特异性和热稳定性等。另外,本文通过分析比较MDH系统发生树的重建,将其蛋白超家族分成两个主分支,同时在古生菌、细菌和真核微生物等不同细胞的MDH之间建立联系。
关键词:苹果酸脱氢酶;碳代谢;三羧酸循环

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

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