期刊
JOURNAL OF ZHEJIANG UNIVERSITY-SCIENCE B
卷 17, 期 4, 页码 247-261出版社
ZHEJIANG UNIV
DOI: 10.1631/jzus.B1500219
关键词
Malate dehydrogenase; Carbon metabolism; Tricarboxylic acid cycle
类别
资金
- Universidad Nacional Autonoma de Mexico-Direccion General de Asuntos del Personal Academico-Programa de Apoyo a Proyectos de Investigacion e Innovacion Tecnologica (UNAM-DGAPA-PAPIIT) [IN206313]
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 reportsabout 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.
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