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


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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journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
%A Tóshiko Takahashi-Íñiguez
%A Nelly Aburto-Rodríguez
%A Ana Laura Vilchis-González
%A María Elena Flores
%J Journal of Zhejiang University SCIENCE B
%V 17
%N 4
%P 247-261
%@ 1673-1581
%D 2016
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1500219

T1 - Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
A1 - Tóshiko Takahashi-Íñiguez
A1 - Nelly Aburto-Rodríguez
A1 - Ana Laura Vilchis-González
A1 - María Elena Flores
J0 - Journal of Zhejiang University Science B
VL - 17
IS - 4
SP - 247
EP - 261
%@ 1673-1581
Y1 - 2016
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1500219

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.



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