Malate dehydrogenase in plants: evolution, structure, and a myriad of functions

Author:

Baird Lisa M.1ORCID,Berndsen Christopher E.2ORCID,Monroe Jonathan D.2

Affiliation:

1. 1Department of Biology, University of San Diego, ­5998 Alcalá Park, San Diego, CA 92110, U.S.A.

2. 2Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr. MSC 4501, Harrisonburg, VA 22807, U.S.A.

Abstract

Abstract Malate dehydrogenase (MDH) catalyzes the interconversion of oxaloacetate and malate coupled to the oxidation/reduction of coenzymes NAD(P)H/NAD(P)+. While most animals have two isoforms of MDH located in the cytosol and mitochondria, all major groups of land plants have at least six MDHs localized to the cytosol, mitochondria, plastids, and peroxisomes. This family of enzymes participates in important reactions in plant cells including photosynthesis, photorespiration, lipid metabolism, and NH4+ metabolism. MDH also helps to regulate the energy balance in the cell and may help the plant cope with various environmental stresses. Despite their functional diversity, all of the plant MDH enzymes share a similar structural fold and act as dimers. In this review, we will introduce readers to our current understanding of the plant MDHs, including their evolution, structure, and function. The focus will be on the MDH enzymes of the model plant Arabidopsis thaliana.

Funder

National Science Foundation

Publisher

Portland Press Ltd.

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