PTHR23382

MALATE DEHYDROGENASE

PANTHER entry
Member databasePANTHER
PANTHER typefamily

Description
Imported from IPR010945

Malate dehydrogenases catalyse the interconversion of malate and oxaloacetate using dinucleotide cofactors
[1]
. The enzymes in this entry are found in archaea, bacteria and eukaryotes and fall into two distinct groups. The first group are cytoplasmic, NAD-dependent enzymes which participate in the citric acid cycle (
1.1.1.37
). The second group are found in plant chloroplasts, use NADP as cofactor, and participate in the C4 cycle (
1.1.1.82
).

Structural studies indicate that these enzymes are homodimers with very similar overall topology, though the chloroplast enzymes also have N- and C-terminal extensions, and all contain the classical Rossman fold for NAD(P)H binding
[2, 3, 4, 5]
. Substrate specificity is determined by a mobile loop at the active site which uses charge balancing to discriminate between the correct substrates (malate and oxaloacetate) and other potential oxo/hydroxyacid substrates the enzyme may encounter within the cell
[6]
.

References
Imported from IPR010945

1.Malate dehydrogenase: a model for structure, evolution, and catalysis. Goward CR, Nicholls DJ. Protein Sci. 3, 1883-8, (1994). View articlePMID: 7849603

2.Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ. Biochemistry 32, 3913-22, (1993). View articlePMID: 8471603

3.Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho Y. J. Biol. Chem. 274, 11761-7, (1999). View articlePMID: 10206992

4.Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form. Johansson K, Ramaswamy S, Saarinen M, Lemaire-Chamley M, Issakidis-Bourguet E, Miginiac-Maslow M, Eklund H. Biochemistry 38, 4319-26, (1999). View articlePMID: 10194350

5.Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Carr PD, Verger D, Ashton AR, Ollis DL. Structure 7, 461-75, (1999). View articlePMID: 10196131

6.Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. Chapman AD, Cortes A, Dafforn TR, Clarke AR, Brady RL. J. Mol. Biol. 285, 703-12, (1999). View articlePMID: 10075524

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