InterPro : IPR010945

Name  Malate dehydrogenase, type 2 Short Name  Malate_DH_type2
Type  Family Description  Malate dehydrogenases catalyse the interconversion of malate and oxaloacetate using dinucleotide cofactors []. The enzymes in this entry are found in archaea, bacteria and eukaryotes and fall into two distinct groups. The first group are cytoplamsic, NAD-dependent enzymes which participate in the citric acid cycle (). The second group are found in plant chloroplasts, use NADP as cofactor, and participate in the C4 cycle ().Structural studies indicate that these enzymes are homodimers with very sinmilar 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 [, , , ]. 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 [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

3 Child Features

Id Name Short Name Type
IPR011274 Malate dehydrogenase, NAD-dependent, cytosolic Malate_DH_NAD-dep_euk Family
IPR011272 Lactate dehydrogenase, protist Lactate_DH_protist Family
IPR011273 Malate dehydrogenase, NADP-dependent, plants Malate_DH_NADP-dep_pln Family

5 Contains

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal Lactate_DH/Glyco_Ohase_4_C Domain
IPR001236 Lactate/malate dehydrogenase, N-terminal Lactate/malate_DH_N Domain
IPR022383 Lactate/malate dehydrogenase, C-terminal Lactate/malate_DH_C Domain
IPR001252 Malate dehydrogenase, active site Malate_DH_AS Active_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR001557 L-lactate/malate dehydrogenase L-lactate/malate_DH Family

6 Publications

First Author Title Year Journal Volume Pages
Johansson K Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form. 1999 Biochemistry 38 4319-26
Chapman AD Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. 1999 J Mol Biol 285 703-12
Kelly CA Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. 1993 Biochemistry 32 3913-22
Kim SY Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. 1999 J Biol Chem 274 11761-7
Carr PD Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. 1999 Structure 7 461-75
Goward CR Malate dehydrogenase: a model for structure, evolution, and catalysis. 1994 Protein Sci 3 1883-8



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)