v5.1.0.3
Glycine data from LIS
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 cytoplasmic, 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 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 [ , , , ]. 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 []. |
Short Name | Malate_DH_type2 |