Member database | Pfam |
Pfam type | domain |
Short name | Ldh_1_C |
Clan | LDH_C |
Author | Bateman A;0000-0002-6982-4660 Eddy SR;0000-0001-6676-4706 Griffiths-Jones SR;0000-0001-6043-807X |
Sequence Ontology | 0000417 |
Description
L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes.
References
1. 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