Protein Family Models

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. [1]. 10075524. 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 1999;285:703-712. (from Pfam)

Date:

2024-08-14

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. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold. [1]. 10075524. 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 1999;285:703-712.. [2]. 12029364. Molecular evolution within the L-malate and L-lactate. dehydrogenase super-family.. Madern D;. J Mol Evol 2002;54:825-840. (from Pfam)

Date:

2024-08-14

L-lactate dehydrogenase converts (S)-lactate and NAD(+) to pyruvate and NADH

Date:

2015-09-18

This model represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme function as as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified [1] which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of malate dehydrogenases.

Date:

2021-05-12

Date:

2020-10-26