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lactate/malate dehydrogenase, alpha/beta C-terminal domain
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)
NAD-binding protein
This domain is found in a wide variety of proteins. These protein include potassium channels Swiss:P31069, phosphoesterases Swiss:Q59027, and various other transporters. This domain binds to NAD. Domain called KTN in figure 2.. [1]. 9478130. A novel family of predicted phosphoesterases includes Drosophila. prune protein and bacterial RecJ exonuclease.. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:17-19.. [2]. 8412700. NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA. and sequence similarity between TrkA and domains of a family of. dehydrogenases suggest a role for NAD+ in bacterial transport.. Schlosser A, Hamann A, Bossemeyer D, Schneider E, Bakker EP;. Mol Microbiol 1993;9:533-543.. Called TRKA-N domain. See alignment in figure 8a.. [3]. 11292341. Regulatory potential, phyletic distribution and evolution of. ancient, intracellular small-molecule-binding domains.. Anantharaman V, Koonin EV, Aravind L;. J Mol Biol 2001;307:1271-1292. (from Pfam)
lactate/malate dehydrogenase, NAD binding domain
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)
malate dehydrogenase
malate dehydrogenase catalyzes the oxidation of malate to oxaloacetate
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