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Links from Protein

Items: 8

1.

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)

GO Terms:
Molecular Function:
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)
Date:
2024-10-16
Family Accession:
NF014867.5
Method:
HMM
2.

lactate/malate family dehydrogenase

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)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-11-04
Family Accession:
NF012286.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

malate dehydrogenase

malate dehydrogenase specifically oxidizes malate to oxaloacetate

Date:
2024-05-21
Family Accession:
10102004
Method:
Sparcle
8.

malate dehydrogenase

This model represents the NAD-dependent malate dehydrogenase found in eukaryotes and certain gamma proteobacteria. The enzyme is involved in the citric acid cycle as well as the glyoxalate cycle. Several isoforms exidt in eukaryotes. In S. cereviseae, for example, there are cytoplasmic, mitochondrial and peroxisomal forms. Although malate dehydrogenases have in some cases been mistaken for lactate 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 lactate dehydrogenases.

Gene:
mdh
GO Terms:
Biological Process:
tricarboxylic acid cycle (GO:0006099)
Molecular Function:
L-malate dehydrogenase (NAD+) activity (GO:0030060)
Date:
2021-04-27
Family Accession:
TIGR01772.1
Method:
HMM
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