InterPro : IPR001236

Name  Lactate/malate dehydrogenase, N-terminal Short Name  Lactate/malate_DH_N
Type  Domain Description  L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis []. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. 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.This entry represents the N-terminal, and is thought to be a Rossmann NAD-binding fold.
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

5 Found In

Id Name Short Name Type
IPR001557 L-lactate/malate dehydrogenase L-lactate/malate_DH Family
IPR010945 Malate dehydrogenase, type 2 Malate_DH_type2 Family
IPR010097 Malate dehydrogenase, type 1 Malate_DH_type1 Family
IPR011304 L-lactate dehydrogenase L-lactate_DH Family
IPR011275 Malate dehydrogenase, type 3 Malate_DH_type3 Family

1 Parent Features

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain

2 Publications

First Author Title Year Journal Volume Pages
Read JA Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. 2001 Proteins 43 175-85
Gleason WB Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. 1994 Biochemistry 33 2078-88



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)