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Lactate dehydrogenase (LDH) is the enzyme in the glycolytic pathway that converts pyruvate to lactate with concomitant interconversion of NADH and NAD+. In mammals, the enzyme is encoded by three genes: LDHA (M or muscle form), LDHB (H or heart form), and LDHC (X or testis form). The three human LDHs have 84-89% sequence similarities and 69-75% amino acid identities. There are five different LDH isoenzymes based on the proportion of M and H chains existing in the LDH tetrameric structure. The LDHA is hypoxia inducible and its expression is directly controlled by the transcriptional activity of the hypoxia inducible factor 1a (HIF1a). LDHB is also known to be upregulated in many cancers. Mutations in the LDHA gene can lead to Glycogen storage disease 11 (GSD11).
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Protein Aliases: Cell proliferation-inducing gene 19 protein; epididymis secretory sperm binding protein Li 133P; L-lactate dehydrogenase A chain; Lactate Dehydrogenase; lactate dehydrogenase M; Lactic Dehydrogenase; LDH muscle subunit; LDH-A; LDH-M; OTTHUMP00000165206; proliferation-inducing gene 19; Renal carcinoma antigen NY-REN-59
Gene Aliases: GSD11; HEL-S-133P; LDHA; LDHM; PIG19
UniProt ID: (Human) P00338
Entrez Gene ID: (Human) 3939
Molecular Function: dehydrogenase