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EC Number	Posttranslational Modification	Commentary	Reference
1.1.1.27	acylation	lysine acetylation appears as a specific modification of LDH-5. It is involved in the control of its activity. Acetylation at Y5 decreases the LDHA protein level and inhibits LDH-5 activity. Lysine-5 acetylation reduces and be accompanied with increased LDHA protein levels in both early and late stages of pancreatic cancers. Acetylated LDHA can be recognized by a cytosolic chaperone and it is easily degraded by lysosomal proteolysis	740255
1.1.1.27	phosphoprotein	L-lactate dehydrogenase (LDHA) is a substrate of protein tyrosine phosphatase PTP1B	760891
1.1.1.27	phosphoprotein	LDH-5 can serve as a substrate of the oncogenic viral Src (v-Src) tyrosine kinase and the oncogenic receptor tyrosine kinase FGFR1. Direct phosphorylation of LDHA at Y10 and Y83 strongly enhances LDH-5 tetramer formation and cofactor binding, resulting in significantly increased LDH enzymatic activity. LDHA tyrosine phosphorylation also decides about the translocation of LDH-5 to the nucleus	740255
1.1.1.27	phosphoprotein	purified LDH from aerobic control crayfish shows significantly higher amounts of serine/threonine phosphorylation than does the anoxic enzyme form	740337

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Release 2023.1 (January 2023)