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Literature summary for 1.2.1.12 extracted from

  • Blatnik, M.; Thorpe, S.R.; Baynes, J.W.
    Succination of proteins by fumarate: mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in diabetes (2008), Ann. N. Y. Acad. Sci., 1126, 272-275.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine in diabetic rats, modification of GAPDH by S-(2-succinyl)cysteine is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
S-(2-succinyl)cysteine chemical modification by S-(2-succinyl)cysteine causes irreversible inactivation of glyceraldehyde-3-phosphate dehydrogenase in vitro. In diabetic rats, succination of GAPDH is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
diabetic rat
-