Title : Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenase.

Pub. Date : 1999 Jul 9

PMID : 10391884






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenase. Sulfhydryl Compounds glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
2 We now demonstrate that in contrast to NO-mediated attachment of NAD, covalent attachment of NADH to GAPDH proceeds in the presence of low molecular weight thiols, independent of NO. Sulfhydryl Compounds glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
3 Lys-C digestion of GAPDH, followed by peptide isolation by high performance liquid chromatography, matrix-assisted laser desorption ionization time-of-flight analysis, and Edman sequencing, demonstrated that NADH attachment occurred at Cys-149, the active-site thiol. Sulfhydryl Compounds glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
4 Thus, linkage of GAPDH to NADH, in contrast to NAD, occurs in the presence of thiol, is independent of NO, and is mediated by superoxide. Sulfhydryl Compounds glyceraldehyde-3-phosphate dehydrogenase Homo sapiens