Title : Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is inactivated by S-sulfuration in vitro.

Pub. Date : 2015 Dec

PMID : 26453916






7 Functional Relationships(s)
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1 One of the first proteins shown to be modified by H2S was glyceraldehyde 3-phosphate dehydrogenase (GAPDH) [1] where the S-sulfuration of the active site cysteine (Cys 152) resulted in ~7-fold increase in the activity of the enzyme. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
2 One of the first proteins shown to be modified by H2S was glyceraldehyde 3-phosphate dehydrogenase (GAPDH) [1] where the S-sulfuration of the active site cysteine (Cys 152) resulted in ~7-fold increase in the activity of the enzyme. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
3 One of the first proteins shown to be modified by H2S was glyceraldehyde 3-phosphate dehydrogenase (GAPDH) [1] where the S-sulfuration of the active site cysteine (Cys 152) resulted in ~7-fold increase in the activity of the enzyme. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
4 One of the first proteins shown to be modified by H2S was glyceraldehyde 3-phosphate dehydrogenase (GAPDH) [1] where the S-sulfuration of the active site cysteine (Cys 152) resulted in ~7-fold increase in the activity of the enzyme. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
5 S-sulfuration of GAPDH occurred at Cys 247 after sulfide treatment, Cys 156 and Cys 247 after polysulfide treatment. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
6 Treatment of glutathione disulfide oxidized GAPDH with polysulfide also produced S-sulfuration of Cys 156. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens
7 Treatment of a C156S mutant of GAPDH with sulfide and polysulfide resulted in S-sulfuration of Cys 152, which also caused a decrease and not an increase in enzymatic activity. Cysteine glyceraldehyde-3-phosphate dehydrogenase Homo sapiens