Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities.
The hydrogen peroxide-induced 'non-phosphorylating' activity of D-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is shown to be a result of the successive action of two forms of the enzyme subunits: one catalyzing production of 1,3-bisphosphoglycerate, and the other performing its hydrolytic decomposition. The latter form is produced by mild oxidation of GAPDH in the presence of a low hydrogen peroxide concentration when essential Cys-149 is oxidized to the sulfenate derivative. The results obtained with a C153S mutant of Bacillus stearothermophilus GAPDH rule out the possibility that intrasubunit acyl transfer between Cys-149 and a sulfenic form of Cys-153 is required for the 'non-phosphorylating' activity of the enzyme.
Schmalhausen
E V
EV
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
Nagradova
N K
NK
Boschi-Muller
S
S
Branlant
G
G
Muronetz
V I
VI
D003001:Cloning, Molecular; D003545:Cysteine; D004926:Escherichia coli; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010766:Phosphorylation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013434:Sulfenic Acids
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D013434:Sulfenic Acids; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010744:Phosphoric Monoester Hydrolases; D003545:Cysteine