D-Glyceraldehyde-3-phosphate dehydrogenase: structural basis and functional role of the acyl transfer reactions.
The catalytic mechanism of D-glyceraldehyde-3-phosphate dehydrogenase is considered in the light of the available structural information. The design features of the enzyme molecule determining the pathway of the acyl transfer, i.e., the transfer of the acyl group produced in the oxidative step of the reaction to one of the two acceptors, inorganic phosphate or water, are discussed. The properties of enzyme forms possessing cysteine residues oxidized to sulfenic acid derivatives are described. The participation of these residues in the acyl transfer to water is considered.
Nagradova
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NK
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. nagrad@bac.genebee.msu.su
Schmalhausen
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EV
D020134:Catalytic Domain; D003545:Cysteine / Q000737:chemistry; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D010085:Oxidative Phosphorylation; D011487:Protein Conformation
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D003545:Cysteine