D-glyceraldehyde-3-phosphate dehydrogenase: pre-existent asymmetry of the tetramer and its functional implications.
Modification of a single arginine residue per subunit of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase stabilizes the tetramer in a conformation wherein only two active sites are capable of performing catalysis (oxidation of D-glyceraldehyde 3-phosphate or hydrolysis of p-nitrophenyl acetate). The modified enzyme exhibits half-of-the sites reactivity towards iodoacetate and iodoacetamide, known to be 'all-of-the-sites reagents' with the native enzyme. Evidence is presented supporting the model of a built-in asymmetry of the tetramer. The results obtained suggest that the arginine residue (probably Arg-231) controls the conformational transition between the asymmetric and symmetric states of the tetramer.
Nagradova
N K
NK
A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
Kuzminskaya
E V
EV
Asryants
R A
RA
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D005986:Glyceraldehyde 3-Phosphate / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D011487:Protein Conformation; D011817:Rabbits; D013329:Structure-Activity Relationship
D009243:NAD; D005986:Glyceraldehyde 3-Phosphate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases