[Comparative study of glyceraldehyde-3-phosphate dehydrogenases isolated from rabbit skeletal muscles and baker's yeast using cationic fluorescent probes].
The tetrameric molecule of glyceraldehyde-3-phosphate dehydrogenase possesses the ability to bind fluorescent probes of cationic nature (auramine O and acridine orange) outside the active center. The rabbit skeletal muscle and yeast enzymes share some common features, e.g., the conformational non-equivalency of subunits; two subunits per tetramer can bind auramine O; conformational changes caused by the binding of adenyl mononucleotides and involving the microenvironment of auramine O binding sites; the ability to bind the cationic probe at pH values typical for the maximal activity of the enzyme in the reaction of glyceraldehyde 3-phosphate oxidation. The yeast and rabbit muscle enzymes are distinguished in terms of localization of the probe binding sites with respect to the active center and/or in the nature of conformational changes induced by NAD+ binding. It was demonstrated that nicotinamide mononucleotide may serve as a co-enzyme in glyceraldehyde 3-phosphate oxidation catalyzed by yeast dehydrogenase; this reaction in inhibited by AMP.
D000165:Acridine Orange; D000818:Animals; D001576:Benzophenoneidum; D001665:Binding Sites; D005456:Fluorescent Dyes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005456:Fluorescent Dyes; D001576:Benzophenoneidum; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D000165:Acridine Orange
Sravnitel'noe issledovanie glitseral'degid-3-fosfatdegidrogenaz, izolirovannykh iz skeletnykh myshts krolika i iz pekarskikh drozhzheĭ, s pomoshch'iu fluorestsentnykh zondov kationnoĭ prirody.