Fluorescence studies on glyceraldehyde-3-phosphate dehydrogenase from bovine heart muscle.
Glyceraldehyde-3-phosphate dehydrogenase is a glycolytic enzyme that catalyses conversion of glyceraldehyde-3-phosphate to 1,3-diphosphoglycerate. ATP has been found to have an inhibitory effect on this enzyme. To establish the interaction between the enzyme and ATP, a fluorescence technique was used. Fluorescence quenching in the presence of ATP suggests cooperative binding of ATP to the enzyme (the Hill obtained coefficient equals 2.78). The interaction between glyceraldehyde-3-phosphate dehydrogenase and ATP may control not only glycolysis but other activities of this enzyme, such as binding to the cytoskeleton.
Seweryn
E
E
Wrocław Medical University, Department of Medical Biochemistry, Poland. ewaseweryn@yahoo.com
Banaś
T
T
Berdowska
I
I
Zieliński
B
B
Ceremuga
I
I
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D010210:Papillary Muscles / Q000201:enzymology; D013050:Spectrometry, Fluorescence
D000255:Adenosine Triphosphate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases