Studies on the topographical localization of the binding sites for substrate and for actin on the enzymes, glyceraldehydephosphate dehydrogenase and phosphofructokinase.
The effect of proteolysis on the catalytic activity and the binding capacity for actin has been studied in the case of both glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphofructokinase (PFK). With both of these enzymes, the differential response of these two parameters is interpreted as an indication of the distinct topographical separation of the active sites and binding sites. These results have been discussed in relation to the positioning of the catalytic and binding sites on these enzymes, the nature of their interaction with actin, their relative stability in cellular situations and the phenomenon of enzyme ambiguity.
D000199:Actins / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D002918:Chymotrypsin; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis*; D010732:Phosphofructokinase-1 / Q000032:analysis*; D014357:Trypsin
D000199:Actins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010732:Phosphofructokinase-1; D002918:Chymotrypsin; D014357:Trypsin