Remarks on the supramolecular organization of the glycolytic system in vivo.
The great latent catalytic capacity, manifested at the extremely high intracellular concentrations and in large apparent kcat/Km values, of the glycolytic enzymes on the one hand and their tendency in experiments in vitro to form functionally-specific flux-enhancing (channeling) complexes on the other, is considered and discussed as an apparent discrepancy. A random association of glycolytic enzymes in vivo is probable.
Batke
J
J
Institute of Enzymology, Hungarian Academy of Sciences, Budapest.
D000818:Animals; D002384:Catalysis; D003593:Cytoplasm / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006019:Glycolysis; D008954:Models, Biological; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D005993:Glycerolphosphate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase