The aldolase-substrate intermediates and their interaction with glyceraldehyde-3-phosphate dehydrogenase in a reconstructed glycolytic system.
The relative concentration of the aldolase x fructose-bisphosphate and of the aldolase x dihydroxy-acetone-phosphate complexes is regulated, in the steady state, by the nature of the accompanying glycolytic enzymes. Particularly in the presence of triose phosphate isomerase, the aldolase x dihydroxyactone-phosphate complexes are largely prevalent. This situation is very likely to hold in rabbit muscle in vivo. Aldolase and gyceraldehyde-3-phosphate dehydrogenase slowly form a complex; however, no evidence has been found for the direct transfer of glyceraldehyde 3-phosphate between the two enzymes.
D000818:Animals; D004099:Dihydroxyacetone Phosphate / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006019:Glycolysis; D011817:Rabbits; D013379:Substrate Specificity; D014305:Triose-Phosphate Isomerase / Q000378:metabolism
D004099:Dihydroxyacetone Phosphate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase; D014305:Triose-Phosphate Isomerase