Inhibition and inactivation of liver aldolase

Abstract

Substrate analogs xylulose 1,5-bisphosphate, glucitol 1,6-bisphosphate, alpha-2,5-anhydroglucitol 1,6-bisphosphate, alpha-, beta-methyl fructofuranoside 1,6-bisphosphate, ribulose 1,5-bisphosphate, ribulose 5-phosphate, and ribose 5-phosphate and inactivating agents 1-chloro-2, 4-dinitrobenzene, 4-hydroxymercuribenzoate, and pyridoxal phosphate were examined for their effects on liver aldolase. These studies support the use of the beta-anomer and acyclic form as substrate. They also suggest that the liver enzyme active site is similar to the muscle enzyme but with a much weaker 6-phosphate binding site.