PMID:348198

Citation	Baldwin, SA and Perham, RN (1978) Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain). Biochem. J. 169:643-52
Abstract	Investigation of aldolase 1, the class-I D-fructose 1,6-bisphosphate aldolase (EC4.1.2.13) from Escherichia coli (Crookes' strain), showed it to have unusual kinetic and structural properties. The enzyme appeared to be larger than was previously supposed and may be a decamer with a mol. wt. of approx. 340000. Its fructose 1,6-bisphosphate-cleavage activity was unaffected by these compounds. The enhancement exhibited a strong dependence on pH. These novel kinetic properties do not seem to be shared by any other fructose 1,6-bisphosphate aldolase, but recall the activation by polycarboxylic acids of the deoxyribose 3-phosphate aldolases from some other organisms. In view of its unusual properties, it is unlikely that aldolase 1 from E. coli is closely related to the class-1 aldolases that have been detected in several other prokaryotes, or to the typical class-1 enzymes from eukaryotes.
Links	PubMed PMC1183837
Keywords	Amino Acids/analysis; Chemical Phenomena; Chemistry; Citrates/pharmacology; Escherichia coli/enzymology; Fructose-Bisphosphate Aldolase/immunology; Fructose-Bisphosphate Aldolase/isolation & purification; Fructose-Bisphosphate Aldolase/metabolism; Kinetics; Molecular Weight; Phosphoenolpyruvate/pharmacology; Protein Conformation
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