Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain).
A new form of the class-II D-fructose 1,6-bisphosphate aldolase (EC 4.1.2.13) of Escherichia coli (Crookes' strain) was isolated from an extract of glycerol-grown bacteria. It has a higher molecular weight (approx. 80000)than previous preparations of the enzyme and closely resembles the typical class-II aldolase from yeast in size and amino acid composition. On the other hand, its kinetic behaviour is not typical of a class-II aldolase. The enzyme has no requirement for thiol compounds either for stability or activity, added K+ ions have no effect, and the optimum pH for the cleavage activity is unusually high. The class-II enzymes from the prokaryote E. coli and the eukaryote yeast show no immunological identity. However, the similarity of their structures suggests that they have evolved from a common ancestor.
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D004120:Dimethyl Suberimidate / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D005779:Immunodiffusion; D007700:Kinetics; D008970:Molecular Weight; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D000596:Amino Acids; D013438:Sulfhydryl Compounds; D004120:Dimethyl Suberimidate; D005634:Fructose-Bisphosphate Aldolase