PMID:417719
| Citation |
Baldwin, SA, Perham, RN and Stribling, D (1978) Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain). Biochem. J. 169:633-41 |
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| Abstract |
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. |
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| Keywords |
Amino Acids/analysis; Chemical Phenomena; Chemistry; Dimethyl Suberimidate/pharmacology; Escherichia coli/enzymology; Fructose-Bisphosphate Aldolase/immunology; Fructose-Bisphosphate Aldolase/isolation & purification; Fructose-Bisphosphate Aldolase/metabolism; Immunodiffusion; Kinetics; Molecular Weight; Sulfhydryl Compounds/pharmacology |
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