Amino acid sequence homology among fructose-1,6-bisphosphatases.
The hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate is a key reaction of carbohydrate metabolism. The enzyme that catalyzes this reaction, fructose-1,6-bisphosphatase, appears to be present in all forms of living organisms. Regulation of the enzyme activity, however, occurs by a variety of distinct mechanisms. These include AMP inhibition (most sources), cyclic AMP-dependent phosphorylation (yeast), and light-dependent activation (chloroplast). In the present studies, we have made a comparison of the primary structure of mammalian fructose-1,6-bisphosphatase with the sequence of peptides isolated from the yeast Saccharomyces cerevisiae, Escherichia coli, and spinach chloroplast enzymes. Our results demonstrate a high degree of sequence homology, suggesting a common evolutionary origin for all fructose-1,6-bisphosphatases.
D000595:Amino Acid Sequence; D000818:Animals; D002736:Chloroplasts / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000201:enzymology; D006597:Fructose-Bisphosphatase / Q000032:analysis* / Q000235:genetics; D010446:Peptide Fragments / Q000032:analysis; D010944:Plants; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013045:Species Specificity; D013552:Swine
D010446:Peptide Fragments; D006597:Fructose-Bisphosphatase