title: Function, structure and evolution of fructose-1,6-bisphosphatase.
abstract: 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 this short review, we have analyzed the function of several fructose-1,6-bisphosphatases and we have made a comparison of partial amino acid sequences obtained from the enzymes of the yeast Saccharomyces cerevisiae, Escherichia coli, and spinach chloroplasts with the known entire amino acid sequence of a mammalian gluconeogenic fructose-1,6-bisphosphatase. These results demonstrate a very high degree of sequence conservation, suggesting a common evolutionary origin for all fructose-1,6-bisphosphatases.
authors.affiliation: Department of Biological Chemistry and Structure, University of Health Sciences, Chicago Medical School, Illinois 60064, USA.
authors.forename: F
authors.initials: F
authors.lastname: Marcus
authors.forename: J
authors.initials: J
authors.lastname: Rittenhouse
authors.forename: B
authors.initials: B
authors.lastname: Gontero
authors.forename: P B
authors.initials: PB
authors.lastname: Harrsch
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D016384:Consensus Sequence; D000242:Cyclic AMP / Q000502:physiology; D004789:Enzyme Activation; D019143:Evolution, Molecular; D006597:Fructose-Bisphosphatase / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D005635:Fructosediphosphates / Q000378:metabolism; D005636:Fructosephosphates / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000502:physiology; D005943:Gluconeogenesis; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D005635:Fructosediphosphates; D005636:Fructosephosphates; D005656:Fungal Proteins; D010940:Plant Proteins; C027618:fructose-6-phosphate; D000242:Cyclic AMP; D006597:Fructose-Bisphosphatase; C029063:fructose-1,6-diphosphate