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PubMed · 8816077

Function, structure and evolution of fructose-1,6-bisphosphatase.

F Marcus·J Rittenhouse·B Gontero·P B Harrsch
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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.

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Amino Acid SequenceAnimalsBacterial ProteinsConsensus SequenceCyclic AMPEnzyme ActivationEvolution, MolecularFructose-BisphosphataseFructosediphosphatesFructosephosphatesFungal ProteinsGluconeogenesisMolecular Sequence DataPlant ProteinsSequence AlignmentSequence Homology, Amino AcidSpecies SpecificityStructure-Activity RelationshipComparative StudyJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.Review

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F Marcus, J Rittenhouse, B Gontero, P B Harrsch. 1987. Function, structure and evolution of fructose-1,6-bisphosphatase.. https://pubmed.ncbi.nlm.nih.gov/8816077/

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