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- W211535930 abstract "All vertebrate fructose 1,6-bisphosphatases studied were found to be susceptible to limited proteolysis by subtilisin or by an endogenous lysosomal proteinase. The amino acid sequence adjacent to the proteinase-sensitive region appears to be highly conserved, suggesting that proteolysis may play a critical role in the function of the enzyme. One possible function is release from inhibition by AMP. At pH 5.5 endogenous modification appears to be due to a specific lysosomal proteinase, which is distinct from cathepsins A, B, C or D. Susceptibility of rabbit liver Fru-P2ase to subtilisin can be employed to monitor ligand-induced changes in the conformation of the protein. This technique has provided evidence for an interaction between rabbit liver Fru-P2ase and rabbit liver aldolase, enzymes that catalyze successive steps in gluconeogenesis. The interaction is tissue-specific, and is not seen when either enzyme from liver is replaced by its muscle counterpart." @default.
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- W211535930 date "1980-01-01" @default.
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- W211535930 title "PARTIAL AMINO ACID SEQUENCE OF RABBIT LIVER FRUCTOSE 1,6-BISPHOSPHATASE (Fru-P2ase, EC 3.1.3.11) AND SITES OF CLEAVAGE BY PROTEINASES" @default.
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- W211535930 doi "https://doi.org/10.1016/b978-0-08-024417-4.50006-8" @default.
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