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- W97472787 abstract "Fructose-1,6-bisphosphatase, one of the key enzymes in gluconeogenesis, is activated and converted to an alkaline form by incubation with a protease, converting enzyme, obtained from the heavy particle fraction of rat liver. The converting enzyme is located in the lysosomes and is different from cathepsins A, B, C, and D. The cleavage pattern is complex, resulting in fragments of various molecular weights. Cleavage at Asn64- Val65 appears to be associated with the change in catalytic properties. In addition to being activated at alkaline pH, the converted enzyme is less susceptible to AMP inhibition. This is in agreement with the expected changes in the properties of the enzyme when it functions under gluconeogenic conditions." @default.
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- W97472787 date "1981-01-01" @default.
- W97472787 modified "2023-10-14" @default.
- W97472787 title "CONVERTING ENZYME OF FRUCTOSE-1,6-BISPHOSPHATASE FROM RAT LIVER" @default.
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- W97472787 doi "https://doi.org/10.1016/b978-0-08-027377-8.50011-7" @default.
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