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- W1975926271 abstract "Abstract 1. 1. Chemical modification of fatty acid synthetase, an enzyme which catalyzes seven different reactions, with phenylglyoxal (an arginine specific reagent) preferentially inhibited the ketoacyi and enoyl reductase activities and consequently the overall activity of the enzyme, 2. 2. NADP and analogs containing the 2'-phosphate protected both reductases and the overall activity of the enzyme from inactivation by phenylglyoxal suggesting that an arginine residue interacts with the 2'-phosphate of NADPH at the active site of the two reductase domains. 3. 3. Pyridoxal-5'-phosphate, by forming a Schiff base with a lysine(s), inactivated the overall activity of fatty acid synthetase by specifically inactivating the enoyl reductase component of the enzyme. 4. 4. Protection of the enzyme activities against Pyridoxal-5'-phosphate inhibition by NADP analogs strongly suggested that in the active site of enoyl reductase the ϵ-amino group of a lysine residue interacts with the pyrophosphoryl bridge of NADPH." @default.
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- W1975926271 date "1980-01-01" @default.
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- W1975926271 title "Selective chemical modification of the active sites of the ketoacyl reductase and enoyl reductase of fatty acid synthetase from lactating rat mammary glands" @default.
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- W1975926271 doi "https://doi.org/10.1016/0020-711x(80)90011-7" @default.
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