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- W1600233472 abstract "The pH 6 acetolactate-forming enzyme from Serratia marcescens has been purified to homogeneity, and some of its characteristics have been described. Cocarboxylase and manganese have been completely removed from the enzyme. The addition of FAD to the enzyme did not stimulate the formation of acetolactate, and no FAD was released from the enzyme after trichloro-acetic acid treatment. The enzyme did not crystallize as the same enzyme from Aerobacter aerogenes does, but the kinetic properties of the enzyme are similar. The pH optimum in acetate is 6.0, and the enzyme activity is inhibited by phosphate and sulfate. These compounds cause sigmoidal kinetics, and apparent Michaelis kinetics are observed in acetate." @default.
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- W1600233472 date "1970-05-01" @default.
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- W1600233472 title "The pH 6 Acetolactate-Forming Enzyme from Serratia marcescens. Purification and Properties" @default.
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- W1600233472 doi "https://doi.org/10.1111/j.1432-1033.1970.tb00269.x" @default.
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