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- W2171530023 abstract "Some kinetic properties of the formation of a thioester-bound l -seryl-enzyme intermediate are described. The rate constant of formation is 3.12 × 10 2 M −1 s −1 and the rate constant for spontaneous breakdown is 2.47 × 10 −3 s −1 . These constants yield a value of log K = 5.10 for the overall equilibrium constant which agrees favorably with a value of 5.20 calculated from equilibrium binding data. E 1 ·serine formation requires a thiol group which is extremely reactive to N -ethylmaleimide; the second-order rate constant for enzyme inactivation by this reagent is 77.1 M −1 s −1 at pH 6.6 and 0 C. Excess l -serine does not protect the enzyme against inactivation. In addition to an adenosine triphosphate-[ 32 P]-inorganic pyrophosphate exchange, the enzyme also catalyzes an l -serine-dependent adenosine triphosphate-[ 3 H]adenosine monophosphate exchange in accordance with the scheme proposed for the activation of serine." @default.
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- W2171530023 date "1973-11-01" @default.
- W2171530023 modified "2023-09-27" @default.
- W2171530023 title "Studies on the Enzymes Involved in the Biosynthesis of Cyclo-Tris ( N -2,3-Dihydroxybenzoyl- l -Seryl) in Escherichia coli : Kinetic Properties of the l -Serine–Activating Enzyme" @default.
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- W2171530023 doi "https://doi.org/10.1128/jb.116.2.790-796.1973" @default.
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