Studies on the Catalytic Mechanism of Escherichia coli Succinic Thiokinase

Frederick Grinnell; Jonathan S. Nishimura

doi:10.1021/bi00838a033

Studies on the Catalytic Mechanism of Escherichia coli Succinic Thiokinase

Frederick Grinnell, Jonathan S. Nishimura

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Abstract

The coenzyme A analog, desulfocoenzyme A, does not significantly affect the rate of succinyl phosphate formation from phosphorylated succinic thiokinase (succinate:coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5). The effector action of desulfocoenzyme A seems to require the presence of adenosine triphosphate. Phosphoryl-enzyme is shown to be an intermediate in succinyl phosphate formation from adenosine triphosphate and succinate, and additional evidence is presented supporting the intermediary role of phosphoryl-enzyme in the over-all catalytic mechanism of the enzyme.

Original language	English (US)
Pages (from-to)	4126-4130
Number of pages	5
Journal	Biochemistry
Volume	8
Issue number	10
DOIs	https://doi.org/10.1021/bi00838a033
State	Published - Jan 1 1969

ASJC Scopus subject areas

Biochemistry

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abstract = "The coenzyme A analog, desulfocoenzyme A, does not significantly affect the rate of succinyl phosphate formation from phosphorylated succinic thiokinase (succinate:coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5). The effector action of desulfocoenzyme A seems to require the presence of adenosine triphosphate. Phosphoryl-enzyme is shown to be an intermediate in succinyl phosphate formation from adenosine triphosphate and succinate, and additional evidence is presented supporting the intermediary role of phosphoryl-enzyme in the over-all catalytic mechanism of the enzyme.",

author = "Frederick Grinnell and Nishimura, {Jonathan S.}",

year = "1969",

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AU - Grinnell, Frederick

AU - Nishimura, Jonathan S.

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N2 - The coenzyme A analog, desulfocoenzyme A, does not significantly affect the rate of succinyl phosphate formation from phosphorylated succinic thiokinase (succinate:coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5). The effector action of desulfocoenzyme A seems to require the presence of adenosine triphosphate. Phosphoryl-enzyme is shown to be an intermediate in succinyl phosphate formation from adenosine triphosphate and succinate, and additional evidence is presented supporting the intermediary role of phosphoryl-enzyme in the over-all catalytic mechanism of the enzyme.

AB - The coenzyme A analog, desulfocoenzyme A, does not significantly affect the rate of succinyl phosphate formation from phosphorylated succinic thiokinase (succinate:coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5). The effector action of desulfocoenzyme A seems to require the presence of adenosine triphosphate. Phosphoryl-enzyme is shown to be an intermediate in succinyl phosphate formation from adenosine triphosphate and succinate, and additional evidence is presented supporting the intermediary role of phosphoryl-enzyme in the over-all catalytic mechanism of the enzyme.

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Studies on the Catalytic Mechanism of Escherichia coli Succinic Thiokinase

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