Studies on the catalytic mechanism of Escherichia coli succinic thiokinase

Frederick Grinnell, Jonathan S. Nishimura

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)4126-4130
Number of pages5
JournalBiochemistry
Volume8
Issue number10
StatePublished - 1969

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Succinate-CoA Ligases
Escherichia coli
Succinic Acid
Enzymes
Adenosine Triphosphate
Coenzyme A Ligases
Coenzyme A
Adenosine Diphosphate
succinyl phosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Studies on the catalytic mechanism of Escherichia coli succinic thiokinase. / Grinnell, Frederick; Nishimura, Jonathan S.

In: Biochemistry, Vol. 8, No. 10, 1969, p. 4126-4130.

Research output: Contribution to journalArticle

Grinnell, Frederick ; Nishimura, Jonathan S. / Studies on the catalytic mechanism of Escherichia coli succinic thiokinase. In: Biochemistry. 1969 ; Vol. 8, No. 10. pp. 4126-4130.
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