Studies on the Catalytic Mechanism of Escherichia coli Succinic Thiokinase

Frederick Grinnell, Jonathan S. Nishimura

Research output: Contribution to journalArticle

4 Scopus citations

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
DOIs
StatePublished - Jan 1 1969

ASJC Scopus subject areas

  • Biochemistry

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