Evidence for Succinyl Phosphate as an Enzyme-bound Intermediate in the Reaction Catalyzed by Succinyl Coenzyme A Synthetase

Jonathan S. Nishimura, Alton Meister

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

When purified succinyl coenzyme A synthetase from Escherichia coli was incubated with [I4C]succinyl phosphate and coenzyme A, [14C]succinyl coenzyme A was formed. Incubation of the enzyme with [32P]succinyl phosphate and adenosine 5'-diphosphate led to adenosine 5 '-triphosphate (ATP) synthesis. When the enzyme was incubated with [y-32P]ATP and succinate evidence was obtained for synthesis of succinyl phosphate, which was separated and identified by paper electrophoresis. Evidence that the enzyme is phosphorylated by succinyl phosphate was also obtained. The data support the conclusion that enzyme-bound succinyl phosphate is an intermediate in the reaction.

Original languageEnglish (US)
Pages (from-to)1457-1462
Number of pages6
JournalBiochemistry
Volume4
Issue number7
DOIs
StatePublished - Jul 1 1965
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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