Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates

William W. Farrar, Kent Plowman

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.

Original languageEnglish (US)
Pages (from-to)537-542
Number of pages6
JournalInternational Journal of Biochemistry
Volume6
Issue number8
DOIs
StatePublished - Jan 1 1975

Fingerprint

Acetate-CoA Ligase
Electronic data interchange
Coenzyme A
Acetates
Adenosine Triphosphate
Kinetics
Substrates
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates. / Farrar, William W.; Plowman, Kent.

In: International Journal of Biochemistry, Vol. 6, No. 8, 01.01.1975, p. 537-542.

Research output: Contribution to journalArticle

Farrar, William W. ; Plowman, Kent. / Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates. In: International Journal of Biochemistry. 1975 ; Vol. 6, No. 8. pp. 537-542.
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