Regulation of Pyruvate Carboxylase by Coenzyme A and Acyl Coenzyme A Thio Esters

Terrance Cooper, C. R. Benedict

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Pyruvate carboxylase has been purified 235-fold from dried baker’s yeast. Like pyruvate carboxylase from a variety of other sources the purified enzyme from yeast is stimulated by acetyl coenzyme A. Unlike other documented systems, the yeast enzyme is stimulated by coenzyme A, acetoacetyl coenzyme A, palmityl coenzyme A, pantethine, and adenosine 3′,5′-cyclic phosphate. A partial explanation of the stimulation of yeast pyruvate carboxylase by coenzyme A and acyl thio esters is that these compounds specifically lower the Km for bicarbonate. In addition to the unique effector specificity, the yeast carboxylase also differs from vertebrate organ carboxylases in the kinetics of effector binding. Typical Michaelis-Menten kinetics are observed in a plot of reaction velocity vs. effector concentration. In vertebrate carboxylase preparations a similar plot has yielded higher order nonlinear kinetics. These data indicate major differences between the yeast and vertebrate organ pyruvate carboxylases.

Original languageEnglish (US)
Pages (from-to)3032-3036
Number of pages5
JournalBiochemistry
Volume7
Issue number9
DOIs
StatePublished - Sep 1 1968
Externally publishedYes

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Pyruvate Carboxylase
Acyl Coenzyme A
Coenzyme A
Yeast
Esters
Yeasts
Vertebrates
Dried Yeast
Kinetics
Acetyl Coenzyme A
Enzymes
Bicarbonates
Adenosine
Saccharomyces cerevisiae
Phosphates

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Regulation of Pyruvate Carboxylase by Coenzyme A and Acyl Coenzyme A Thio Esters. / Cooper, Terrance; Benedict, C. R.

In: Biochemistry, Vol. 7, No. 9, 01.09.1968, p. 3032-3036.

Research output: Contribution to journalArticle

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