Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase

Henry M. Miziorko, David R Shortle, M. Daniel Lane

Research output: Contribution to journalArticle

Abstract

By controlling conditions which affect the relative rates of the partial reactions in HMG-CoA synthesis, it has been possible to trap and partially characterize HMG (-SCoA)-S-enzyme, the postulated central intermediate in catalysis. At -25° in 25% ethanol, the breakdown of HMG (-SCoA)-S-enzyme to HMG-SCoA and HS-enzyme is slowed relative to its rate of formation from acetoacetyl-SCoA and acetyl-S-enzyme. Under these conditions label from acetoacetyl-S[3H]CoA or [14C]acetyl-S-enzyme can be trapped in the accumulated intermediate with [14C] activity appearing in the HMG moiety.

Original languageEnglish (US)
Pages (from-to)92-98
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume69
Issue number1
DOIs
StatePublished - Mar 8 1976

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Coenzymes
Enzymes
Coenzyme A
Catalysis
Labels
Ethanol
3-hydroxy-3-methylglutaryl-coenzyme A

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase. / Miziorko, Henry M.; Shortle, David R; Lane, M. Daniel.

In: Biochemical and Biophysical Research Communications, Vol. 69, No. 1, 08.03.1976, p. 92-98.

Research output: Contribution to journalArticle

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