The Participation of an Enzyme-bound Oxygen Group in a Coenzyme A Transferase Reaction

A well supported mechanism for succinyl-CoA:3-ketoacid coenzyme A transferase (EC 2.8.3.5) involving an enzyme-CoA intermediate requires the participation of an oxygen atom of the enzyme or of the CoA moiety. Measurements of loss of 18 O from acetoacetate show that CoA oxygens do not participate. An...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of biological chemistry Vol. 244; no. 9; pp. 2366 - 2371
Main Authors Benson, R W, Boyer, P D
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 10.05.1969
Subjects
Acetoacetates
Anhydrides
Binding Sites
Chemical Phenomena
Chemistry
Coenzyme A
Keto Acids
Oxidation-Reduction
Oxygen Isotopes
Succinates
Transferases - isolation & purification
Online AccessGet full text

Cover

More Information
Summary:A well supported mechanism for succinyl-CoA:3-ketoacid coenzyme A transferase (EC 2.8.3.5) involving an enzyme-CoA intermediate requires the participation of an oxygen atom of the enzyme or of the CoA moiety. Measurements of loss of 18 O from acetoacetate show that CoA oxygens do not participate. An oxygen-containing group on the enzyme is reversibly labeled from succinate- 18 O in the presence of acetoacetyl-CoA or succinyl-CoA. The 18 O-labeled enzyme does not contain succinyl or CoA moieties. A binding of acetoacetate- 14 C to the enzyme preparation does not appear to reflect an anhydride precursor to the enzyme-CoA form.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)78234-9