Affiliation:
1. Department of Food Science and Technology, University of California, Davis, California
Abstract
Harvey
, R. J. (University of California, Davis)
and E. B. Collins
. Role of citritase in acetoin formation by
Streptococcus diacetilactis
and
Leuconostoc citrovorum
. J. Bacteriol.
82:
954–959. 1961.—Cell-free extracts of
Streptococcus diacetilactis
and
Leuconostoc citrovorum
converted citrate to acetate, oxalacetate, pyruvate, carbon dioxide, and acetoin. The products, stoichiometry, and cofactor requirements of the citrate-splitting reaction were identical to those reported for citritase. Coenzyme A was not required; the reaction was stimulated by magnesium or manganous ions, and inhibited by calcium ions. In
S. diacetilactis
the enzyme is constitutive; it has been found inducible in all other organisms that have been studied. Ten strains of
S. diacetilactis
, three strains of
Leuconostoc
, and one strain of
S. liquefaciens
contained the enzyme; 21 strains of
S. cremoris
and 3 strains of
S. lactis
did not. Cell-free extracts of
S. diacetilactis
and
L. citrovorum
converted pyruvate to acetoin and carbon dioxide in the presence of manganous ions and thiamine pyrophosphate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference31 articles.
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4. Coenzyme A dependence and acetyl donor function of the pyruvate-formate exchange system;CHANTRENNE H.;J. Biol. Chem.,1950
5. Formation of diacetyl and acetoin by certain starter organisms;COLLINS E. B.;Milchwissenschaft,1959
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