Galactokinase activity in Streptococcus thermophilus.

Abstract:

:ATP-dependent phosphorylation of [14C]galactose by 11 strains of Streptococcus thermophilus indicated that these organisms possessed the Leloir enzyme, galactokinase (galK). Activities were 10 times higher in fully induced, galactose-fermenting (Gal+) strains than in galactose-nonfermenting (Gal-) strains. Lactose-grown, Gal- cells released free galactose into the medium and were unable to utilize residual galactose or to induce galK above basal levels. Gal+ S. thermophilus 19258 also released galactose into the medium, but when lactose was depleted growth on galactose commenced, and galK increased from 0.025 to 0.22 micromol of galactose phosphorylated per min per mg of protein. When lactose was added to galactose-grown cells of S. thermophilus 19258, galK activity rapidly decreased. These results suggest that galK in Gal+ S. thermophilus is subject to an induction-repression mechanism, but that galK cannot be induced in Gal- strains.

journal_name

Appl Environ Microbiol

authors

Hutkins R,Morris HA,McKay LL

doi

10.1128/AEM.50.4.777-780.1985

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

777-80

issue

4

eissn

0099-2240

issn

1098-5336

journal_volume

50

pub_type

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