Physiological function of the maltose operon regulator, MalR, in Lactococcus lactis.

ABSTRACT:

Background

Maltose metabolism is initiated by an ATP-dependent permease system in Lactococcus lactis. The subsequent degradation of intracellular maltose is performed by the concerted action of Pi-dependent maltose phosphorylase and beta-phosphoglucomutase. In some Gram-positive bacteria, maltose metabolism is regulated by a maltose operon regulator (MalR), belonging to the LacI-GalR family of transcriptional regulators. A gene presumed to encode MalR has been found directly downstream the maltose phosphorylase-encoding gene, malP in L. lactis. The purpose of this study was to investigate the physiological role of the MalR protein in maltose metabolism in L. lactis.

Results

A L. lactis ssp. lactis mutant, TMB5004, deficient in the putative MalR protein, was physiologically c

SUBMITTER: Andersson U 

PROVIDER: S-EPMC130022 | biostudies-literature | 2002 Sep

REPOSITORIES: biostudies-literature