Alternate pathways of l-rhamnose transport in Arthrobacter pyridinolis

Susan L. Levinson, Terry A. Krulwich

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

Phosphoenolpyruvate: hexose phosphotransferase-negative mutants of Arthrobacterpyridinolis fail to grow on l-rhamnose. Although phosphoenolpyruvate: l-rhamnose phosphotransferase activity could not be consistently demonstrated in extracts of rhamnose-grown cells, low levels of phosphoenolpyruvate-dependent uptake of rhamnose were found using isolated membrane vesicles from rhamnose-grown cells. This uptake was not inhibited by uncoupling agents or an inhibitor of the respiratory chain. Phosphotransferase-negative mutants could grow on l-rhamnose if l-malate was also present in the medium. l-Malate- and succinate-dependent uptake of rhamnose was found in membrane vesicles. Either of the two oxidizable substrates caused a 5-fold stimulation of the rate of l-rhamnose uptake over that observed in the absence of additions. Malate-dependent l-rhamnose uptake had a Km for rhamnose of 2.9 × 10-6 m. It was inhibited by uncoupling agents, inhibitors of the respiratory chain, and sulfhydryl reagents.

Original languageEnglish
Pages (from-to)445-450
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume160
Issue number2
DOIs
StatePublished - Feb 1974
Externally publishedYes

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