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. 1987 Sep;84(17):6093–6097. doi: 10.1073/pnas.84.17.6093

Arginine transport in Streptococcus lactis is catalyzed by a cationic exchanger.

A J Driessen, B Poolman, R Kiewiet, W Konings
PMCID: PMC299014  PMID: 2819865

Abstract

Streptococcus lactis metabolizes arginine via the arginine deiminase pathway to ornithine, CO2, NH3, and ATP. The translocation of arginine and ornithine has been studied using membrane vesicles of galactose/arginine-grown cells of S. lactis fused with cytochrome c oxidase proteoliposomes by the freeze/thaw--sonication procedure earlier described. In the presence of reduced cytochrome c the fused membranes rapidly accumulate ornithine. Addition of arginine releases accumulated ornithine. Rapid uncoupler-insensitive exchange between external arginine and internal ornithine is seen at rates that are at least 60-fold higher than the rate of protonmotive force-driven arginine translocation. This arginine:ornithine exchange activity was reconstituted in proteoliposomes after solubilization of S. lactis membranes with octyl beta-D-glucopyranoside. These proteoliposomes catalyze a one-to-one exchange between arginine and ornithine. The arginine:ornithine exchange system is the first exchange system for cationic metabolites found in bacteria. Translocation of arginine via this system does not require metabolic energy obtained by arginine metabolism.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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