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PMID: 1657604 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Lysine excretion by Corynebacterium glutamicum. 2. Energetics and mechanism of the transport system.

European journal of biochemistry ·Vol. 202 ·No. 1 ·1991-11-15 ·Pages 137-43

Bröer S, Krämer R

Abstract

Lysine excretion in Corynebacterium glutamicum was characterized as secondary transport process. It is modulated by three forces: the membrane potential, the chemical potential of lysine, and the proton gradient. The ATP content of the cells did not correlate with the export activity. Lysine is excreted in symport with presumably two OH- ions which is not distinguishable experimentally from an antiport mechanism against two protons. The substrate-loaded carrier is uncharged. When the external substrate concentration is low and no proton gradient present, reorientation of the positively charged, unloaded carrier is rate-limiting. Export then depends on the membrane potential. When the external substrate is high, translocation of the loaded, uncharged carrier is rate-limiting, and export is not modulated by the membrane potential. The lysine secretion system in C. glutamicum is shown to be well adapted to the requirements of metabolite export.

MeSH Terms
Adenosine Triphosphate/metabolism Biological Transport, Active Carrier Proteins/metabolism Cell Membrane/metabolism Chemical Phenomena Chemistry, Physical Corynebacterium/metabolism Electrochemistry Hydrogen-Ion Concentration Lysine/metabolism Membrane Potentials Protons
Chemicals
Carrier Proteins Protons Adenosine Triphosphate Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bröer S
Institut für Biotechnologie I, Forschungszentrum Jülich, Federal Republic of Germany.
Krämer R
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1991-11-15
Pages
137-43
Language
English
Region
England
NLM ID
0107600
Subset
IM
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