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JB Accepts, published online ahead of print on 1 February 2008
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J. Bacteriol. doi:10.1128/JB.01896-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Dissection of ammonium uptake systems in Corynebacterium glutamicum: mechanism and energetics of AmtA and AmtB

Britta Walter, Melanie Küspert, Daniel Ansorge, Reinhard Krämer*, and Andreas Burkovski*

Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstr. 5, 91058 Erlangen, Germany; Institut für Biochemie der Universität zu Köln, Zülpicher-Str. 47, 50674 Köln, Germany

* To whom correspondence should be addressed. Email: r.kraemer{at}uni-koeln.de. aburkov{at}biologie.uni-erlangen.de.


  Abstract

Corynebacterium glutamicum has two different Amt-type proteins. While AmtB has a low substrate affinity and is not saturable up to 3 mM methylammonium, AmtA has a high substrate affinity and mediates saturable, membrane potential-dependent transport, resulting in a high steady-state accumulation of methylammonium even in the absence of metabolic trapping.




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