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Journal of Bacteriology, April 2008, p. 2611-2614, Vol. 190, No. 7
0021-9193/08/$08.00+0 doi:10.1128/JB.01896-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstr. 5, 91058 Erlangen, Germany,1 Institut für Biochemie der Universität zu Köln, Zülpicher-Str. 47, 50674 Köln, Germany2
Received 4 December 2007/ Accepted 18 January 2008
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.
Published ahead of print on 1 February 2008.
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