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Dissection of Ammonium Uptake Systems inCorynebacterium glutamicum: Mechanism of Action and Energetics of AmtA and AmtB
Author(s) -
Britta Walter,
Melanie Küspert,
Daniel Ansorge,
Reinhard Krämer,
Andreas Burkovski
Publication year - 2008
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01896-07
Subject(s) - corynebacterium glutamicum , biology , biophysics , substrate (aquarium) , biochemistry , ammonium , gene , chemistry , ecology , organic chemistry
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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