Dissection of ammonium uptake systems in Corynebacterium glutamicum: mechanism of action and energetics of AmtA and AmtB.
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.
Walter
Britta
B
Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstr. 5, 91058 Erlangen, Germany.
Küspert
Melanie
M
Ansorge
Daniel
D
Krämer
Reinhard
R
Burkovski
Andreas
A
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D001692:Biological Transport; D027682:Cation Transport Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D002855:Chromatography, Thin Layer; D048230:Corynebacterium glutamicum / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008744:Methylamines / Q000378:metabolism / Q000493:pharmacokinetics; D009154:Mutation; D000644:Quaternary Ammonium Compounds / Q000378:metabolism* / Q000493:pharmacokinetics; D013379:Substrate Specificity
D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D008744:Methylamines; D000644:Quaternary Ammonium Compounds; C027451:methylamine