Amino Acid Transport in Mycobacterium smegmatis
AUTOR(ES)
Yabu, Kunihiko
RESUMO
The transport of d-alanine, d-glutamic acid, and d-valine in Mycobacterium smegmatis was compared quantitatively with that of their l-isomers. It appeared that the uptake of d-alanine was mediated by an active process displaying saturation kinetics characteristic of enzyme function, whereas the uptake of d-glutamic acid was accomplished by a passive process showing diffusion kinetics. Both processes were involved in the uptake of l-alanine, l-glutamic acid, d-valine, and l-valine. d-Valine competed with l-valine for entry into the cell through a single active process. d-Alanine and l-alanine also utilized the same active process, but the d-isomer could not enter the cell through the passive process. The passive process exhibited characteristics of diffusion, but was sensitive to sulfhydryl-blocking reagents and showed competition among structurally related amino acids. These last findings suggested that the passive process is a facilitated diffusion.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=284962Documentos Relacionados
- A Mutant of Mycobacterium smegmatis Defective in Dipeptide Transport
- Iron transport in Mycobacterium smegmatis: Uptake of iron from ferric citrate.
- Ethambutol-Mediated Alterations in Ribonucleic Acid Components of Mycobacterium smegmatis
- Amino Acid Transport in Mycoplasma
- Heterogeneity of deoxyribonucleic acid molecules isolated from Mycobacterium smegmatis.
