Neutral Amino Acid Transport in Pseudomonas fluorescens
AUTOR(ES)
Hechtman, P.
RESUMO
Membrane transport of β-alanine, l-alanine, and l-proline was studied in a β-alanine transaminaseless mutant (strain 67) of Pseudomonas fluorescens. In this mutant β-alanine is metabolically inert, and it was therefore possible to demonstrate active transport of this substrate in the absence of intracellular catabolism. The permease which catalyzes the uptake of β-alanine also transports l-proline and l-alanine. This common transport system was distinguished from permeases which transport only l-alanine and only l-proline by competition studies in strain 67 and by studies of transport specificity in a permeaseless mutant (strain 67/4MTR).
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=285069Documentos Relacionados
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