Affiliation:
1. deBelle Laboratory for Biochemical Genetics, McGill University-Montreal Children's Hospital Research Institute, Montreal 108, Quebec, Canada
Abstract
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).
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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