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. 1970 Nov;104(2):857–863. doi: 10.1128/jb.104.2.857-863.1970

Neutral Amino Acid Transport in Pseudomonas fluorescens

P Hechtman a,1, C R Scriver a
PMCID: PMC285069  PMID: 5489439

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).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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