Affiliation:
1. Department of Bacteriology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel
Abstract
Spermine inhibited the transport of neutral aliphatic amino acids (valine, leucine, isoleucine, alanine, and glycine) into cells of
Micrococcus lysodeikticus
. On the other hand, spermine did not affect the uptake of basic (arginine and histidine), acidic (glutamic acid), or aromatic (phenylalanine and tyrosine) amino acids. Inhibition of uptake of the neutral amino acids by spermine is apparently of a noncompetitive nature; the
V
max
decreased, whereas the apparent
K
m
remained unaltered. The inhibition is most likely due to a specific binding of spermine to the carrier(s) of these amino acids. Related polyamines, spermidine and cadaverine, also caused inhibition of valine uptake, though to a lesser extent; spermidine was less active than spermine, and cadaverine showed the weakest effect of all. Valine, leucine, and isoleucine were transported into
M. lysodeikticus
cells by a common carrier as evidenced from competition experiments. The uptake of these amino acids is an active process; it was temperature-dependent and inhibited by azide (10
−1
m
to 2.5 × 10
−2
m
) and dinitrophenol (10
−3
m
). The intracellular concentration of valine was 100-fold higher than in the medium.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
3 articles.
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