Open AccessKinetic properties of yeast lysine permeases coded by genes on multi‐copy vectors
Author(s) -
Sychrová Hana,
Matějčková Alena,
Kotyk Arnošt
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06487.x
Subject(s) - permease , lysine , yeast , saccharomyces cerevisiae , biochemistry , chemistry , substrate (aquarium) , membrane , transporter , gene , biophysics , biology , amino acid , ecology
Abstract Amplification of the LYP1 transport system in the plasma membrane of Saccharomyces cerevisiae did not change the substrate specificity, the affinity and the pH optimum of the transport system for lysine, but significantly increased the uptake velocity and accumulation ratio. The dependence of active lysine uptake and accumulation on pH is probably given by the properties of the permease itself rather than by the value of available protonmotive force.