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多拷贝载体上基因编码的酵母赖氨酸通透酶的动力学特性

Kinetic properties of yeast lysine permeases coded by genes on multi-copy vectors.

作者信息

Sychrová H, Matĕjcková A, Kotyk A

机构信息

Department of Membrane Transport, Institute of Physiology, Czech Academy of Sciences, Prague, Czech Republic.

出版信息

FEMS Microbiol Lett. 1993 Oct 1;113(1):57-61. doi: 10.1111/j.1574-6968.1993.tb06487.x.

DOI:10.1111/j.1574-6968.1993.tb06487.x
PMID:8243983
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.

摘要

酿酒酵母质膜中LYP1转运系统的扩增并未改变赖氨酸转运系统的底物特异性、亲和力和最适pH值,但显著提高了摄取速度和积累比率。赖氨酸的主动摄取和积累对pH的依赖性可能由通透酶本身的性质决定,而非由可用质子动力的值决定。

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