Hillenga D J, Versantvoort H J, Driessen A J, Konings W N
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands.
J Bacteriol. 1996 Jul;178(14):3991-5. doi: 10.1128/jb.178.14.3991-3995.1996.
The characteristics of the basic amino acid permease (system VI) of the filamentous fungus Penicillium chrysogenum were studied in plasma membranes fused with liposomes containing the beef heart mitochondrial cytochrome c oxidase. In the presence of reduced cytochrome c, the hybrid membranes accumulated the basic amino acids arginine and lysine. Inhibition studies with analogs revealed a narrow substrate specificity. Within the external pH range of 5.5 to 7.5, the transmembrane electrical potential (delta psi) functions as the main driving force for uphill transport of arginine, although a low level of uptake was observed when only a transmembrane pH gradient was present. It is concluded that the basic amino acid permease is a H+ symporter. Quantitative analysis of the steady-state levels of arginine uptake in relation to the proton motive force suggests a H+-arginine symport stoichiometry of one to one. Efflux studies demonstrated that the basic amino acid permease functions in a reversible manner.
研究了丝状真菌产黄青霉基本氨基酸通透酶（系统VI）在与含有牛心线粒体细胞色素c氧化酶的脂质体融合的质膜中的特性。在还原型细胞色素c存在的情况下，杂种膜积累碱性氨基酸精氨酸和赖氨酸。用类似物进行的抑制研究揭示了狭窄的底物特异性。在外部pH值为5.5至7.5的范围内，跨膜电势（δψ）是精氨酸向上运输的主要驱动力，尽管当仅存在跨膜pH梯度时观察到低水平的摄取。得出的结论是，碱性氨基酸通透酶是一种H +同向转运体。对精氨酸摄取的稳态水平与质子动力的定量分析表明，H + -精氨酸同向转运化学计量比为1：1。流出研究表明，碱性氨基酸通透酶以可逆方式起作用。
