Israeli E, Kalra V K, Brodie A F
J Bacteriol. 1977 May;130(2):729-35. doi: 10.1128/jb.130.2.729-735.1977.
On the basis of mutual inhibition of uptake with different amino acids in whole cells of Mycobacterium phlei, it was demonstrated that the binding site of proline was different from those of all other amino acids studied. Other groups of amino acids share a common binding site: lysine, histidine, and arginine; valine, leucine, and isoleucine; tryptophan, tyrosine, and phenylalanine; glutamic acid and aspartic acid. The exit and entry processes were studied for proline, glutamine, and glutamic acid. It was observed that in each case the entry and exit processes were mediated by different membrane sites.
基于草分枝杆菌全细胞中不同氨基酸对摄取的相互抑制作用,已证明脯氨酸的结合位点与所研究的所有其他氨基酸的结合位点不同。其他氨基酸组共享一个共同的结合位点:赖氨酸、组氨酸和精氨酸;缬氨酸、亮氨酸和异亮氨酸;色氨酸、酪氨酸和苯丙氨酸;谷氨酸和天冬氨酸。对脯氨酸、谷氨酰胺和谷氨酸的进出过程进行了研究。观察到在每种情况下,进出过程均由不同的膜位点介导。