Chludzinski A M, Salter D S, Nasser D
J Bacteriol. 1972 Mar;109(3):1162-9. doi: 10.1128/jb.109.3.1162-1169.1972.
A marine bacterium, Vibrio MB22, has been studied to determine the pattern of feedback regulation of the first enzyme unique to the biosynthesis of the aromatic amino acids, 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAHP) synthetase. The crude extract was used to study response of the enzyme to various salts as well as possible feedback inhibitors. Ethylenediaminetetraacetic acid was found to be inhibitory to enzyme activity, and only CoCl(2), of the salts tested, allowed full recovery as well as apparent stimulation of the DAHP synthetase activity. The DAHP synthetase activity was inhibited solely by the aromatic amino acids, tyrosine, tryptophan, and phenylalanine, of the possible effectors tested. Further work demonstrated the existence of three isozymes of DAHP synthetase, each primarily inhibited by one of the aromatic amino acids.
对一种海洋细菌——弧菌MB22进行了研究,以确定芳香族氨基酸生物合成中特有的第一种酶,即3-脱氧-D-阿拉伯庚酮糖酸7-磷酸(DAHP)合成酶的反馈调节模式。用粗提取物研究该酶对各种盐以及可能的反馈抑制剂的反应。发现乙二胺四乙酸对酶活性有抑制作用,在所测试的盐中,只有CoCl₂能使DAHP合成酶活性完全恢复并明显受到刺激。在所测试的可能效应物中,DAHP合成酶活性仅受到芳香族氨基酸酪氨酸、色氨酸和苯丙氨酸的抑制。进一步的研究表明存在三种DAHP合成酶同工酶,每种同工酶主要受到一种芳香族氨基酸的抑制。