恶臭假单胞菌
生物
色氨酸
生物化学
色氨酸合酶
酶
大肠杆菌
丝氨酸
假单胞菌
氨基酸
脱氨基
蛋白质亚单位
细菌
微生物学
遗传学
基因
作者
Toshio Enatsu,Irving P. Crawford
标识
DOI:10.1128/jb.108.1.431-438.1971
摘要
The two protein components of Pseudomonas putida tryptophan synthetase have been purified to homogeneity. Although there is general similarity between the Pseudomonas enzyme and that of the enteric bacteria, many differences were found. Components from Escherichia coli and P. putida do not stimulate each other enzymatically, and the enzymes differ in their response to monovalent cations. Serine deamination occurs best with the intact enzyme of P. putida , not with the β 2 subunit alone as in E. coli . The amino acid compositions of the α subunits differ appreciably. These findings extend earlier studies showing differences between enteric organisms and pseudomonads in the regulation and genetic organization of the enzymes of the tryptophan pathway.
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