来自大肠杆菌K12的分支酸变位酶/预苯酸脱水酶的可溶性胰蛋白酶肽段的氨基酸序列。
Amino acid sequences of soluble tryptic peptides of chorismate mutase/prephenate dehydratase from Escherichia coli K12.
作者信息
Baldwin G S, Davidson B E
出版信息
Biochim Biophys Acta. 1979 Aug 28;579(2):483-6. doi: 10.1016/0005-2795(79)90078-3.
The amino acid sequences of 28 soluble tryptic peptides from chorismate mutase/prephenate dehydratase from Escherichia coli K12 have been determined. Together with the four unique cysteine-containing peptides sequenced by Gething and Davidson ((1976) Eur. J. Biochem. 71, 327-336) this accounts for approximately 75% of the total sequence expected for this protein. A high frequency of identify between some of the peptides suggests the possibility of gene duplication during the evolution of the structural gene for the enzyme.
已测定了来自大肠杆菌K12的分支酸变位酶/预苯酸脱水酶的28个可溶性胰蛋白酶肽段的氨基酸序列。加上由格辛和戴维森测定序列的4个独特的含半胱氨酸肽段（（1976年）《欧洲生物化学杂志》71卷，327 - 336页），这大约占该蛋白质预期总序列的75%。一些肽段之间的高同源性表明在该酶结构基因的进化过程中存在基因重复的可能性。
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