Tso J Y, Hermodson M A, Zalkin H
J Biol Chem. 1980 Feb 25;255(4):1451-7.
The amino acid sequence of anthranilate synthase component II (AS II) from Serratia marcescens was determined. The cysteine residue essential for glutamine utilization was alkylated selectively by iodo [1-14C]acetamide prior to separation of the two protein components of anthranilate synthase. The isolated AS II then was subjected to cleavage by cyanogen bromide and by trypsin after citraconylation to obtain overlapping fragments. AS II is a single polypeptide chain of 192 residues having a calculated molecular weight of 20,956. The active site region is virtually identical to that of the Pseudomonas putida AS II enzyme (Kawamura, M., Keim, P.S., Goto, Y., Zalkin, H., and Heinrikson, R.L. (1978) J. Biol. Chem. 253, 4659-4668). Overall amino acid sequence similarity is 43%.
测定了粘质沙雷氏菌邻氨基苯甲酸合酶组分II（AS II）的氨基酸序列。在分离邻氨基苯甲酸合酶的两种蛋白质组分之前，用碘代[1-¹⁴C]乙酰胺选择性地烷基化了对谷氨酰胺利用至关重要的半胱氨酸残基。然后将分离得到的AS II在柠康酰化后用溴化氰和胰蛋白酶进行切割，以获得重叠片段。AS II是一条由192个残基组成的单多肽链，计算分子量为20,956。其活性位点区域与恶臭假单胞菌AS II酶的活性位点区域几乎相同（川村，M.，凯姆，P.S.，后藤，Y.，扎尔金，H.，和海因里克森，R.L.（1978年）《生物化学杂志》253，4659 - 4668）。整体氨基酸序列相似性为43%。
