Ambler R P, Auffret A D, Clarke P H
FEBS Lett. 1987 May 11;215(2):285-90. doi: 10.1016/0014-5793(87)80163-1.
Amino acid sequence studies show that the aliphatic amidase (EC 3.5.1.4) from Pseudomonas aeruginosa PAC142 consists of a single polypeptide chain of 346 residues, giving an Mr of 38,400. The evidence from the amino acid studies is in complete agreement with that deduced from the DNA sequence of the amiE gene. Studies of the protein from Pseudomonas putida A87 show that it differs from the Ps. aeruginosa protein by about 30 amino acid substitutions. It now becomes possible to relate changes in the enzyme which result in altered specificity to structural changes in the protein.
氨基酸序列研究表明,铜绿假单胞菌PAC142的脂肪族酰胺酶(EC 3.5.1.4)由一条346个残基的单多肽链组成,Mr为38,400。氨基酸研究的证据与从amiE基因的DNA序列推导出来的结果完全一致。恶臭假单胞菌A87的蛋白质研究表明,它与铜绿假单胞菌的蛋白质约有30个氨基酸替换不同。现在有可能将导致特异性改变的酶的变化与蛋白质的结构变化联系起来。