DD-肽酶的作用机制：酪氨酸-159在链霉菌R61 DD-肽酶中的作用。
The mechanism of action of DD-peptidases: the role of tyrosine-159 in the Streptomyces R61 DD-peptidase.
作者信息
Wilkin J M, Jamin M, Damblon C, Zhao G H, Joris B, Duez C, Frère J M
机构信息
Centre d'Ingéniérie des protéines, Université de Liège, Belgium.
出版信息
Biochem J. 1993 Apr 15;291 ( Pt 2)(Pt 2):537-44. doi: 10.1042/bj2910537.
Abstract
Tyrosine-159 of the Streptomyces R61 penicillin-sensitive DD-peptidase was replaced by serine or phenylalanine. The second mutation yielded a very poorly active protein whose rate of penicillin binding was also drastically decreased, except for the reactions with nitrocefin and methicillin. The consequences of the first mutation were more surprising, since a large proportion of the thiolesterase activity was retained, together with the penicillin-binding capacity. Conversely, the peptidase properties was severely affected. In both cases, a drastic decrease in the transferase activity was observed. The results are compared with those obtained by mutation of the corresponding residue in the class A beta-lactamase of Streptomyces albus G.
摘要
将链霉菌R61青霉素敏感型DD-肽酶的酪氨酸-159替换为丝氨酸或苯丙氨酸。第二次突变产生了一种活性非常低的蛋白质，其青霉素结合速率也大幅降低，但与头孢硝噻吩和甲氧西林的反应除外。第一次突变的结果更令人惊讶，因为很大一部分硫酯酶活性以及青霉素结合能力得以保留。相反，肽酶特性受到严重影响。在这两种情况下，均观察到转移酶活性大幅下降。将这些结果与通过对白色链霉菌G的A类β-内酰胺酶中相应残基进行突变所获得的结果进行了比较。
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