作为链霉菌R61 DD-肽酶家族成员的活性位点丝氨酸青霉素识别酶。
The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.
作者信息
Joris B, Ghuysen J M, Dive G, Renard A, Dideberg O, Charlier P, Frère J M, Kelly J A, Boyington J C, Moews P C
机构信息
Service de Microbiologie, Université de Liège, Belgium.
出版信息
Biochem J. 1988 Mar 1;250(2):313-24. doi: 10.1042/bj2500313.
Abstract
Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2 beta-lactamase (considered as the first known member of an additional class D), the low-Mr DD-peptidases/penicillin-binding proteins (protein no. 5 of Escherichia coli and Bacillus subtilis) and penicillin-binding domains of the high-Mr penicillin-binding proteins (PBP1A, PBP1B, PBP2 and PBP3 of E. coli). Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families. The amino acid alignments reveal several conserved boxes that consist of strict identities or homologous amino acids. The significance of these boxes is highlighted by the known results of X-ray crystallography, chemical derivatization and site-directed-mutagenesis experiments.
摘要
以链霉菌R61 DD - 肽酶/青霉素结合蛋白为参考进行的同源性搜索和氨基酸比对，已应用于A类和C类β - 内酰胺酶、Oxa - 2β - 内酰胺酶（被认为是另一D类的首个已知成员）、低分子量DD - 肽酶/青霉素结合蛋白（大肠杆菌和枯草芽孢杆菌的5号蛋白）以及高分子量青霉素结合蛋白的青霉素结合结构域（大肠杆菌的PBP1A、PBP1B、PBP2和PBP3）。尽管进化距离可能有很大差异，但所有这些与青霉素相互作用的蛋白和结构域似乎都是活性位点丝氨酸酶单一超家族的成员，不同于经典的胰蛋白酶或枯草杆菌蛋白酶家族。氨基酸比对揭示了几个由严格相同或同源氨基酸组成的保守框。X射线晶体学、化学衍生化和定点诱变实验的已知结果突出了这些框的重要性。
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