THE ACTIVE-SITE-SERINE PENICILLIN-RECOGNIZING ENZYMES AS MEMBERS OF THE STREPTOMYCES R61 DD-PEPTIDASE FAMILY
THE ACTIVE-SITE-SERINE PENICILLIN-RECOGNIZING ENZYMES AS MEMBERS OF THE STREPTOMYCES R61 DD-PEPTIDASE FAMILY
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DOI：
10.1042/bj2500313
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发表时间：
1988-03-01
影响因子：
4.1
通讯作者：
KNOX, JR
中科院分区：
文献类型：
--
作者：
JORIS, B;GHUYSEN, JM;KNOX, JR
使用链霉菌R61 DD-肽酶/青霉素结合蛋白作为参照，同源性搜索和氨基酸比对已经应用于β- A类和C类内酰胺酶，Oxa-2 β-内酰胺酶，内酰胺酶（被认为是另一类D的第一个已知成员）、低Mr 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）和高Mr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）。大肠杆菌）。虽然进化的距离可能会有很大的不同，所有这些青霉素相互作用的蛋白质和结构域似乎是一个单一的超家族的活性位点丝氨酸酶不同于经典的胰蛋白酶或枯草杆菌蛋白酶家族的成员。氨基酸比对揭示了几个保守的盒子，由严格的身份或同源氨基酸。X射线晶体学、化学衍生和定点诱变实验的已知结果突出了这些框的意义。
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.