ON THE ORIGIN OF BACTERIAL-RESISTANCE TO PENICILLIN - COMPARISON OF A BETA-LACTAMASE AND A PENICILLIN TARGET

被引：214

作者：

KELLY, JA

DIDEBERG, O

CHARLIER, P

WERY, JP

LIBERT, M

MOEWS, PC

KNOX, JR

DUEZ, C

FRAIPONT, C

JORIS, B

DUSART, J

FRERE, JM

GHUYSEN, JM

机构：

[1] UNIV CONNECTICUT, DEPT MOLEC & CELL BIOL, STORRS, CT 06268 USA

[2] UNIV CONNECTICUT, INST MAT SCI, STORRS, CT 06268 USA

[3] UNIV LIEGE, INST PHYS B5, SERV CRISTALLOG, B-4000 SART TILMAN, BELGIUM

[4] UNIV LIEGE, INST CHIM, SERV MICROBIOL, B-4000 SART TILMAN, BELGIUM

来源：

SCIENCE | 1986年 / 231卷 / 4744期

关键词：

D O I：

10.1126/science.3082007

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the .beta.-lactamase from Bacillus licheniformis 749/C. Although the two enzymes have distinct catalytic properties and lack relatedness in their overall amino acid sequences except near the active-site serine, the significant similarity found by X-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that .beta.-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.

引用

页码：1429 / 1431

页数：3

共 23 条

[1] THE STRUCTURE OF BETA-LACTAMASES [J].