The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain

被引：59

作者：

Donovan, David M.

Foster-Frey, Juli

Dong, Shengli

Rousseau, Genevive M.

Moineau, Sylvain

Pritchard, David G.

机构：

[1] USDA ARS, ANRI, Biotechnol & Germplasm Lab, Beltsville, MD 20705 USA

[2] Univ Alabama, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA

[3] Univ Laval, Felix Herelle Refernce Ctr Bacterial Viruses, Fac Med Dent, GREB,Fac Sci & Genie,Dept Biochim & Microbiol, Quebec City, PQ G1K 7P4, Canada

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2006年 / 72卷 / 07期

关键词：

D O I：

10.1128/AEM.03065-05

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. Truncations and point mutations indicated that the Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity.

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页码：5108 / 5112

页数：5

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