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Applied and Environmental Microbiology, October 2006, p. 6825-6828, Vol. 72, No. 10
0099-2240/06/$08.00+0     doi:10.1128/AEM.00829-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Endopeptidase and Glycosidase Activities of the Bacteriophage B30 Lysin

John R. Baker, Chengbao Liu, Shengli Dong, and David G. Pritchard*

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama

Received 7 April 2006/ Accepted 16 July 2006

Synthetic peptides corresponding to portions of group B streptococcal peptidoglycan were used to show that the endopeptidase activity of bacteriophage B30 lysin cleaves between D-Ala in the stem peptide and L-Ala in the cross bridge and that the minimal peptide sequence cleaved is DL-{gamma}-Glu-Lys-D-Ala-Ala-Ala. The only glycosidase activity present is that of N-acetyl-ß-D-muramidase.


* Corresponding author. Mailing address: Department of Biochemistry & Molecular Genetics, MCLM 552, University of Alabama at Birmingham, 1530 3rd Ave. S, Birmingham, AL 35294-0005. Phone: (205) 934-6023. Fax: (205) 934-6022. E-mail: davidp1{at}uab.edu.


Applied and Environmental Microbiology, October 2006, p. 6825-6828, Vol. 72, No. 10
0099-2240/06/$08.00+0     doi:10.1128/AEM.00829-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Pritchard, D. G., Dong, S., Kirk, M. C., Cartee, R. T., Baker, J. R. (2007). LambdaSa1 and LambdaSa2 Prophage Lysins of Streptococcus agalactiae. Appl. Environ. Microbiol. 73: 7150-7154 [Abstract] [Full Text]