Skl, a novel choline-binding N-acetylmuramoyl-L-alanine amidase of Streptococcus mitis SK137 containing a CHAP domain

FEBS Letters
Daniel LlullErnesto García

Abstract

The skl gene from Streptococcus mitis SK137 encodes a peptidoglycan hydrolase (Skl) that has been purified and biochemically characterized. Analysis of the degradation products obtained by digestion of pneumococcal cell walls with Skl revealed that this enzyme is an N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28), showing optimum activity at 30 degrees C and at a pH of 6.5. Skl is a unique member of the choline-binding family of proteins since it contains a cysteine, histidine-dependent amidohydrolases/peptidases (CHAP) domain. The CHAP domain of Skl showed homology to lysins of unknown especificity from a variety of streptococcal prophages. Skl represents the first characterized member of a new subfamily of CHAP-containing choline-binding proteins.

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Citations

Mar 8, 2011·Molecular Oral Microbiology·J Mitchell
Jan 27, 2009·Applied and Environmental Microbiology·Patricia RomeroTim J Mitchell
Jul 28, 2009·Journal of Bacteriology·Lalitha BiswasFriedrich Götz
Oct 25, 2007·Journal of Molecular Microbiology and Biotechnology·Séverine LayecNathalie Leblond-Bourget
Jun 12, 2010·International Journal of Food Microbiology·Pilar GarcíaAna Rodríguez
Jul 29, 2008·Research in Microbiology·Séverine LayecNathalie Leblond-Bourget
Jun 9, 2007·Molecular Microbiology·Jean-Pierre ClaverysLeiv Sigve Håvarstein
Aug 23, 2007·FEMS Microbiology Letters·Jan R van der Ploeg
Jan 22, 2017·Journal of Biotechnology·Szymon P SzafrańskiMeike Stiesch
Aug 31, 2020·Clinical and Experimental Vaccine Research·Davoud AfsharMohammad Azarsa
Mar 19, 2019·Critical Reviews in Food Science and Nutrition·Rachel ShannonSampathkumar Balamurugan

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