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• W2039793609 startingPage "1959" @default.
• W2039793609 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." @default.
• W2039793609 created "2016-06-24" @default.
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• W2039793609 date "2006-03-03" @default.
• W2039793609 modified "2023-10-17" @default.
• W2039793609 title "Skl, a novel choline-binding<i>N</i>-acetylmuramoyl-<scp>l</scp>-alanine amidase of<i>Streptococcus mitis</i>SK137 containing a CHAP domain" @default.
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• W2039793609 doi "https://doi.org/10.1016/j.febslet.2006.02.060" @default.
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