Chemical studies on the structure of mucopeptide isolated from Streptococcus bovis.

Journal of Bacteriology
J KaneR M KRAUSE

Abstract

Mucopeptides isolated from Streptococcus bovis cell walls were found to be composed of alanine, glutamic acid, lysine, and threonine in a mole ratio of 3:1:1:1. A dipeptide, N(epsilon)-lysylthreonine, was isolated from S. bovis mucopeptide by ion-exchange chromatography. This finding suggests that threonine is associated with the bridge which cross-links adjacent tetrapeptides by connecting the epsilon-amino group of lysine of one tetrapeptide to the carboxyl group of d-alanine of another to form the mucopeptide matrix.

References

Aug 1, 1968·The Journal of Experimental Medicine·W W KarakawaR M Krause
May 1, 1969·Journal of General Microbiology·J A Kane, W W Karakawa
Aug 1, 1966·The Journal of Experimental Medicine·W W Karakawa, R M Krause
May 1, 1960·The Journal of Experimental Medicine·S D ELLIOTT
Sep 1, 1964·Bacteriological Reviews·R H DEIBEL
Jan 1, 1945·The Biochemical Journal·F Sanger

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Citations

Jan 1, 1973·Journal of Bacteriology·F FiedlerO Kandler
Dec 1, 1972·Bacteriological Reviews·K H Schleifer, O Kandler
May 1, 1973·Infection and Immunity·K K Srivastava, I H Siddique

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