Chemical studies on the structure of mucopeptide isolated from Streptococcus bovis.
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.
D000409:Alanine / Q000032:analysis; D002473:Cell Wall / Q000032:analysis; D002852:Chromatography, Ion Exchange; D005944:Glucosamine / Q000032:analysis; D005971:Glutamates / Q000032:analysis; D008239:Lysine / Q000032:analysis; D009088:Mucoproteins / Q000032:analysis* / Q000302:isolation & purification; D013291:Streptococcus / Q000032:analysis*; D013912:Threonine / Q000032:analysis
D005971:Glutamates; D009088:Mucoproteins; D013912:Threonine; D008239:Lysine; D005944:Glucosamine; D000409:Alanine