The glycylglycine endopeptidase in lysostaphin has been found capable of catalysing both hydrolysis and transpeptidation reactions when acting on glycyl peptides. The ability of the enzyme to utilize dansyldiglycine (5-dimethylaminoaphthalene-1-sulphonylglycylglycine) as an acceptor molecule in transpeptidation reactions, although it is incapable of hydrolysing the peptide bond in this compound, indicates the enzyme must be capable of forming the equivalent of an imino-enzyme intermediate during the catalytic process.
Research Article| October 01 1977
Lysostaphin endopeptidase-catalysed transpeptidation reactions of the imino-transfer type
Biochem J (1977) 167 (1): 293-296.
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G L Sloan, E C Smith, J H Lancaster; Lysostaphin endopeptidase-catalysed transpeptidation reactions of the imino-transfer type. Biochem J 1 October 1977; 167 (1): 293–296. doi: https://doi.org/10.1042/bj1670293
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