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.

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