Sloan G L, Smith E C, Lancaster J H
Biochem J. 1977 Oct 1;167(1):293-6. doi: 10.1042/bj1670293.
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.
已发现溶葡萄球菌素中的甘氨酰甘氨酸内肽酶在作用于甘氨酰肽时能够催化水解和转肽反应。该酶在转肽反应中能够利用丹磺酰二甘氨酸(5-二甲基氨基萘-1-磺酰基甘氨酰甘氨酸)作为受体分子,尽管它不能水解该化合物中的肽键,这表明该酶在催化过程中必须能够形成相当于亚氨基酶中间体的物质。