Joris B, Dusart J, Frere J M, van Beeumen J, Emanuel E L, Petursson S, Gagnon J, Waley S G
Biochem J. 1984 Oct 1;223(1):271-4. doi: 10.1042/bj2230271.
Labelling the beta-lactamase of Enterobacter cloacae P99 with a poor substrate or a mechanism-based inactivator points to an active-site serine residue in a sequence closely resembling that of the ampC beta-lactamase. These results establish the P99 enzyme as a class-C beta-lactamase, and the concurrence of the two approaches helps to confirm the reliability of determining active-site sequences with the aid of mechanism-based inactivators.
用一种不良底物或基于机制的失活剂标记阴沟肠杆菌P99的β-内酰胺酶,结果表明在一个与ampCβ-内酰胺酶序列非常相似的序列中存在一个活性位点丝氨酸残基。这些结果确定P99酶为C类β-内酰胺酶,两种方法的同时使用有助于确证借助基于机制的失活剂确定活性位点序列的可靠性。