De Meester F, Joris B, Lenzini M V, Dehottay P, Erpicium T, Dusart J, Klein D, Ghuysen J M, Frère J M, Van Beeumen J
Laboratoires de Microbiologie et d'Enzymologie, Université de Liège, Belgium.
Biochem J. 1987 Jun 1;244(2):427-32. doi: 10.1042/bj2440427.
The active-site serine of the extracellular beta-lactamases of Streptomyces cacaoi and Streptomyces albus G has been labelled with beta-iodopenicillanate. The determination of the sequence of the labelled peptides obtained after trypsin digestion of the denatured proteins indicate both enzymes to be class A beta-lactamases. Surprisingly the two Streptomyces enzymes do not appear to be especially homologous, and none of them exhibited a high degree of homology with the Streptomyces R61 DD-peptidase. Our data confirm that, as a family of homologous enzymes, class A is rather heterogeneous, with only a small number of conserved residues in all members of the class.
可可链霉菌和白色链霉菌G的细胞外β-内酰胺酶的活性位点丝氨酸已用β-碘青霉素酸盐标记。对变性蛋白质进行胰蛋白酶消化后得到的标记肽段序列测定表明这两种酶均为A类β-内酰胺酶。令人惊讶的是,这两种链霉菌酶似乎并非特别同源,且它们与链霉菌R61 DD-肽酶均未表现出高度同源性。我们的数据证实,作为一个同源酶家族,A类相当异质,该类所有成员中只有少数保守残基。