Muraki M, Jigami Y, Morikawa M, Tanaka H
Biochim Biophys Acta. 1987 Feb 25;911(3):376-80. doi: 10.1016/0167-4838(87)90081-1.
Three human lysozymes containing a mutation either at Asp-53 to Glu or at Tyr-63 to Trp or Phe were synthesized and examined for their immunological and enzymatical activities in comparison with the native one. All mutants were immunologically indistinguishable from native human lysozyme. The [Trp63] and [Phe63] mutants catalysed the hydrolysis of Micrococcus lysodeikticus cell wall and glycol chitin effectively, while the [Glu53] mutant displayed very low activity toward M. lysodeikticus cells and no detectable activity toward glycol chitin.
合成了三种人溶菌酶，它们在Asp-53处发生了突变为Glu，或者在Tyr-63处突变为Trp或Phe，并与天然人溶菌酶相比，检测了它们的免疫活性和酶活性。所有突变体在免疫上与天然人溶菌酶没有区别。[Trp63]和[Phe63]突变体有效地催化了溶壁微球菌细胞壁和糖基几丁质的水解，而[Glu53]突变体对溶壁微球菌细胞的活性非常低，对糖基几丁质没有可检测到的活性。
