Booker S, Broderick J, Stubbe J
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Biochem Soc Trans. 1993 Aug;21 ( Pt 3)(3):727-30. doi: 10.1042/bst0210727.
Ribonucleotide reductases isolated from E. coli and from L. leichmannii differ considerably in their primary and quaternary structures, as well as in their cofactor requirements. Despite these differences, studies with the wt enzymes and the normal substrate, and with the wt enzymes and a variety of mechanism-based inhibitors, demonstrate amazing mechanistic similarities between the two reductases. Recent studies with five cysteine mutants of both reductases reveal strikingly similar phenotypes, indicating that, despite the differences in the primary structures, the groups involved in catalysis in both enzymes appear to be similar.
从大肠杆菌和莱氏乳酸杆菌中分离出的核糖核苷酸还原酶在一级结构和四级结构以及辅因子需求方面存在很大差异。尽管存在这些差异,但对野生型酶与正常底物以及野生型酶与多种基于机制的抑制剂的研究表明,这两种还原酶在机制上具有惊人的相似性。最近对这两种还原酶的五个半胱氨酸突变体的研究揭示了惊人相似的表型,表明尽管一级结构存在差异,但两种酶中参与催化的基团似乎相似。