Vitković L
Can J Microbiol. 1987 Jun;33(6):563-5. doi: 10.1139/m87-095.
The phenotypes characteristic of the pleiotropic lytic-deficient Bacillus subtilis mutants have been attributed to reductions in N-acetyl-muramoyl-L-alanine amidase (EC 3.5.1.28) and endo-beta-N-acetyl-glucosaminidase (EC 3.2.1.30). It is reported here that these peptidoglycan hydrolases are secreted. The FJ3 (lyt-1), FJ6 (lyt-2), and Ni15 (lyt-15) mutants secreted the enzymes in amounts comparable to a Lyt+ strain. Thus, the Lyt- mutants appear not be as deficient in the enzymes' synthesis as their cell-bound activities indicated. Based on the levels of cell-bound and extracellular activities measured during growth, it is suggested that the Lyt- phenotype may be due to a deficiency of the enzymes' acceptor(s) in cell walls.
多效性溶菌缺陷型枯草芽孢杆菌突变体的表型特征归因于N-乙酰胞壁酰-L-丙氨酸酰胺酶（EC 3.5.1.28）和内切-β-N-乙酰氨基葡萄糖苷酶（EC 3.2.1.30）的减少。本文报道这些肽聚糖水解酶是可分泌的。FJ3（lyt-1）、FJ6（lyt-2）和Ni15（lyt-15）突变体分泌这些酶的量与Lyt+菌株相当。因此，Lyt-突变体在这些酶的合成方面似乎并不像其细胞结合活性所显示的那样缺乏。根据生长过程中测得的细胞结合和细胞外活性水平，推测Lyt-表型可能是由于细胞壁中这些酶的受体缺乏所致。
