一种具有活性膜相关磷脂酶A1的枯草芽孢杆菌渗透敏感突变体。
An osmotically fragile mutant of Bacillus subtilis with an active membrane-associated phospholipase A 1 .
作者信息
Kent C, Lennarz W J
出版信息
Proc Natl Acad Sci U S A. 1972 Oct;69(10):2793-7. doi: 10.1073/pnas.69.10.2793.
Abstract
By use of a newly developed procedure for the isolation of mutants with osmotically fragile protoplasts, a mutant of Bacillus subtilis was isolated that has a very active enzyme system for the catabolism of phospholipids via the sequential action of a phospholipase A(1) (EC 3.1.1.4) and a lysophospholipase (EC 3.1.1.5). The wild-type bacteria contain no detectable phospholipase A(1) activity, but do contain a protein that specifically inhibits the phospholipase A(1) in the mutant. This protein may play an important role in the control of phospholipid catabolism.
摘要
通过使用一种新开发的用于分离具有渗透易碎原生质体的突变体的程序，分离出了枯草芽孢杆菌的一个突变体，该突变体具有一个非常活跃的酶系统，可通过磷脂酶A(1)（EC 3.1.1.4）和溶血磷脂酶（EC 3.1.1.5）的顺序作用来进行磷脂的分解代谢。野生型细菌没有可检测到的磷脂酶A(1)活性，但确实含有一种能特异性抑制突变体中磷脂酶A(1)的蛋白质。这种蛋白质可能在磷脂分解代谢的控制中起重要作用。
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