Loewen P C
J Bacteriol. 1984 Feb;157(2):622-6. doi: 10.1128/jb.157.2.622-626.1984.
A number of catalase-deficient mutants of Escherichia coli which exhibit no assayable catalase activity were isolated. The only physiological difference between the catalase mutants and their parents was a 50- to 60-fold greater sensitivity to killing by hydrogen peroxide. For comparison, mutations in the xthA and recA genes of the same strains increased the sensitivity of the mutants to hydrogen peroxide by seven- and fivefold, respectively, showing that catalase was the primary defense against hydrogen peroxide. One class of mutants named katE was localized between pfkB and xthA at 37.8 min on the E. coli genome. A second class of catalase mutants was found which did not map in this region.
我们分离出了许多缺乏过氧化氢酶活性的大肠杆菌突变体。过氧化氢酶突变体与其亲本之间唯一的生理差异是对过氧化氢杀伤的敏感性提高了50至60倍。作为比较，同一菌株的xthA和recA基因突变分别使突变体对过氧化氢的敏感性提高了7倍和5倍，这表明过氧化氢酶是抵御过氧化氢的主要防御机制。一类名为katE的突变体位于大肠杆菌基因组37.8分钟处的pfkB和xthA之间。还发现了另一类过氧化氢酶突变体，它们并不定位于此区域。
