Catalase-negative mutants of Escherichia coli

Efrat Meir, Ezra Yagil*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Catalase activity in crude extracts of Escherichia coli has two pH optima: one at pH 6.8 and the other at pH 10.5. The former is inducible by H2O2 and is the major species in exponential cells. The latter is constitutive and is the major species in stationary cells. Both activities are repressed by glucose. Catalase-negative mutants that are impaired in the pH-6.8 activity were isolated by the inability of aerobically grown mutagenized colonies to decompose H2O2. One mutant (cat2) characterized is hypersensitive to H2O2.

Original languageEnglish
Pages (from-to)13-17
Number of pages5
JournalCurrent Microbiology
Issue number1
StatePublished - Jan 1984


Dive into the research topics of 'Catalase-negative mutants of Escherichia coli'. Together they form a unique fingerprint.

Cite this