A novel catalase-peroxidase (CP) from methanol-grown cells of Mycobacterium sp. strain JC1 was purified. The CP exhibited properties of both typical mycobacterial CPs (i.e. strict pH optimum, labile to heat treatment, capable of oxidizing NADH, and resistant to inhibition by 3-amino-1,2,4- triazole) and true catalases (i.e. stable against ethanol-chloroform treatment). The enzyme oxidized methanol and shared common antigenic groups with other mycobacteria. Isoniazid had almost no effect on the growth and expression of CP but inhibited the enzyme activity to some extent. Sodium nitroprusside arrested the growth but strongly stimulated the expression of CP with a concomitant increase in activity after the mid-exponential growth phase.
Bibliographical noteFunding Information:
This work was supported by a research grant (KRF-2000-015-DP0382) from the Korea Research Foundation.
All Science Journal Classification (ASJC) codes
- Molecular Biology