2003
DOI: 10.1016/s0378-1097(03)00644-x
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Purification, characterization, and physiological response of a catalase-peroxidase inMycobacteriumsp. strain JC1 DSM 3803 grown on methanol

Abstract: 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 expres… Show more

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Cited by 9 publications
(8 citation statements)
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“…Aspergillus niger catalase and bovine liver catalase were obtained from Amano Enzyme (Nagoya) and Sigma, respectively, and used as references. The peroxidase activity of the catalase was examined by measuring the rate of oxidation of 0.25 mM o-dianisidine (ε460= 11.3 mM -1 cm -1 ) in the presence of 10 mM H 2 O 2 (18). Reactions were monitored spectrophotometrically at 460 nm.…”
Section: Methodsmentioning
confidence: 99%
“…Aspergillus niger catalase and bovine liver catalase were obtained from Amano Enzyme (Nagoya) and Sigma, respectively, and used as references. The peroxidase activity of the catalase was examined by measuring the rate of oxidation of 0.25 mM o-dianisidine (ε460= 11.3 mM -1 cm -1 ) in the presence of 10 mM H 2 O 2 (18). Reactions were monitored spectrophotometrically at 460 nm.…”
Section: Methodsmentioning
confidence: 99%
“…Pyr-1 and Ro et al [66] purified a catalase-peroxidase from Mycobacterium sp. strain JC1 DSM 3803 which produced the enzyme at high levels when grown in the presence of carbon monoxide and methanol as sole carbon and energy sources.…”
Section: Properties Of Catalase-peroxidasementioning
confidence: 99%
“…Plant peroxidases, including HRP, have about 20% sequence similarity and remarkable structural similarity to the N-terminal domain of KatG proteins, particularly in the vicinity of the heme active site, raising the possibility that KatG proteins may also exhibit an NADH peroxidase-oxidase activity. Indeed, there are reports of NADH being oxidized to NAD ϩ by KatG in both peroxidase (22) and an oxidase-like (7) reactions, but the reaction of KatG with NADH has not been characterized. Given the potential importance of any reaction involving NADH in isonicotinoyl-NAD formation, this report investigates the interactions of KatG with NADH, demonstrat-ing an oxygen-dependent NADH oxidase activity and a direct role for KatG in the formation of isonicotinoyl-NAD.…”
Section: Isonicotinic Acid Hydrazide (Isoniazid or Inh)mentioning
confidence: 99%