Enzyme Activities Related to the Methanol Oxidation of Mycobacterium sp. strain JC1 DSM 3803

Youngtae Ro, Eungbin Kim, Youngmin Kim

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Mycobacterium sp. strain JC1 DSM 3803 grown in methanol showed no methanol dehydrogenase or oxidase activities found in most methylotrophic bacteria and yeasts, respectively. Even though the methanol-grown cells exhibited a little methanol-dependent oxidation by cytochrome c-dependent methanol dehydrogenase and alcohol dehydrogenase, they were not the key enzymes responsible for the methanol oxidation of the cells, in that the cells contained no c-type cytochrome and the methanol oxidizing activity from the partially purified alcohol dehydrogenase was too low, respectively. In substrate switching experiments, we found that only a catalase-peroxidase among the three types of catalase found in glucose-grown cells was highly expressed in the methanol-grown cells and that its activity was relatively high during the exponential growth phase in Mycobacterium sp. JC1. Therefore, we propose that catalase-peroxidase is an essential enzyme responsible for the methanol metabolism directly or indirectly in Mycobacterium sp. JC1.

Original languageEnglish
Pages (from-to)209-217
Number of pages9
JournalJournal of Microbiology
Volume38
Issue number4
Publication statusPublished - 2000 Dec 1

Fingerprint

Mycobacterium
Methanol
Enzymes
Catalase
Alcohol Dehydrogenase
Peroxidase
Cytochrome c Group
Cytochromes c
Yeasts
Bacteria
Glucose
Growth

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology

Cite this

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title = "Enzyme Activities Related to the Methanol Oxidation of Mycobacterium sp. strain JC1 DSM 3803",
abstract = "Mycobacterium sp. strain JC1 DSM 3803 grown in methanol showed no methanol dehydrogenase or oxidase activities found in most methylotrophic bacteria and yeasts, respectively. Even though the methanol-grown cells exhibited a little methanol-dependent oxidation by cytochrome c-dependent methanol dehydrogenase and alcohol dehydrogenase, they were not the key enzymes responsible for the methanol oxidation of the cells, in that the cells contained no c-type cytochrome and the methanol oxidizing activity from the partially purified alcohol dehydrogenase was too low, respectively. In substrate switching experiments, we found that only a catalase-peroxidase among the three types of catalase found in glucose-grown cells was highly expressed in the methanol-grown cells and that its activity was relatively high during the exponential growth phase in Mycobacterium sp. JC1. Therefore, we propose that catalase-peroxidase is an essential enzyme responsible for the methanol metabolism directly or indirectly in Mycobacterium sp. JC1.",
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Enzyme Activities Related to the Methanol Oxidation of Mycobacterium sp. strain JC1 DSM 3803. / Ro, Youngtae; Kim, Eungbin; Kim, Youngmin.

In: Journal of Microbiology, Vol. 38, No. 4, 01.12.2000, p. 209-217.

Research output: Contribution to journalArticle

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AB - Mycobacterium sp. strain JC1 DSM 3803 grown in methanol showed no methanol dehydrogenase or oxidase activities found in most methylotrophic bacteria and yeasts, respectively. Even though the methanol-grown cells exhibited a little methanol-dependent oxidation by cytochrome c-dependent methanol dehydrogenase and alcohol dehydrogenase, they were not the key enzymes responsible for the methanol oxidation of the cells, in that the cells contained no c-type cytochrome and the methanol oxidizing activity from the partially purified alcohol dehydrogenase was too low, respectively. In substrate switching experiments, we found that only a catalase-peroxidase among the three types of catalase found in glucose-grown cells was highly expressed in the methanol-grown cells and that its activity was relatively high during the exponential growth phase in Mycobacterium sp. JC1. Therefore, we propose that catalase-peroxidase is an essential enzyme responsible for the methanol metabolism directly or indirectly in Mycobacterium sp. JC1.

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