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Related Experiment Videos

Alkene monooxygenase from Mycobacterium: a multicomponent enzyme.

S Hartmans1, F J Weber, D P Somhorst

  • 1Department of Food Science, Agricultural University Wageningen, The Netherlands.

Journal of General Microbiology
|November 1, 1991
PubMed
Summary

Researchers detected alkene monooxygenase (AMO) activity in Mycobacterium strains, suggesting it is a multicomponent enzyme. This enzyme utilizes NADH or NADPH and shares similarities with methane monooxygenases.

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Enhancement of Exopolysaccharide Production by Lactobacillus delbrueckii subsp. bulgaricus NCFB 2772 with a Simplified Defined Medium.

Applied and environmental microbiology·2005

Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Ethene utilization by microorganisms is crucial for bioremediation and industrial processes.
  • Alkene monooxygenases (AMOs) are key enzymes in the metabolism of gaseous alkenes.
  • Understanding AMO structure and function is essential for optimizing biotechnological applications.

Purpose of the Study:

  • To characterize the alkene monooxygenase (AMO) activity in ethene-utilizing Mycobacterium strains.
  • To investigate the enzymatic properties and potential multicomponent nature of AMO.
  • To compare AMO characteristics with known methane monooxygenases.

Main Methods:

  • Detection of AMO activity in cell-free extracts of Mycobacterium E3 and Mycobacterium aurum L1.
  • Assay development to measure AMO activity and assess linearity with protein concentration.

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  • Enzyme fractionation to identify distinct components of the AMO system.
  • Inhibition studies using acetylene to probe enzyme components.
  • Analysis of reductase activity in different cellular fractions.

    • Main Results:

    • NADH- or NADPH-dependent AMO activity was detected in Mycobacterium E3 and Mycobacterium aurum L1.
    • AMO activity was not linear with protein concentration, indicating a multicomponent enzyme system.
    • Fractionation revealed two essential components for AMO activity: an oxygenase component (inhibited by acetylene) and a reductase component.
    • The reductase activity was dependent on cell induction and likely represents the NADH-acceptor reductase of AMO.
    • AMO inhibition patterns closely resembled those of three-component soluble methane monooxygenases.

    Conclusions:

    • Mycobacterium E3 and Mycobacterium aurum L1 possess a multicomponent alkene monooxygenase (AMO).
    • The AMO system comprises at least two distinct fractions: an oxygenase and a reductase.
    • The identified reductase activity is likely crucial for AMO function and is dependent on cell induction.
    • The findings provide insights into the enzymatic machinery for ethene metabolism in mycobacteria.