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M Bruneteau1, G Michel

  • 1Laboratoire de Chimie biologique, Faculté des Sciences de Lyon, 43 boulevard du 11 novembre 1918, 69-, Villeurbanne, France

FEBS Letters
|April 12, 1971
PubMed
Summary
This summary is machine-generated.

Mycobacterium avium contains an L-alanine reductase enzyme. This enzyme converts L-alanine into L-alaninol, a component of mycoside C(2), with optimal activity when ATP and NADH are present.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Mycobacterium avium is a significant pathogen.
  • Mycoside C(2) is a complex glycolipid found in mycobacterial cell walls.
  • The biosynthesis pathway of mycoside C(2) involves several enzymatic steps.

Purpose of the Study:

  • To identify and characterize enzymes involved in mycoside C(2) biosynthesis in Mycobacterium avium.
  • To investigate the role of L-alanine reductase in the production of L-alaninol, a mycoside C(2) constituent.

Main Methods:

  • Preparation of cell-free extracts from Mycobacterium avium cultures.
  • Enzyme assays to measure L-alanine reductase activity.
  • Analysis of reaction products using chromatographic and spectroscopic methods.

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  • Optimization of enzyme activity by varying substrate and cofactor concentrations.

    • Main Results:

    • A cell-free preparation from Mycobacterium avium exhibited L-alanine reductase activity.
    • The enzyme catalyzes the reduction of L-alanine to L-alaninol.
    • Enzyme activity was significantly enhanced by the presence of adenosine triphosphate (ATP) and nicotinamide adenine dinucleotide (NADH).
    • L-alaninol was confirmed as a constituent of mycoside C(2).

    Conclusions:

    • Mycobacterium avium possesses an L-alanine reductase essential for L-alaninol synthesis.
    • The enzyme's activity is dependent on ATP and NADH, suggesting an energy-requiring reduction process.
    • This finding contributes to understanding the complex biosynthesis of mycobacterial cell wall components like mycoside C(2).