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Malolactic enzyme in Lactobacillus murinus.

A M Strasser de Saad1, A A Pesce de Ruiz Holgado, G Oliver

  • 1Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Argentina.

Biochimie
|March 1, 1988
PubMed
Summary
This summary is machine-generated.

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The inducible malolactic enzyme from Lactobacillus murinus is regulated at the transcription level and requires L-malic acid, glucose, and amino acids for induction. This enzyme catalyzes L-malate to L-lactate and CO2 conversion.

Area of Science:

  • Enzymology
  • Microbial Biochemistry
  • Molecular Biology

Background:

  • The malolactic enzyme facilitates the conversion of L-malate to L-lactate and CO2.
  • Understanding the regulation and kinetics of this enzyme is crucial for microbial metabolism studies.

Purpose of the Study:

  • To characterize the inducible malolactic enzyme from Lactobacillus murinus.
  • To elucidate the enzyme's catalytic mechanism, kinetics, and regulatory properties.

Main Methods:

  • Enzyme purification to homogeneity.
  • Characterization of enzyme kinetics, including optimal conditions and activation energy.
  • Investigation of reaction mechanism using substrate and inhibitor studies.
  • Subunit analysis using sodium dodecyl sulphate.

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Main Results:

  • The enzyme is inducible at the transcriptional level by L-malic acid in the presence of glucose and amino acids.
  • Purified enzyme has a molecular weight of 220,000 Da, composed of two 110,000 Da subunits.
  • Optimal activity at 37°C and pH 5.5, with positive cooperativity observed at non-optimal pH.
  • Catalyzes NAD+ and manganese-dependent conversion of L-malate to L-lactate and CO2 via a compulsory-order mechanism.
  • NAD+ binds first, Mn2+ acts as an allosteric activator, and malate binds to the enzyme-NAD-Mn2+ complex.
  • Specific inhibitors identified, distinguishing it from other malic enzymes.

Conclusions:

  • The malolactic enzyme of Lactobacillus murinus exhibits unique regulatory and kinetic properties.
  • The enzyme's mechanism involves a specific binding order of cofactors and substrate.
  • This study provides a detailed characterization differentiating it from other malic enzymes.