Purification and characterization of the catabolic α-acetolactate synthase from Leuconostoc mesenteroides subsp. cremoris

@article{Phalip1995PurificationAC,
  title={Purification and characterization of the catabolic α-acetolactate synthase from Leuconostoc mesenteroides subsp. cremoris},
  author={Vincent Phalip and Philippe Schmitt and Charles Divi{\`e}s},
  journal={Current Microbiology},
  year={1995},
  volume={31},
  pages={316-321}
}
The α-acetolactate synthase from Leuconostoc mesenteroides subsp. cremoris was purified to homogeneity in SDS-PAGE. The enzyme is a trimer of 3×55,000 Da. It was unstable but could be preserved by addition of pyruvate and thiamine pyrophosphate in the buffer. The enzyme exhibits Michaelis-Menten kinetics, and K m for pyruvate is 10 mM. Three intermediates in glucose metabolism (ATP, 3-phosphoglycerate, and phosphoenolpyruvate) exhibit a noncompetitive inhibition towards the enzyme. This enzyme… CONTINUE READING

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