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Acetolactate synthase of Leuconostoc lactis and its regulation of acetoin production

  • Timothy M. Cogan (a1), Richard J. Fitzgerald (a2) and Shawn Doonan (a2)
Summary

The acetolactate synthase of Leuconostoc lactis NCW1 was studied. The Mn2+ content of cell free extracts was 3·2 µ/mg protein. The enzyme did not require Mn2+ for activity, had an optimum pH between 5 and 6 and was labile. Incubation at 21 °C or addition of thiamine pyrophosphate followed by storage at 4 °C stabilized the enzyme. It was allosteric with at least two binding sites for pyruvate and was inhibited by several products of glucose metabolism (6-phosphogluconate, 3-phosphoglycerate, 2-phosphoglycerate, PEP and ATP) at pH 5·4. Except for ATP, which became more inhibitory, the inhibition disappeared completely (6-phosphogluconate, 2-phosphoglycerate, and PEP) or partly (3-phosphoglycerate) at pH 4·7. The role of these compounds in the regulation of acetoin production from citrate by leuconostocs is discussed.

Copyright
COPYRIGHT: © Proprietors of Journal of Dairy Research 1984
References
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Journal of Dairy Research
  • ISSN: 0022-0299
  • EISSN: 1469-7629
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