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Acetolactate synthase of Leuconostoc lactis and its regulation of acetoin production

Published online by Cambridge University Press:  01 June 2009

Timothy M. Cogan ,
Richard J. Fitzgerald  and
Shawn Doonan
Timothy M. Cogan
Affiliation:
Moorepark Research Centre, The Agricultural Institute, Fermoy, Co. Cork, Irish Republic
Richard J. Fitzgerald
Affiliation:
Department of Biochemistry, University College, Cork, Irish Republic
Shawn Doonan
Affiliation:
Department of Biochemistry, University College, Cork, Irish Republic
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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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 51 , Issue 4 , November 1984 , pp. 597 - 604
Copyright
Copyright © Proprietors of Journal of Dairy Research 1984

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References

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