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The metabolism of [14C]bicarbonate by Streptococcus lactis: the fixation of [14C]bicarbonate by pyruvate carboxylase

Published online by Cambridge University Press:  01 June 2009

Alan J. Hillier  and
G. Richard Jago
Alan J. Hillier
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
G. Richard Jago
Affiliation:
Dairy Research Laboratory, Division of Food Research, CSIRO, Highett, Victoria 3190, Australia
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Summary

The fixation of [14C]bicarbonate into aspartate by Streptococcus lactis C10 was achieved by the combined reactions of pyruvate carboxylase (E.C. 6.4.1.1) and glutamate-oxaloacetate transaminase (E.C. 2.6.1.1). The pyruvate carboxylase from Str. lactis C10, which was most active at pH 8·0, was activated by the divalent metal ions Mn2+, Mg2+ and Co2+, and inhibited by sulphydryl reagents. The enzyme was inhibited non-competitively by aspartic acid and competitively by oxaloacetate.

Type
Original Articles
Information
Journal of Dairy Research , Volume 45 , Issue 3 , October 1978 , pp. 433 - 444
Copyright
Copyright © Proprietors of Journal of Dairy Research 1978

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References

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