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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

REFERENCES

Atkinson, D. E. & Walton, G. M. (1967). Journal of Biological Chemistry 242, 3239.CrossRefGoogle Scholar
Hartman, R. E. (1970). Journal of Bacteriology 102, 341.CrossRefGoogle Scholar
Hillier, A. J. & Jago, G. R. (1978 a). Journal of Dairy Research 45, 231.CrossRefGoogle Scholar
Hiller, A. J. & Jago, G. R. (1978 b). Journal of Dairy Research 45, 423.CrossRefGoogle Scholar
Hillier, A. J., Rice, G. H. & Jago, G. R. (1978). Journal of Dairy Research 45, 241.CrossRefGoogle Scholar
Keech, D. B. & Utter, M. F. (1963). Journal of Biological Chemistry 238, 2609.CrossRefGoogle Scholar
Krebs, H. A. & Eggleston, L. V. (1945). Biochemical Journal 39, 408.CrossRefGoogle Scholar
Lachica, V. F. & Hartman, P. A. (1969 a). Canadian Journal of Microbiology 15, 57.CrossRefGoogle Scholar
Lachica, V. F. & Hartman, P. A. (1969 b). Canadian Journal of Microbiology 15, 61.CrossRefGoogle Scholar
McClure, W. R., Lardy, H. A. & Kneifel, H. P. (1971). Journal of Biological Chemistry 246, 3569.CrossRefGoogle Scholar
Sachs, D. H. & Painter, E. (1972). Science, New York 175, 781.CrossRefGoogle Scholar
Scrutton, M. C., Olmsted, M. R. & Utter, M. F. (1969). Methods in Enzymology 13, 235.CrossRefGoogle Scholar
Scrutton, M. C. & Fung, C. H. (1972). Archives of Biochemistry and Biophysics 150, 636.CrossRefGoogle Scholar
Scrutton, M. C. & Young, M. R. (1972). In The Enzymes, 3rd edn, vol. 6, p. 1. (Ed. Boyer, P. D..) New York: Academic Press.Google Scholar
Seubert, W. & Weicker, H. (1969). Methods in Enzymology 13, 258.CrossRefGoogle Scholar
Wilkinson, G. N. (1961). Biochemical Journal 80, 324.CrossRefGoogle Scholar
Young, M. R., Tolbert, B. & Utter, M. F. (1969). Methods in Enzymology 13, 250.CrossRefGoogle Scholar