The metabolism of [14C]bicarbonate byStreptococcus lactis: the fixation of [14C]bicarbonate by pyruvate carboxylase
- 1 October 1978
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 45 (3) , 433-444
- https://doi.org/10.1017/s0022029900016654
Abstract
Summary: The fixation of [14C]bicarbonate into aspartate byStreptococcus lactisC10 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 fromStr. lactisC10, 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.This publication has 16 references indexed in Scilit:
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