The metabolism of [14C]bicarbonate by Streptococcus lactis: the fixation of [14C]bicarbonate by pyruvate carboxylase.
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.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000263:Adenylate Kinase / Q000378:metabolism; D001219:Aspartate Aminotransferases / Q000378:metabolism; D001639:Bicarbonates / Q000378:metabolism*; D007700:Kinetics; D011766:Pyruvate Carboxylase / Q000378:metabolism*; D013291:Streptococcus / Q000201:enzymology*
D001639:Bicarbonates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D001219:Aspartate Aminotransferases; D000263:Adenylate Kinase; D011766:Pyruvate Carboxylase