Affiliation:
1. Instituto de Química Biológica, Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires, Argentina
Abstract
Levels of pyruvate carboxylase (PC), phosphopyruvate carboxylase (PEPC), and malate dehydrogenase (decarboxylating) were compared in wild-type bakers' yeast (I), a cytoplasmic-respiratory mutant (II), a biotin-deficient wild-type yeast (III), and a biotin-deficient respiratory mutant (IV). PC activities were greatly reduced in III and IV, whereas PEPC was reduced in II and IV. Malate dehydrogenase (decarboxylating) could not be detected in any of the yeasts. With yeast I growing on glucose as the sole carbon source, PEPC decreased to negligible levels during the logarithmic phase of growth (glucose repression effect), whereas PC increased. Both enzymes reverted to their original levels during the stationary phase, when glucose in the medium was exhausted. In agreement with the leading role of PC for CO
2
assimilation, the rates of
14
CO
2
fixation in yeasts I and II were approximately equal and were much higher than that in yeast IV. With I and II, most of the
14
C was distributed similarly in oxalacetate derivatives; with yeast IV, most of
14
C appeared in a compound apparently unrelated to CO
2
fixation via C
4
-dicarboxylic acids.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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