Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:4.1.1.49 (
phosphoenolpyruvate carboxykinase
)
4,654
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The anaplerotic and gluconeogenetic metabolism of baker's yeast was studied at the enzymatic level during glucose-ethanol diauxic growth in the presence and absence of aspartate. Of the two possible anaplerotic systems, only the pyruvate carboxylase by-pass was present during the whole growth process. The second system, the glyoxylate by-pass (isocitrate lyase as the indicator), like the specific enzymes of the gluconeogenetic metabolism,
phosphoenolpyruvate carboxykinase
and
hexosediphosphatase
began to appear only after the glucose had been consumed. The addition of glucose during the growth phase based on ethanol effected a rapid disappearance of
phosphoenolpyruvate carboxykinase
and
hexosediphosphatase
activities. The activity of pyruvate carboxylase decreased when the growth medium was supplied with asparate. The presence of aspartate had no effect on the activities of the other enzymes studied.
...
PMID:On the activity and regulation of anaplerotic and gluconeogenetic enzymes during the growth process of baker's yeast. The biphasic growth. 17 81
Strains of Saccharomyces cerevisiae bearing nonsense mutations in the structural gene for proteinase B (EC 3.4.22.9) have been examined for the ability to make the transition from growth on acetate to growth on glucose and for the ability to inactivate three glucoeogenic enzymes during the transition because proteinase B has been proposed by others to be responsible for the inactivation of the three enzymes during the growth transition. The mutant strains make the growth transition normally. Catabolite inactivation of
hexosediphosphatase
(D-fructose-1,6-biphosphate 1-phosphohydrolase, EC 3.1.3.11), malate dehydrogenase (L-malate:NAD+ oxidoreductase, EC 1.1.1.37), and
phosphoenolpyruvate carboxykinase (ATP)
[
ATP:oxaloacetate carboxy-lyase
(transphosphorylating),
EC 4.1.1.49
] occurred in prb1 mutants with kinetics similar to those seen in wild-type strains. We infer that proteinase B activity is not essential for the process of catabolite inactivation.
...
PMID:Catabolite inactivation of gluconeogenic enzymes in mutants of yeast deficient in proteinase B. 22 2
