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Literature summary for 1.2.4.1 extracted from

  • Lee, J.; Oh, S.; Bhattacharya, S.; Zhang, Y.; Florens, L.; Washburn, M.P.; Workman, J.L.
    The plasticity of the pyruvate dehydrogenase complex confers a labile structure that is associated with its catalytic activity (2020), PLoS ONE, 15, e0243489 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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Saccharomyces cerevisiae 5739
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P16387 E1 component subunit alpha
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Saccharomyces cerevisiae BY4741 P16387 E1 component subunit alpha
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Subunits

Subunits Comment Organism
More the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Pda1
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity Saccharomyces cerevisiae