A multienzyme complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase.

Catalysis of the reaction: ATP + biotin + apo-(3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)) = AMP + diphosphate + (3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)).

A component, along with aminomethyltransferase, of the glycine cleavage system; it is found as a homodimer or as a tetramer with two alpha subunits and two beta subunits.

Catalysis of the reaction: ATP + biotin + apo-(methylmalonyl-CoA:pyruvate carboxytransferase) = AMP + diphosphate + (methylmalonyl-CoA:pyruvate carboxytransferase).

Any substance involved in the initiation, activation, perpetuation, repression or termination of polypeptide synthesis at the ribosome.

An enzyme complex that catalyzes the phosphorylation of phosphorylase b to form phosphorylase a.

The directed movement of a protein to a specific location.

The processes by which a protein is maintained in a location and prevented from moving elsewhere. These include sequestration, stabilization to prevent transport elsewhere and the active retrieval of proteins that do move away.

pyruvate dehydrogenase complex (sensu Eukaryota)

pyruvate dehydrogenase complex (lipoamide) (sensu Eukaryota)

Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Usually contains more subunits than its bacterial counterpart; for example, one known complex contains 30 E1 dimers, 60 E2 monomers, and 6 E3 dimers as well as a few copies of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase. As in, but not restricted to, the eukaryotes (Eukaryota, ncbi_taxonomy_id:2759).

regulation of circadian sleep/wake cycle, sleep