Literature summary for 1.2.4.1 extracted from

Chauhan, H.J.; Domingo, G.J.; Jung, H.I.; Perham, R.N.
Sites of limited proteolysis in the pyruvate decarboxylase component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and their role in catalysis (2000), Eur. J. Biochem., 267, 7158-7169.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	-	-

Subunits

Subunits	Comment	Organism
More	there may be two conformers of E1alpha in the pyruvate decarboxylase E1 heterotetramer, one being more susceptible to proteolysis than the other. A highly conserved region in E1a, part of a surface loop at the entrance to the active site, is the most susceptible to cleavage in E1 (a2b2). As a result, the oxidative decarboxylation of pyruvate catalysed by E1 in the presence of dichlorophenol indophenol as an artificial electron acceptor is markedly enhanced, but the reductive acetylation of a free lipoyl domain is unchanged. The parameters of the interaction between cleaved E1 and the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase E2 component are identical to those of the wild-type E1. However, a pyruvate dehydrogenase complex assembled in vitro with cleaved E1p exhibits a markedly lower overall catalytic activity than that assembled with untreated E1	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)