Literature summary extracted from

Hodgson, J.A.; Lowe, P.N.; Perham, R.N.
Wild-type and mutant forms of the pyruvate dehydrogenase multienzyme complex from Bacillus subtilis (1983), Biochem. J., 211, 463-472.

General Stability

EC Number	General Stability	Organism
1.8.1.4	stable to trypsin treatment	Bacillus subtilis

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.8.1.4	55000	-	2 * 55000, SDS-PAGE	Bacillus subtilis
1.8.1.4	110000	-	gel filtration	Bacillus subtilis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.2.1.104	Bacillus subtilis	-	-	-
1.8.1.4	Bacillus subtilis	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.2.1.104	pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4	Bacillus subtilis
1.8.1.4	from pyruvate dehydrogenase complex	Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.8.1.4	125	-	-	Bacillus subtilis

Storage Stability

EC Number	Storage Stability	Organism
1.8.1.4	-20°C, stable for several months	Bacillus subtilis

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.8.1.4	dihydrolipoamide + NAD+	-	Bacillus subtilis	lipoamide + NADH	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.8.1.4	dimer	2 * 55000, SDS-PAGE	Bacillus subtilis

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.2.1.104	-	40	rapid decline of activity	Bacillus subtilis

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.8.1.4	NAD+	-	Bacillus subtilis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)