Function and Biology Details
Reaction catalysed:
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
- Transketolase-like, pyrimidine-binding domain
- Thiamin diphosphate-binding fold
- Transketolase, C-terminal domain
- Pyruvate dehydrogenase E1 component subunit beta
- Dehydrogenase, E1 component
- Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Pyruvate dehydrogenase E1 heterotetramer (preferred)
PDBe Complex ID:
PDB-CPX-140174 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Molecule details ›
Chains: A, C
Length: 365 amino acids
Theoretical weight: 40.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Dehydrogenase E1 component
Structure domains: Rossmann fold
Length: 365 amino acids
Theoretical weight: 40.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P08559 (Residues: 30-390; Coverage: 93%)
Sequence domains: Dehydrogenase E1 component
Structure domains: Rossmann fold
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Molecule details ›
Chains: B, D
Length: 341 amino acids
Theoretical weight: 37.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 341 amino acids
Theoretical weight: 37.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P11177 (Residues: 31-359; Coverage: 92%)
Sequence domains:
Structure domains:
