CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.970
Functional Family Pyruvate dehydrogenase E1 component

Enzyme Information

1.2.4.1
Pyruvate dehydrogenase (acetyl-transferring).
based on mapping to UniProt P0AFG8
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
-!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.

UniProtKB Entries (1)

P0AFG8
ODP1_ECOLI
Escherichia coli K-12
Pyruvate dehydrogenase E1 component

PDB Structure

PDB 2G25
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
A Thiamin-bound, Pre-decarboxylation Reaction Intermediate Analogue in the Pyruvate Dehydrogenase E1 Subunit Induces Large Scale Disorder-to-Order Transformations in the Enzyme and Reveals Novel Structural Features in the Covalently Bound Adduct.
Arjunan, P., Sax, M., Brunskill, A., Chandrasekhar, K., Nemeria, N., Zhang, S., Jordan, F., Furey, W.
J.Biol.Chem.