CATH Classification

Domain Context

CATH Clusters

Superfamily E3-binding domain
Functional Family Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Enzyme Information

2.3.1.61
Dihydrolipoyllysine-residue succinyltransferase.
based on mapping to UniProt P0AFG6
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine.
-!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.

UniProtKB Entries (1)

P0AFG6
ODO2_ECOLI
Escherichia coli K-12
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

PDB Structure

PDB 2WXC
External Links
Method SOLUTION NMR
Organism
Primary Citation
The Folding Mechanism of Bbl: Plasticity of Transition-State Structure Observed within an Ultrafast Folding Protein Family.
Neuweiler, H., Sharpe, T.D., Rutherford, T.J., Johnson, C.M., Allen, M.D., Ferguson, N., Fersht, A.R.
J.Mol.Biol.