CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
4 | Few Secondary Structures |
|
4.10 | Irregular |
|
4.10.320 | Dihydrolipoamide Transferase |
|
4.10.320.10 | E3-binding domain |
Domain Context
CATH Clusters
| Superfamily | E3-binding domain |
| Functional Family | Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex |
Enzyme Information
| 2.3.1.168 |
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase.
based on mapping to UniProt P11182
2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.
-!- A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. -!- In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
|
UniProtKB Entries (1)
| P09622 |
DLDH_HUMAN
Homo sapiens
Dihydrolipoyl dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 3RNM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and Thermodynamic Basis for Weak Interactions between Dihydrolipoamide Dehydrogenase and Subunit-binding Domain of the Branched-chain {alpha}-Ketoacid Dehydrogenase Complex.
J.Biol.Chem.
|
