CATH Classification

Domain Context

CATH Clusters

Superfamily TPP helical domain
Functional Family

Enzyme Information
Oxoglutarate dehydrogenase (succinyl-transferring).
based on mapping to UniProt A0R2B1
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
-!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC, which also binds multiple copies of EC -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC
2-hydroxy-3-oxoadipate synthase.
based on mapping to UniProt A0R2B1
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2).
-!- The product decarboxylates to 5-hydroxy-4-oxopentanoate. -!- The enzyme can decarboxylate 2-oxoglutarate. -!- Acetaldehyde can replace glyoxylate. -!- Formerly EC
Dihydrolipoyllysine-residue succinyltransferase.
based on mapping to UniProt A0R2B1
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 and EC -!- The lipoyl group of this enzyme is reductively succinylated by EC, and the only observed direction catalyzed by EC is that where this succinyl group is passed to coenzyme A.
2-oxoglutarate decarboxylase.
based on mapping to UniProt A0R2B1
2-oxoglutarate = succinate semialdehyde + CO(2).
-!- Highly specific.

UniProtKB Entries (1)

Mycobacterium smegmatis str. MC2 155
Multifunctional 2-oxoglutarate metabolism enzyme

PDB Structure

External Links
Primary Citation
Functional Plasticity and Allosteric Regulation of Alpha-Ketoglutarate Decarboxylase in Central Mycobacterial Metabolism.
Wagner, T., Bellinzoni, M., Wehenkel, A.M., O'Hare, H.M., Alzari, P.M.