spacer Crystal structure of the SucA domain of Mycobacterium smegmatis KGD, post-decarboxylation intermediate from pyruvate (2-hydroxyethyl-ThDP)
UniProt
Accession A0R2B1search
Name KGD_MYCS2
Keywords Transferase, Multifunctional enzyme, Metal-binding, Magnesium, Acyltransferase, 3D-structure, Decarboxylase, Tricarboxylic acid cycle, Lyase, Thiamine pyrophosphate, Reference proteome, Coiled coil, Allosteric enzyme, Oxidoreductase, Complete proteome
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Polymers A B C D
 
Enzyme nomenclature
EC number 1.2.4.2 ExPASy BRENDA search
Polymers B, D, A, C
Name oxoglutarate dehydrogenase (lipoamide), oxoglutarate dehydrogenase (succinyl-transferring)
Comment Requires thiamine diphosphate; component of the multienzyme 2-oxoglutarate dehydrogenase complex.
Contains thiamine diphosphate. 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 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
EC number 4.1.1.71 ExPASy BRENDA search
Polymers A, D, C, B
Name 2-oxoglutarate decarboxylase
Comment Requires thiamine diphosphate. Highly specific.
EC number 2.3.1.61 ExPASy BRENDA search
Polymers D, C, A, B
Name dihydrolipoamide S-succinyltransferase, dihydrolipoyllysine-residue succinyltransferase
Comment This enzyme is a lipoyl-protein and is a component of the multienzyme 2-oxoglutarate dehydrogenase complex.
A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
EC number 2.2.1.5 ExPASy BRENDA search
Polymers A, C, D, B
Name 2-hydroxy-3-oxoadipate synthase
Comment The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.
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