KEGG   ENZYME: 1.2.1.105
Entry
EC 1.2.1.105                Enzyme                                 

Name
2-oxoglutarate dehydrogenase system;
2-oxoglutarate dehydrogenase complex
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
Sysname
2-oxoglutarate:NAD+ 2-oxidoreductase (CoA-succinylating)
Reaction(IUBMB)
2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH [RN:R08549]
Reaction(KEGG)
R08549
Substrate
2-oxoglutarate [CPD:C00026];
CoA [CPD:C00010];
NAD+ [CPD:C00003]
Product
succinyl-CoA [CPD:C00091];
CO2 [CPD:C00011];
NADH [CPD:C00004]
Comment
The 2-oxoglutarate dehydrogenase system is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, branched-chain alpha-keto acid dehydrogenase system, EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). This enzyme system converts 2-oxoglutarate to succinyl-CoA and produces NADH and CO2 in a complicated series of irreversible reactions. The reaction catalysed by this system is the sum of three activities: EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) (E1), EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase (E2) and EC 1.8.1.4, dihydrolipoyl dehydrogenase (E3).
History
EC 1.2.1.105 created 2020
Reference
1  [PMID:1554728]
  Authors
Robien MA, Clore GM, Omichinski JG, Perham RN, Appella E, Sakaguchi K, Gronenborn AM.
  Title
Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli.
  Journal
Biochemistry 31:3463-71 (1992)
DOI:10.1021/bi00128a021
Reference
2  [PMID:9677295]
  Authors
Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML.
  Title
Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex.
  Journal
J Mol Biol 280:655-68 (1998)
DOI:10.1006/jmbi.1998.1924
Reference
3  [PMID:11477096]
  Authors
Reed LJ
  Title
A trail of research from lipoic acid to alpha-keto acid dehydrogenase complexes.
  Journal
J Biol Chem 276:38329-36 (2001)
DOI:10.1074/jbc.R100026200
Reference
4  [PMID:16338405]
  Authors
Murphy GE, Jensen GJ.
  Title
Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes.
  Journal
Structure 13:1765-73 (2005)
DOI:10.1016/j.str.2005.08.016
Reference
5  [PMID:17367808]
  Authors
Frank RA, Price AJ, Northrop FD, Perham RN, Luisi BF.
  Title
Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex.
  Journal
J Mol Biol 368:639-51 (2007)
DOI:10.1016/j.jmb.2007.01.080
Reference
6  [PMID:18004749]
  Authors
Bunik VI, Degtyarev D.
  Title
Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins.
  Journal
Proteins 71:874-90 (2008)
DOI:10.1002/prot.21766
Reference
7  [PMID:21809826]
  Authors
Shim da J, Nemeria NS, Balakrishnan A, Patel H, Song J, Wang J, Jordan F, Farinas ET.
  Title
Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; substitutions that lead to acceptance of substrates lacking the 5-carboxyl group.
  Journal
Biochemistry 50:7705-9 (2011)
DOI:10.1021/bi200936n
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.105
IUBMB Enzyme Nomenclature: 1.2.1.105
ExPASy - ENZYME nomenclature database: 1.2.1.105
BRENDA, the Enzyme Database: 1.2.1.105
LinkDB

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