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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.8.1.4

Accepted Name
Dihydrolipoyl dehydrogenase.
Alternative Name(s)
Dehydrolipoate dehydrogenase.
Diaphorase.
Dihydrolipoamide dehydrogenase.
Dihydrolipoic dehydrogenase.
Dihydrothioctic dehydrogenase.
E3 component of alpha-ketoacid dehydrogenase complexes.
Glycine-cleavage system L-protein.
L-protein.
LDP-Glc.
LDP-Val.
Lipoamide dehydrogenase (NADH).
Lipoamide oxidoreductase (NADH).
Lipoamide reductase.
Lipoamide reductase (NADH).
Lipoate dehydrogenase.
Lipoic acid dehydrogenase.
Lipoyl dehydrogenase.
Reaction catalysed
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) <=> protein N(6)-(lipoyl)lysine + NADH
Cofactor(s)
FAD.
Comment(s)
  • A component of the multienzyme 2-oxo-acid dehydrogenase complexes.
  • In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups.
  • It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes.
  • Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine.
  • It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate.
  • Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase.
  • The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein.
  • Formerly EC 1.6.4.3.
Cross-references
PROSITEPDOC00073
BRENDA1.8.1.4
EC2PDB1.8.1.4
ExplorEnz1.8.1.4
PRIAM enzyme-specific profiles1.8.1.4
KEGG Ligand Database for Enzyme Nomenclature1.8.1.4
IUBMB Enzyme Nomenclature1.8.1.4
IntEnz1.8.1.4
MEDLINEFind literature relating to 1.8.1.4
MetaCyc1.8.1.4
UniProtKB/Swiss-Prot
Q9M5K3, DLDH1_ARATH;  P21880, DLDH1_BACSU;  P11959, DLDH1_GEOSE;  
Q9I1L9, DLDH1_PSEAE;  P09063, DLDH1_PSEPU;  Q9M5K2, DLDH2_ARATH;  
P54533, DLDH2_BACSU;  Q5UYG6, DLDH2_HALMA;  Q9I3D1, DLDH2_PSEAE;  
P31052, DLDH2_PSEPU;  O34324, DLDH3_BACSU;  Q5UWH2, DLDH3_HALMA;  
Q9HUY1, DLDH3_PSEAE;  P31046, DLDH3_PSEPU;  P35484, DLDH_ACHLA;  
P18925, DLDH_AZOVI;  P57303, DLDH_BUCAI;  Q8K9T7, DLDH_BUCAP;  
Q89AQ8, DLDH_BUCBP;  O17953, DLDH_CAEEL;  P49819, DLDH_CANLF;  
Q9PJI3, DLDH_CHLMU;  O50311, DLDH_CHLP8;  Q9Z773, DLDH_CHLPN;  
Q8KCW2, DLDH_CHLTE;  O84561, DLDH_CHLTR;  Q8NTE1, DLDH_CORGL;  
Q8CIZ7, DLDH_CRIGR;  P52992, DLDH_CUPNH;  Q54EW8, DLDH_DICDI;  
P0A9P2, DLDH_ECO57;  P0A9P1, DLDH_ECOL6;  P0A9P0, DLDH_ECOLI;  
P43784, DLDH_HAEIN;  Q9HN74, DLDH_HALSA;  Q04829, DLDH_HALVD;  
P09622, DLDH_HUMAN;  P80647, DLDH_HYMDI;  Q60HG3, DLDH_MACFA;  
O18480, DLDH_MANSE;  Q811C4, DLDH_MESAU;  O08749, DLDH_MOUSE;  
P66005, DLDH_MYCBO;  P47513, DLDH_MYCGE;  Q50068, DLDH_MYCLE;  
P75393, DLDH_MYCPN;  P9WHH8, DLDH_MYCTO;  P9WHH9, DLDH_MYCTU;  
P31023, DLDH_PEA;  P09623, DLDH_PIG;  Q5R4B1, DLDH_PONAB;  
P84545, DLDH_POPEU;  P14218, DLDH_PSEFL;  Q6P6R2, DLDH_RAT;  
O05940, DLDH_RHIEC;  P95596, DLDH_RHOCA;  O00087, DLDH_SCHPO;  
P0A9P3, DLDH_SHIFL;  P80503, DLDH_SOLTU;  Q5HGY8, DLDH_STAAC;  
P0A0E6, DLDH_STAAM;  P99084, DLDH_STAAN;  Q6GHY9, DLDH_STAAR;  
Q6GAB8, DLDH_STAAS;  P0A0E8, DLDH_STAAU;  P0A0E7, DLDH_STAAW;  
P72740, DLDH_SYNY3;  P85207, DLDH_THESS;  Q04933, DLDH_TRYBB;  
P90597, DLDH_TRYCR;  Q9KPF6, DLDH_VIBCH;  O50286, DLDH_VIBPA;  
P09624, DLDH_YEAST;  P50970, DLDH_ZYMMO;  A8MS68, PLPD1_ARATH;  
F4JLP5, PLPD2_ARATH;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-