ID   1.8.1.4
DE   dihydrolipoyl dehydrogenase.
AN   dehydrolipoate dehydrogenase.
AN   diaphorase.
AN   dihydrolipoamide dehydrogenase.
AN   dihydrolipoic dehydrogenase.
AN   dihydrothioctic dehydrogenase.
AN   E3 component of alpha-ketoacid dehydrogenase complexes.
AN   glycine-cleavage system L-protein.
AN   LDP-Glc.
AN   LDP-Val.
AN   lipoamide dehydrogenase (NADH).
AN   lipoamide oxidoreductase (NADH).
AN   lipoamide reductase.
AN   lipoamide reductase (NADH).
AN   lipoate dehydrogenase.
AN   lipoic acid dehydrogenase.
AN   lipoyl dehydrogenase.
AN   L-protein.
CA   N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-
CA   lipoyl]-L-lysyl-[protein] + NADH.
CC   -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes.
CC   -!- In the pyruvate dehydrogenase complex, it binds to the core of
CC       EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups.
CC   -!- It plays a similar role in the oxoglutarate and 3-methyl-2-
CC       oxobutanoate dehydrogenase complexes.
CC   -!- Another substrate is the dihydrolipoyl group in the H-protein of the
CC       glycine-cleavage system, in which it acts, together with EC 1.4.4.2
CC       and EC 2.1.2.10 to break down glycine.
CC   -!- It can also use free dihydrolipoate, dihydrolipoamide or
CC       dihydrolipoyllysine as substrate.
CC   -!- Was first shown to catalyze the oxidation of NADH by methylene blue;
CC       this activity was called diaphorase.
CC   -!- The glycine cleavage system is composed of four components that only
CC       loosely associate: the P protein (EC 1.4.4.2), the T protein
CC       (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H
CC       protein.
CC   -!- Formerly EC 1.6.4.3.
DR   Q9M5K3, DLDH1_ARATH;  P21880, DLDH1_BACSU;  P11959, DLDH1_GEOSE;
DR   Q9I1L9, DLDH1_PSEAE;  P09063, DLDH1_PSEPU;  Q9M5K2, DLDH2_ARATH;
DR   P54533, DLDH2_BACSU;  Q5UYG6, DLDH2_HALMA;  Q9I3D1, DLDH2_PSEAE;
DR   P31052, DLDH2_PSEPU;  O34324, DLDH3_BACSU;  Q5UWH2, DLDH3_HALMA;
DR   Q9HUY1, DLDH3_PSEAE;  P31046, DLDH3_PSEPU;  P35484, DLDH_ACHLA ;
DR   P18925, DLDH_AZOVI ;  F1N206, DLDH_BOVIN ;  P57303, DLDH_BUCAI ;
DR   Q8K9T7, DLDH_BUCAP ;  Q89AQ8, DLDH_BUCBP ;  O17953, DLDH_CAEEL ;
DR   P49819, DLDH_CANLF ;  G0SB20, DLDH_CHATD ;  Q9PJI3, DLDH_CHLMU ;
DR   O50311, DLDH_CHLP8 ;  Q9Z773, DLDH_CHLPN ;  Q8KCW2, DLDH_CHLTE ;
DR   O84561, DLDH_CHLTR ;  Q8NTE1, DLDH_CORGL ;  Q8CIZ7, DLDH_CRIGR ;
DR   P52992, DLDH_CUPNH ;  Q54EW8, DLDH_DICDI ;  P0A9P2, DLDH_ECO57 ;
DR   P0A9P1, DLDH_ECOL6 ;  P0A9P0, DLDH_ECOLI ;  P43784, DLDH_HAEIN ;
DR   Q9HN74, DLDH_HALSA ;  Q04829, DLDH_HALVD ;  P09622, DLDH_HUMAN ;
DR   P80647, DLDH_HYMDI ;  Q60HG3, DLDH_MACFA ;  O18480, DLDH_MANSE ;
DR   Q811C4, DLDH_MESAU ;  O08749, DLDH_MOUSE ;  P66005, DLDH_MYCBO ;
DR   P47513, DLDH_MYCGE ;  Q50068, DLDH_MYCLE ;  P75393, DLDH_MYCPN ;
DR   P9WHH8, DLDH_MYCTO ;  P9WHH9, DLDH_MYCTU ;  P31023, DLDH_PEA   ;
DR   P09623, DLDH_PIG   ;  Q5R4B1, DLDH_PONAB ;  P84545, DLDH_POPEU ;
DR   P14218, DLDH_PSEFL ;  Q6P6R2, DLDH_RAT   ;  O05940, DLDH_RHIEC ;
DR   P95596, DLDH_RHOCA ;  O00087, DLDH_SCHPO ;  P0A9P3, DLDH_SHIFL ;
DR   P80503, DLDH_SOLTU ;  Q5HGY8, DLDH_STAAC ;  P0A0E6, DLDH_STAAM ;
DR   P99084, DLDH_STAAN ;  Q6GHY9, DLDH_STAAR ;  Q6GAB8, DLDH_STAAS ;
DR   P0A0E8, DLDH_STAAU ;  P0A0E7, DLDH_STAAW ;  P72740, DLDH_SYNY3 ;
DR   P85207, DLDH_THESS ;  Q04933, DLDH_TRYBB ;  P90597, DLDH_TRYCR ;
DR   Q9KPF6, DLDH_VIBCH ;  O50286, DLDH_VIBPA ;  P09624, DLDH_YEAST ;
DR   P50970, DLDH_ZYMMO ;  A8MS68, PLPD1_ARATH;  F4JLP5, PLPD2_ARATH;
//