DB code: T00017
| CATH domain | 3.50.50.60 : FAD/NAD(P)-binding domain | Catalytic domain |
|---|---|---|
| 3.50.50.60 : FAD/NAD(P)-binding domain | ||
| 3.30.390.30 : Enolase-like; domain 1 | Catalytic domain | |
| E.C. | 1.8.1.4 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.30.390.30 : Enolase-like; domain 1 | M00163 T00213 T00233 T00242 |
| 3.50.50.60 : FAD/NAD(P)-binding domain | M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00025 T00211 T00213 T00233 T00242 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam | RefSeq |
|---|---|---|---|---|
| P11959 |
Dihydrolipoyl dehydrogenase
|
EC
1.8.1.4
Dihydrolipoamide dehydrogenase E3 component of pyruvate complex |
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
|
| P14218 |
Dihydrolipoyl dehydrogenase
|
EC
1.8.1.4
Dihydrolipoamide dehydrogenase E3 component of 2-oxoglutarate dehydrogenase complex |
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
|
| P09063 |
Dihydrolipoyl dehydrogenase
|
EC
1.8.1.4
Dihydrolipoamide dehydrogenase LPD-Val E3 component of branched-chain alpha-keto acid dehydrogenase complex |
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
|
| P18925 |
Dihydrolipoyl dehydrogenase
|
EC
1.8.1.4
Dihydrolipoamide dehydrogenase E3 component of pyruvate complex |
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
|
| P66004 |
Dihydrolipoyl dehydrogenase
|
EC
1.8.1.4
Dihydrolipoamide dehydrogenase E3 component of alpha keto acid dehydrogenase complexes |
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
NP_214976.1
(Protein)
NC_000962.3 (DNA/RNA sequence) NP_334888.1 (Protein) NC_002755.2 (DNA/RNA sequence) YP_006513791.1 (Protein) NC_018143.1 (DNA/RNA sequence) |
| KEGG enzyme name |
|---|
|
dihydrolipoyl dehydrogenase
LDP-Glc LDP-Val dehydrolipoate dehydrogenase diaphorase dihydrolipoamide dehydrogenase dihydrolipoamide:NAD+ oxidoreductase dihydrolipoic dehydrogenase dihydrothioctic dehydrogenase lipoamide dehydrogenase (NADH) lipoamide oxidoreductase (NADH) lipoamide reductase lipoamide reductase (NADH) lipoate dehydrogenase lipoic acid dehydrogenase lipoyl dehydrogenase protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P11959 | DLDH1_BACST | Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. | Homodimer. Identified in a complex with pdhC. | Cytoplasm. | Binds 1 FAD per subunit. |
| P14218 | DLDH_PSEFL | Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. | Homodimer. | Cytoplasm. | Binds 1 FAD per subunit. |
| P09063 | DLDH1_PSEPU | Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. | Homodimer. | Cytoplasm. | Binds 1 FAD per subunit (By similarity). |
| P18925 | DLDH_AZOVI | Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. | Homodimer. | Cytoplasm. | Binds 1 FAD per subunit. |
| P66004 | DLDH_MYCTU | Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. | Homodimer. | Cytoplasm (Potential). | Binds 1 FAD per subunit. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00010 | Glycolysis / Gluconeogenesis | |
| MAP00020 | Citrate cycle (TCA cycle) | |
| MAP00260 | Glycine, serine and threonine metabolism | |
| MAP00280 | Valine, leucine and isoleucine degradation | |
| MAP00620 | Pyruvate metabolism |
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00016 | C00003 | C02972 | C00004 | C02051 | C00080 | ||||||
| E.C. | ||||||||||||
| Compound | FAD | NAD+ | Dihydrolipoylprotein | NADH | Lipoylprotein | H+ | ||||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | amide group,amine group,nucleotide | carbohydrate,lipid,peptide/protein,sulfhydryl group | amide group,amine group,nucleotide | disulfide bond,lipid,peptide/protein | others | ||||||
| ChEBI |
16238 16238 |
15846 15846 |
16908 16908 |
15378 15378 |
||||||||
| PubChem |
643975 643975 |
5893 5893 |
439153 439153 |
1038 1038 |
||||||||
| 1ebdA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1ebdB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1lpfA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1lpfB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1lvlA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 3ladA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 3ladB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 2a8xA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 2a8xB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1ebdA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ebdB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lpfA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lpfB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lvlA02 |
|
|
|
|
|
Unbound | Bound:NAD | Unbound | Unbound | Unbound | ||
| 3ladA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3ladB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2a8xA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2a8xB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ebdA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ebdB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lpfA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lpfB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lvlA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3ladA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3ladB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2a8xA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2a8xB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P11959, P09063, P18925, P14218 & literature [19], [36] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1ebdA01 |
|
|
|
|
|
TYR 22;CYS 47;CYS 52 | ||||
| 1ebdB01 |
|
|
|
|
|
TYR 22;CYS 47;CYS 52 | ||||
| 1lpfA01 |
|
|
|
|
|
TYR 16;CYS 48;CYS 53 | ||||
| 1lpfB01 |
|
|
|
|
|
TYR 16;CYS 48;CYS 53 | ||||
| 1lvlA01 |
|
|
|
|
|
TYR 18;CYS 43;CYS 48 | ||||
| 3ladA01 |
|
|
|
|
|
TYR 16;CYS 48;CYS 53 | ||||
| 3ladB01 |
|
|
|
|
|
TYR 16;CYS 48;CYS 53 | ||||
| 2a8xA01 |
|
|
|
|
|
TYR 16;CYS 41;CYS 46 | ||||
| 2a8xB01 |
|
|
|
|
|
TYR 16;CYS 41;CYS 46 | ||||
| 1ebdA02 |
|
|
|
|
|
|||||
| 1ebdB02 |
|
|
|
|
|
|||||
| 1lpfA02 |
|
|
|
|
|
|||||
| 1lpfB02 |
|
|
|
|
|
|||||
| 1lvlA02 |
|
|
|
|
|
|||||
| 3ladA02 |
|
|
|
|
|
|||||
| 3ladB02 |
|
|
|
|
|
|||||
| 2a8xA02 |
|
|
|
|
|
|||||
| 2a8xB02 |
|
|
|
|
|
|||||
| 1ebdA03 |
|
|
|
|
|
HIS 446; | invisible H466 | |||
| 1ebdB03 |
|
|
|
|
|
HIS 446; | invisible H466 | |||
| 1lpfA03 |
|
|
|
|
|
HIS 450;HIS 470 | ||||
| 1lpfB03 |
|
|
|
|
|
HIS 450;HIS 470 | ||||
| 1lvlA03 |
|
|
|
|
|
HIS 437;HIS 457 | ||||
| 3ladA03 |
|
|
|
|
|
HIS 450;HIS 470 | ||||
| 3ladB03 |
|
|
|
|
|
HIS 450;HIS 470 | ||||
| 2a8xA03 |
|
|
|
|
|
HIS 443;ASN 463 | ||||
| 2a8xB03 |
|
|
|
|
|
HIS 443;ASN 463 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
Scheme I, Scheme II | |
|
[7]
|
Scheme 2 | |
|
[10]
|
p.989 | |
|
[12]
|
Scheme I, Scheme II, p.3070-3072 | |
|
[13]
|
Scheme 1, Scheme 2 | |
|
[17]
|
||
|
[19]
|
||
|
[36]
|
Scheme 1, Scheme 5 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6894226 |
| Journal | Arch Biochem Biophys |
| Year | 1981 |
| Volume | 206 |
| Pages | 77-86 |
| Authors | Tsai CS, Templeton DM, Wand AJ |
| Title | Multifunctionality of lipoamide dehydrogenase: activities of chemically trapped monomeric and dimeric enzymes. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6688532 |
| Journal | Biochemistry |
| Year | 1983 |
| Volume | 22 |
| Pages | 3792-6 |
| Authors | O'Donnell ME, Johnson FA, Williams CH Jr |
| Title | Proton nuclear magnetic resonance investigation of the mechanism of flavin C-4a adduct formation induced by oxidized nicotinamide adenine dinucleotide binding to monoalkylated pig heart lipoamide dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6546954 |
| Journal | J Mol Biol |
| Year | 1984 |
| Volume | 174 |
| Pages | 483-96 |
| Authors | Rice DW, Schulz GE, Guest JR |
| Title | Structural relationship between glutathione reductase and lipoamide dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3292518 |
| Journal | J Biochem (Tokyo) |
| Year | 1988 |
| Volume | 103 |
| Pages | 463-9 |
| Authors | Takenaka A, Kizawa K, Hata T, Sato S, Misaka E, Tamura C, Sasada Y |
| Title | X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2716052 |
| Journal | J Mol Biol |
| Year | 1989 |
| Volume | 206 |
| Pages | 365-79 |
| Authors | Schierbeek AJ, Swarte MB, Dijkstra BW, Vriend G, Read RJ, Hol WG, Drenth J, Betzel C |
| Title | X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2176163 |
| Journal | FEBS Lett |
| Year | 1990 |
| Volume | 276 |
| Pages | 189-91 |
| Authors | Shi XL, Dalal NS |
| Title | NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1684937 |
| Journal | Eur J Biochem |
| Year | 1991 |
| Volume | 202 |
| Pages | 863-72 |
| Authors | Benen J, van Berkel W, Zak Z, Visser T, Veeger C, de Kok A |
| Title |
Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1765065 |
| Journal | Eur J Biochem |
| Year | 1991 |
| Volume | 202 |
| Pages | 1049-55 |
| Authors | van Berkel WJ, Regelink AG, Beintema JJ, de Kok A |
| Title | The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1652585 |
| Journal | J Biochem (Tokyo) |
| Year | 1991 |
| Volume | 109 |
| Pages | 450-4 |
| Authors | Bando Y, Aki K |
| Title | Mechanisms of generation of oxygen radicals and reductive mobilization of ferritin iron by lipoamide dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). |
| Medline ID | 91350192 |
| PubMed ID | 1880807 |
| Journal | J Mol Biol |
| Year | 1991 |
| Volume | 220 |
| Pages | 975-94 |
| Authors | Mattevi A, Schierbeek AJ, Hol WG |
| Title |
Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. |
| Related PDB | 3lad |
| Related UniProtKB | P18925 |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1456954 |
| Journal | Biochem Int |
| Year | 1992 |
| Volume | 28 |
| Pages | 323-34 |
| Authors | Sreider CM, Grinblat L, Stoppani AO |
| Title | Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: role of flavin and the reactive disulfide groups. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1554695 |
| Journal | Biochemistry |
| Year | 1992 |
| Volume | 31 |
| Pages | 3065-72 |
| Authors | Leichus BN, Blanchard JS |
| Title | Pig heart lipoamide dehydrogenase: solvent equilibrium and kinetic isotope effects. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1633804 |
| Journal | Eur J Biochem |
| Year | 1992 |
| Volume | 207 |
| Pages | 487-97 |
| Authors | Benen J, van Berkel W, Dieteren N, Arscott D, Williams C Jr, Veeger C, de Kok A |
| Title |
Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1633805 |
| Journal | Eur J Biochem |
| Year | 1992 |
| Volume | 207 |
| Pages | 499-505 |
| Authors | Benen J, van Berkel W, Veeger C, de Kok A |
| Title |
Lipoamide dehydrogenase from Azotobacter vinelandii. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1451916 |
| Journal | Int J Biochem |
| Year | 1992 |
| Volume | 24 |
| Pages | 1801-6 |
| Authors | Tsai CS, Wand AJ |
| Title | pH dependent kinetic studies of lipoamide dehydrogenase catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1347528 |
| Journal | J Biol Chem |
| Year | 1992 |
| Volume | 267 |
| Pages | 5128-32 |
| Authors | Kim H, Patel MS |
| Title | Characterization of two site-specifically mutated human dihydrolipoamide dehydrogenases (His-452----Gln and Glu-457----Gln). |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). |
| Medline ID | 92390345 |
| PubMed ID | 1325638 |
| Journal | Proteins |
| Year | 1992 |
| Volume | 13 |
| Pages | 336-51 |
| Authors | Mattevi A, Obmolova G, Sokatch JR, Betzel C, Hol WG |
| Title | The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution. |
| Related PDB | 1lvl |
| Related UniProtKB | P09063 |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8385902 |
| Journal | Arch Biochem Biophys |
| Year | 1993 |
| Volume | 302 |
| Pages | 300-3 |
| Authors | Shi X, Dalal NS |
| Title | One-electron reduction of vanadium(V) by flavoenzymes/NADPH. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
| Medline ID | 93253780 |
| PubMed ID | 8487301 |
| Journal | J Mol Biol |
| Year | 1993 |
| Volume | 230 |
| Pages | 1200-15 |
| Authors | Mattevi A, Obmolova G, Kalk KH, van Berkel WJ, Hol WG |
| Title |
Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. |
| Related PDB | 1lpf |
| Related UniProtKB | P14218 |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8575446 |
| Journal | Eur J Biochem |
| Year | 1995 |
| Volume | 234 |
| Pages | 861-70 |
| Authors | Westphal AH, Fabisz-Kijowska A, Kester H, Obels PP, de Kok A |
| Title | The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7672506 |
| Journal | FASEB J |
| Year | 1995 |
| Volume | 9 |
| Pages | 1138-46 |
| Authors | Krauth-Siegel RL, Schoneck R |
| Title |
Flavoprotein structure and mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7499374 |
| Journal | J Biol Chem |
| Year | 1995 |
| Volume | 270 |
| Pages | 28586-94 |
| Authors | Murthy YV, Massey V |
| Title |
Chemical modification of the N-10 ribityl side chain of flavins. |
| Related PDB | |
| Related UniProtKB | |
| [23] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
| Medline ID | 96398614 |
| PubMed ID | 8805537 |
| Journal | Structure |
| Year | 1996 |
| Volume | 4 |
| Pages | 277-86 |
| Authors | Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG |
| Title | Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. |
| Related PDB | 1ebd |
| Related UniProtKB | P11959 |
| [24] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9143318 |
| Journal | Arch Biochem Biophys |
| Year | 1997 |
| Volume | 340 |
| Pages | 168-76 |
| Authors | Marcinkeviciene J, Blanchard JS |
| Title | Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis. |
| Related PDB | |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9278141 |
| Journal | Biol Chem |
| Year | 1997 |
| Volume | 378 |
| Pages | 617-34 |
| Authors | Berg A, de Kok A |
| Title |
2-Oxo acid dehydrogenase multienzyme complexes. |
| Related PDB | |
| Related UniProtKB | |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9193005 |
| Journal | J Mol Biol |
| Year | 1997 |
| Volume | 269 |
| Pages | 129-41 |
| Authors | Li de la Sierra I, Pernot L, Prange T, Saludjian P, Schiltz M, Fourme R, Padron G |
| Title | Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis. |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10047833 |
| Journal | Biochem Soc Trans |
| Year | 1998 |
| Volume | 26 |
| Pages | S319 |
| Authors | Rice L, Phoenix DA, Wainwright M, Waring JJ |
| Title | Effect of increasing methylation on the ability of methylene blue to cause diaphorase-catalysed oxidation of NADH. |
| Related PDB | |
| Related UniProtKB | |
| [28] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9538259 |
| Journal | J Biochem (Tokyo) |
| Year | 1998 |
| Volume | 123 |
| Pages | 668-74 |
| Authors | Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A |
| Title |
Crystal structure of eucaryotic E3, |
| Related PDB | 1jeh |
| Related UniProtKB | |
| [29] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10806386 |
| Journal | Eur J Biochem |
| Year | 2000 |
| Volume | 267 |
| Pages | 2890-8 |
| Authors | Faure M, Bourguignon J, Neuburger M, MacHerel D, Sieker L, Ober R, Kahn R, Cohen-Addad C, Douce R |
| Title |
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. |
| Related PDB | 1dxl |
| Related UniProtKB | |
| [30] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10806385 |
| Journal | Eur J Biochem |
| Year | 2000 |
| Volume | 267 |
| Pages | 2882-9 |
| Authors | Neuburger M, Polidori AM, Pietre E, Faure M, Jourdain A, Bourguignon J, Pucci B, Douce R |
| Title |
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. |
| Related PDB | |
| Related UniProtKB | |
| [31] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10970889 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 36665-70 |
| Authors | Lindsay H, Beaumont E, Richards SD, Kelly SM, Sanderson SJ, Price NC, Lindsay JG |
| Title | FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [32] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11390211 |
| Journal | Biosens Bioelectron |
| Year | 2001 |
| Volume | 16 |
| Pages | 245-52 |
| Authors | Eicher I, Schmidt HL |
| Title | Electrocatalytic reduction of lipoic acid and electroenzymatic reduction of NAD(P)(+) for integrated dehydrogenase biosensors. |
| Related PDB | |
| Related UniProtKB | |
| [33] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11559360 |
| Journal | Eur J Biochem |
| Year | 2001 |
| Volume | 268 |
| Pages | 4908-17 |
| Authors | Tozawa K, Broadhurst RW, Raine AR, Fuller C, Alvarez A, Guillen G, Padron G, Perham RN |
| Title | Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis. |
| Related PDB | |
| Related UniProtKB | |
| [34] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11170645 |
| Journal | J Med Chem |
| Year | 2001 |
| Volume | 44 |
| Pages | 548-65 |
| Authors | Salmon-Chemin L, Buisine E, Yardley V, Kohler S, Debreu MA, Landry V, Sergheraert C, Croft SL, Krauth-Siegel RL, Davioud-Charvet E |
| Title | 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity. |
| Related PDB | |
| Related UniProtKB | |
| [35] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12200115 |
| Journal | Biochem Biophys Res Commun |
| Year | 2002 |
| Volume | 296 |
| Pages | 779-84 |
| Authors | Bhushan B, Halasz A, Spain JC, Hawari J |
| Title | Diaphorase catalyzed biotransformation of RDX via N-denitration mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [36] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12463758 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 14580-90 |
| Authors | Argyrou A, Blanchard JS, Palfey BA |
| Title | The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [37] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11799204 |
| Journal | Science |
| Year | 2002 |
| Volume | 295 |
| Pages | 1073-7 |
| Authors | Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C |
| Title | Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. |
| Related PDB | |
| Related UniProtKB | |
| [38] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 16093239 |
| Journal | J Biol Chem |
| Year | 2005 |
| Volume | 280 |
| Pages | 33977-83 |
| Authors | Rajashankar KR, Bryk R, Kniewel R, Buglino JA, Nathan CF, Lima CD |
| Title | Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis. |
| Related PDB | 2a8x |
| Related UniProtKB | |
| [39] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15946682 |
| Journal | J Mol Biol |
| Year | 2005 |
| Volume | 350 |
| Pages | 543-52 |
| Authors | Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT |
| Title | Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. |
| Related PDB | 1zmc 1zmd |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme is one of the component of the pyruvate dehydrogenase multienzyme complex which is composed of dihydrolipoamide acetyltransferase(E1), According to the literature [36], (A) Hydride transfer from NADH to FAD, (B) Electron transfer from FADH2 to the redox-active disulfide bond (Cys-Cys), (C) Electron transfer from the active site cysteine residues to lipoamide substrate, In the so-called reductive half-reaction, In the so-called oxidative half-reaction, |
| Created | Updated |
|---|---|
| 2004-12-22 | 2009-03-12 |