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)
3.50.50.60 : FAD/NAD(P)-binding domain M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00025 T00211 T00213 T00233 T00242
3.30.390.30 : Enolase-like; domain 1 M00163 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
15846
16908
15378
PubChem 643975
5893
439153
1038
1ebdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1ebdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1lpfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1lpfB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1lvlA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
3ladA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
3ladB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
2a8xA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
2a8xB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1ebdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ebdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1lpfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1lpfB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1lvlA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAD Unbound Unbound Unbound
3ladA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3ladB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2a8xA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2a8xB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ebdA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ebdB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1lpfA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1lpfB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1lvlA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3ladA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3ladB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2a8xA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2a8xB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 22;CYS 47;CYS 52
1ebdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 22;CYS 47;CYS 52
1lpfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 16;CYS 48;CYS 53
1lpfB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 16;CYS 48;CYS 53
1lvlA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 18;CYS 43;CYS 48
3ladA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 16;CYS 48;CYS 53
3ladB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 16;CYS 48;CYS 53
2a8xA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 16;CYS 41;CYS 46
2a8xB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 16;CYS 41;CYS 46
1ebdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ebdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lpfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lpfB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lvlA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3ladA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3ladB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2a8xA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2a8xB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ebdA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 446; invisible H466
1ebdB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 446; invisible H466
1lpfA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 450;HIS 470
1lpfB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 450;HIS 470
1lvlA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 437;HIS 457
3ladA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 450;HIS 470
3ladB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 450;HIS 470
2a8xA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 443;ASN 463
2a8xB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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. Spectral properties of wild type and mutated enzymes.
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. A comparison with the structure of glutathione reductase.
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. Kinetics of wild-type and mutated enzymes.
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. The role of the C-terminus in catalysis and dimer stabilization.
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. Analysis of redox and thermostability properties.
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. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design.
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. Effects on properties of flavoprotein disulfide oxidoreductases.
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. The central role of the lipoyl domain.
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, lipoamide dehydrogenase from yeast.
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. Crystal structures of H- and L-proteins.
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. 1. Biochemical studies.
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), pyruvate decarboxylase(E2), and dihydrolipoamide dehydrogenase(E3). Moreover, it is homologous to the L protein of glycine cleavage system (M00163 in EzCatDB).
According to the literature [36], this enzyme catalyzes the following reactions:
(A) Hydride transfer from NADH to FAD, giving reduced flavin (FADH2):
(B) Electron transfer from FADH2 to the redox-active disulfide bond (Cys-Cys), giving the oxidized flavin (FAD):
(C) Electron transfer from the active site cysteine residues to lipoamide substrate, giving dihyrolipoamide and the disulfide bond of the cysteine residues.
In the so-called reductive half-reaction, the reactions, (A) and (B), occur.
In the so-called oxidative half-reaction, the reaction, (C), occurs subsequently.

Created Updated
2004-12-22 2009-03-12