T00017
type: Enzyme
cath: FAD/NAD(P)-binding domain
cath: Enolase-like; domain 1
ec: https://purl.uniprot.org/enzyme/1.8.1.4
uniprot: P11959
uniprot: P14218
uniprot: P09063
uniprot: P18925
uniprot: P66004
kegg enzyme: dihydrolipoyl dehydrogenase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Citrate cycle (TCA cycle)
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Valine, leucine and isoleucine degradation
kegg pathway: Pyruvate metabolism
kegg cofactor: FAD
kegg substrate: NAD+
kegg substrate: Dihydrolipoylprotein
kegg product: NADH
kegg product: Lipoylprotein
kegg product: H+
pdb: 1ebdA01
pdb: 1ebdB01
pdb: 1lpfA01
pdb: 1lpfB01
pdb: 1lvlA01
pdb: 3ladA01
pdb: 3ladB01
pdb: 2a8xA01
pdb: 2a8xB01
pdb: 1ebdA02
pdb: 1ebdB02
pdb: 1lpfA02
pdb: 1lpfB02
pdb: 1lvlA02
pdb: 3ladA02
pdb: 3ladB02
pdb: 2a8xA02
pdb: 2a8xB02
pdb: 1ebdA03
pdb: 1ebdB03
pdb: 1lpfA03
pdb: 1lpfB03
pdb: 1lvlA03
pdb: 3ladA03
pdb: 3ladB03
pdb: 2a8xA03
pdb: 2a8xB03
active site residues resources: The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex.
active site residues resources: Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein.
active site residues resources: P11959
active site residues resources: P09063
active site residues resources: P18925
active site residues resources: P14218
references: Pig heart lipoamide dehydrogenase: solvent equilibrium and kinetic isotope effects.
references: Multifunctionality of lipoamide dehydrogenase: activities of chemically trapped monomeric and dimeric enzymes.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/T00017#2
references: Structural relationship between glutathione reductase and lipoamide dehydrogenase.
references: X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method.
references: X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques.
references: NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals.
references: Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes.
references: The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii.
references: Mechanisms of generation of oxygen radicals and reductive mobilization of ferritin iron by lipoamide dehydrogenase.
references: Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase.
references: Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: role of flavin and the reactive disulfide groups.
references: Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes.
references: Lipoamide dehydrogenase from Azotobacter vinelandii. The role of the C-terminus in catalysis and dimer stabilization.
references: pH dependent kinetic studies of lipoamide dehydrogenase catalysis.
references: Characterization of two site-specifically mutated human dihydrolipoamide dehydrogenases (His-452----Gln and Glu-457----Gln).
references: The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution.
references: One-electron reduction of vanadium(V) by flavoenzymes/NADPH.
references: Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties.
references: The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex.
references: Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design.
references: Chemical modification of the N-10 ribityl side chain of flavins. Effects on properties of flavoprotein disulfide oxidoreductases.
references: Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
references: Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis.
references: 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain.
references: Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis.

FAD/NAD(P)-binding domain
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.50.50.60
catalytic domain: index.html

Enolase-like; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.390.30
catalytic domain: index.html

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Citrate cycle (TCA cycle)
type: KeggPathway
references: KEGG:MAP00020

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260

Valine, leucine and isoleucine degradation
type: KeggPathway
references: KEGG:MAP00280

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620

FAD
type: KeggCofactor
references: KEGG:C00016
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Dihydrolipoylprotein
type: KeggSubstrate
references: KEGG:C02972
compound type: carbohydrate
compound type: lipid
compound type: peptide/protein
compound type: sulfhydryl group

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Lipoylprotein
type: KeggProduct
references: KEGG:C02051
compound type: disulfide bond
compound type: lipid
compound type: peptide/protein

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1ebdA01
type: Pdb
references: 1ebd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebd
catalytic residue: TYR 22;CYS 47;CYS 52

1ebdB01
type: Pdb
references: 1ebd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebd
catalytic residue: TYR 22;CYS 47;CYS 52

1lpfA01
type: Pdb
references: 1lpf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lpf
catalytic residue: TYR 16;CYS 48;CYS 53

1lpfB01
type: Pdb
references: 1lpf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lpf
catalytic residue: TYR 16;CYS 48;CYS 53

1lvlA01
type: Pdb
references: 1lvl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lvl
catalytic residue: TYR 18;CYS 43;CYS 48

3ladA01
type: Pdb
references: 3lad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3lad
catalytic residue: TYR 16;CYS 48;CYS 53

3ladB01
type: Pdb
references: 3lad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3lad
catalytic residue: TYR 16;CYS 48;CYS 53

2a8xA01
type: Pdb
references: 2a8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a8x
catalytic residue: TYR 16;CYS 41;CYS 46

2a8xB01
type: Pdb
references: 2a8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a8x
catalytic residue: TYR 16;CYS 41;CYS 46

1ebdA03
type: Pdb
references: 1ebd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebd
catalytic residue: HIS 446;
comment: invisible H466

1ebdB03
type: Pdb
references: 1ebd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebd
catalytic residue: HIS 446;
comment: invisible H466

1lpfA03
type: Pdb
references: 1lpf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lpf
catalytic residue: HIS 450;HIS 470

1lpfB03
type: Pdb
references: 1lpf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lpf
catalytic residue: HIS 450;HIS 470

1lvlA03
type: Pdb
references: 1lvl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lvl
catalytic residue: HIS 437;HIS 457

3ladA03
type: Pdb
references: 3lad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3lad
catalytic residue: HIS 450;HIS 470

3ladB03
type: Pdb
references: 3lad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3lad
catalytic residue: HIS 450;HIS 470

2a8xA03
type: Pdb
references: 2a8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a8x
catalytic residue: HIS 443;ASN 463

2a8xB03
type: Pdb
references: 2a8x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a8x
catalytic residue: HIS 443;ASN 463

Pig heart lipoamide dehydrogenase: solvent equilibrium and kinetic isotope effects.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1554695
journal: Biochemistry
volume: 31
pages: 3065-72
published year: 1992
authors:
  item: Leichus BN
  item: Blanchard JS

Multifunctionality of lipoamide dehydrogenase: activities of chemically trapped monomeric and dimeric enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6894226
journal: Arch Biochem Biophys
volume: 206
pages: 77-86
published year: 1981
authors:
  item: Tsai CS
  item: Templeton DM
  item: Wand AJ

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00017#2
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6688532
journal: Biochemistry
volume: 22
pages: 3792-6
published year: 1983
authors:
  item: O'Donnell ME
  item: Johnson FA
  item: 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.

Structural relationship between glutathione reductase and lipoamide dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6546954
journal: J Mol Biol
volume: 174
pages: 483-96
published year: 1984
authors:
  item: Rice DW
  item: Schulz GE
  item: Guest JR

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3292518
journal: J Biochem (Tokyo)
volume: 103
pages: 463-9
published year: 1988
authors:
  item: Takenaka A
  item: Kizawa K
  item: Hata T
  item: Sato S
  item: Misaka E
  item: Tamura C
  item: Sasada Y

X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2716052
journal: J Mol Biol
volume: 206
pages: 365-79
published year: 1989
authors:
  item: Schierbeek AJ
  item: Swarte MB
  item: Dijkstra BW
  item: Vriend G
  item: Read RJ
  item: Hol WG
  item: Drenth J
  item: Betzel C

NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2176163
journal: FEBS Lett
volume: 276
pages: 189-91
published year: 1990
authors:
  item: Shi XL
  item: Dalal NS

Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1684937
journal: Eur J Biochem
volume: 202
pages: 863-72
published year: 1991
authors:
  item: Benen J
  item: van Berkel W
  item: Zak Z
  item: Visser T
  item: Veeger C
  item: de Kok A

The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1765065
journal: Eur J Biochem
volume: 202
pages: 1049-55
published year: 1991
authors:
  item: van Berkel WJ
  item: Regelink AG
  item: Beintema JJ
  item: de Kok A

Mechanisms of generation of oxygen radicals and reductive mobilization of ferritin iron by lipoamide dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1652585
journal: J Biochem (Tokyo)
volume: 109
pages: 450-4
published year: 1991
authors:
  item: Bando Y
  item: Aki K

Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 91350192
references: http://www.ncbi.nlm.nih.gov/pubmed/1880807
journal: J Mol Biol
volume: 220
pages: 975-94
published year: 1991
authors:
  item: Mattevi A
  item: Schierbeek AJ
  item: Hol WG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P18925

Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: role of flavin and the reactive disulfide groups.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1456954
journal: Biochem Int
volume: 28
pages: 323-34
published year: 1992
authors:
  item: Sreider CM
  item: Grinblat L
  item: Stoppani AO

Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1633804
journal: Eur J Biochem
volume: 207
pages: 487-97
published year: 1992
authors:
  item: Benen J
  item: van Berkel W
  item: Dieteren N
  item: Arscott D
  item: Williams C Jr
  item: Veeger C
  item: de Kok A

Lipoamide dehydrogenase from Azotobacter vinelandii. The role of the C-terminus in catalysis and dimer stabilization.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1633805
journal: Eur J Biochem
volume: 207
pages: 499-505
published year: 1992
authors:
  item: Benen J
  item: van Berkel W
  item: Veeger C
  item: de Kok A

pH dependent kinetic studies of lipoamide dehydrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1451916
journal: Int J Biochem
volume: 24
pages: 1801-6
published year: 1992
authors:
  item: Tsai CS
  item: Wand AJ

Characterization of two site-specifically mutated human dihydrolipoamide dehydrogenases (His-452----Gln and Glu-457----Gln).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1347528
journal: J Biol Chem
volume: 267
pages: 5128-32
published year: 1992
authors:
  item: Kim H
  item: Patel MS

The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
medline id: 92390345
references: http://www.ncbi.nlm.nih.gov/pubmed/1325638
journal: Proteins
volume: 13
pages: 336-51
published year: 1992
authors:
  item: Mattevi A
  item: Obmolova G
  item: Sokatch JR
  item: Betzel C
  item: Hol WG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P09063

One-electron reduction of vanadium(V) by flavoenzymes/NADPH.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8385902
journal: Arch Biochem Biophys
volume: 302
pages: 300-3
published year: 1993
authors:
  item: Shi X
  item: Dalal NS

Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
medline id: 93253780
references: http://www.ncbi.nlm.nih.gov/pubmed/8487301
journal: J Mol Biol
volume: 230
pages: 1200-15
published year: 1993
authors:
  item: Mattevi A
  item: Obmolova G
  item: Kalk KH
  item: van Berkel WJ
  item: Hol WG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P14218

The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8575446
journal: Eur J Biochem
volume: 234
pages: 861-70
published year: 1995
authors:
  item: Westphal AH
  item: Fabisz-Kijowska A
  item: Kester H
  item: Obels PP
  item: de Kok A

Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7672506
journal: FASEB J
volume: 9
pages: 1138-46
published year: 1995
authors:
  item: Krauth-Siegel RL
  item: Schoneck R

Chemical modification of the N-10 ribityl side chain of flavins. Effects on properties of flavoprotein disulfide oxidoreductases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7499374
journal: J Biol Chem
volume: 270
pages: 28586-94
published year: 1995
authors:
  item: Murthy YV
  item: Massey V

Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
medline id: 96398614
references: http://www.ncbi.nlm.nih.gov/pubmed/8805537
journal: Structure
volume: 4
pages: 277-86
published year: 1996
authors:
  item: Mande SS
  item: Sarfaty S
  item: Allen MD
  item: Perham RN
  item: Hol WG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P11959

Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9143318
journal: Arch Biochem Biophys
volume: 340
pages: 168-76
published year: 1997
authors:
  item: Marcinkeviciene J
  item: Blanchard JS

2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9278141
journal: Biol Chem
volume: 378
pages: 617-34
published year: 1997
authors:
  item: Berg A
  item: de Kok A

Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9193005
journal: J Mol Biol
volume: 269
pages: 129-41
published year: 1997
authors:
  item: Li de la Sierra I
  item: Pernot L
  item: Prange T
  item: Saludjian P
  item: Schiltz M
  item: Fourme R
  item: Padron G

Effect of increasing methylation on the ability of methylene blue to cause diaphorase-catalysed oxidation of NADH.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10047833
journal: Biochem Soc Trans
volume: 26
pages: S319
published year: 1998
authors:
  item: Rice L
  item: Phoenix DA
  item: Wainwright M
  item: Waring JJ

Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9538259
journal: J Biochem (Tokyo)
volume: 123
pages: 668-74
published year: 1998
authors:
  item: Toyoda T
  item: Suzuki K
  item: Sekiguchi T
  item: Reed LJ
  item: Takenaka A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

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.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10806386
journal: Eur J Biochem
volume: 267
pages: 2890-8
published year: 2000
authors:
  item: Faure M
  item: Bourguignon J
  item: Neuburger M
  item: MacHerel D
  item: Sieker L
  item: Ober R
  item: Kahn R
  item: Cohen-Addad C
  item: Douce R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10806385
journal: Eur J Biochem
volume: 267
pages: 2882-9
published year: 2000
authors:
  item: Neuburger M
  item: Polidori AM
  item: Pietre E
  item: Faure M
  item: Jourdain A
  item: Bourguignon J
  item: Pucci B
  item: Douce R

FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10970889
journal: J Biol Chem
volume: 275
pages: 36665-70
published year: 2000
authors:
  item: Lindsay H
  item: Beaumont E
  item: Richards SD
  item: Kelly SM
  item: Sanderson SJ
  item: Price NC
  item: Lindsay JG

Electrocatalytic reduction of lipoic acid and electroenzymatic reduction of NAD(P)(+) for integrated dehydrogenase biosensors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11390211
journal: Biosens Bioelectron
volume: 16
pages: 245-52
published year: 2001
authors:
  item: Eicher I
  item: Schmidt HL

Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11559360
journal: Eur J Biochem
volume: 268
pages: 4908-17
published year: 2001
authors:
  item: Tozawa K
  item: Broadhurst RW
  item: Raine AR
  item: Fuller C
  item: Alvarez A
  item: Guillen G
  item: Padron G
  item: Perham RN

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00017#34
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11170645
journal: J Med Chem
volume: 44
pages: 548-65
published year: 2001
authors:
  item: Salmon-Chemin L
  item: Buisine E
  item: Yardley V
  item: Kohler S
  item: Debreu MA
  item: Landry V
  item: Sergheraert C
  item: Croft SL
  item: Krauth-Siegel RL
  item: 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.

Diaphorase catalyzed biotransformation of RDX via N-denitration mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12200115
journal: Biochem Biophys Res Commun
volume: 296
pages: 779-84
published year: 2002
authors:
  item: Bhushan B
  item: Halasz A
  item: Spain JC
  item: Hawari J

The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12463758
journal: Biochemistry
volume: 41
pages: 14580-90
published year: 2002
authors:
  item: Argyrou A
  item: Blanchard JS
  item: Palfey BA

Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11799204
journal: Science
volume: 295
pages: 1073-7
published year: 2002
authors:
  item: Bryk R
  item: Lima CD
  item: Erdjument-Bromage H
  item: Tempst P
  item: Nathan C

Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16093239
journal: J Biol Chem
volume: 280
pages: 33977-83
published year: 2005
authors:
  item: Rajashankar KR
  item: Bryk R
  item: Kniewel R
  item: Buglino JA
  item: Nathan CF
  item: Lima CD
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15946682
journal: J Mol Biol
volume: 350
pages: 543-52
published year: 2005
authors:
  item: Brautigam CA
  item: Chuang JL
  item: Tomchick DR
  item: Machius M
  item: Chuang DT
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

LDP-Glc
type: KeggEnzyme

LDP-Val
type: KeggEnzyme

dehydrolipoate dehydrogenase
type: KeggEnzyme

diaphorase
type: KeggEnzyme

dihydrolipoamide dehydrogenase
type: KeggEnzyme

dihydrolipoamide:NAD+ oxidoreductase
type: KeggEnzyme

dihydrolipoic dehydrogenase
type: KeggEnzyme

dihydrothioctic dehydrogenase
type: KeggEnzyme

lipoamide dehydrogenase (NADH)
type: KeggEnzyme

lipoamide oxidoreductase (NADH)
type: KeggEnzyme

lipoamide reductase
type: KeggEnzyme

lipoamide reductase (NADH)
type: KeggEnzyme

lipoate dehydrogenase
type: KeggEnzyme

lipoic acid dehydrogenase
type: KeggEnzyme

lipoyl dehydrogenase
type: KeggEnzyme

protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase
type: KeggEnzyme

ReferenceForCatalyticMechanism
reference index: 2
reference section: Scheme I, Scheme II

ReferenceForCatalyticMechanism
reference index: 7
reference section: Scheme 2

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.989

ReferenceForCatalyticMechanism
reference index: 12
reference section: Scheme I, Scheme II, p.3070-3072

ReferenceForCatalyticMechanism
reference index: 13
reference section: Scheme 1, Scheme 2

ReferenceForCatalyticMechanism
reference index: 17

ReferenceForCatalyticMechanism
reference index: 19

ReferenceForCatalyticMechanism
reference index: 36
reference section: Scheme 1, Scheme 5