S00319
type: Enzyme
rlcp: p8010
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.1.1.1
macie: M0255
uniprot: P10807
uniprot: P00334
kegg enzyme: alcohol dehydrogenase
kegg enzyme: aldehyde reductase
kegg enzyme: ADH
kegg enzyme: alcohol dehydrogenase (NAD)
kegg enzyme: aliphatic alcohol dehydrogenase
kegg enzyme: ethanol dehydrogenase
kegg enzyme: NAD-dependent alcohol dehydrogenase
kegg enzyme: NAD-specific aromatic alcohol dehydrogenase
kegg enzyme: NADH-alcohol dehydrogenase
kegg enzyme: NADH-aldehyde dehydrogenase
kegg enzyme: primary alcohol dehydrogenase
kegg enzyme: yeast alcohol dehydrogenase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Fatty acid metabolism
kegg pathway: Bile acid biosynthesis
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Tyrosine metabolism
kegg pathway: 1- and 2-Methylnaphthalene degradation
kegg pathway: 3-Chloroacrylic acid degradation
kegg pathway: Retinol metabolism
kegg pathway: Metabolism of xenobiotics by cytochrome P450
kegg pathway: Drug metabolism - cytochrome P450
kegg substrate: NAD+
kegg substrate: Alcohol
kegg product: NADH
kegg product: Aldehyde
kegg product: Ketone
kegg product: H+
pdb: 1a4uA
pdb: 1a4uB
pdb: 1b14A
pdb: 1b14B
pdb: 1b15A
pdb: 1b15B
pdb: 1b16A
pdb: 1b16B
pdb: 1b2lA
pdb: 1sbyA
pdb: 1sbyB
pdb: 1mg5A
pdb: 1mg5B
pdb bound state: Unbound
  compound: NAD+
  pdb: 1a4uA
active site residues resources: P10807
active site residues resources: 1a4u
references: The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster.
references: Secondary-structure prediction from the sequence of Drosophila melanogaster (fruitfly) alcohol dehydrogenase.
references: Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein.
references: The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration.
references: Mechanism of action of Drosophila melanogaster alcohol dehydrogenase.
references: Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability.
references: Kinetic interpretations of active site topologies and residue exchanges in Drosophila alcohol dehydrogenases.
references: Preliminary X-ray crystallographic studies on alcohol dehydrogenase from Drosophila.
references: Drosophila transcriptional repressor protein that binds specifically to negative control elements in fat body enhancers.
references: Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis.
references: The active site architecture of a short-chain dehydrogenase defined by site-directed mutagenesis and structure modeling.
references: Adding a positive charge at residue 46 of Drosophila alcohol dehydrogenase increases cofactor specificity for NADP+.
references: Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase.
references: Involvement of the C-terminal tail in the activity of Drosophila alcohol dehydrogenase. Evaluation of truncated proteins constructed by site-directed mutagenesis.
references: Structures important in mammalian 11 beta- and 17 beta-hydroxysteroid dehydrogenases.
references: Drosophila alcohol dehydrogenase: evaluation of Ser139 site-directed mutants.
references: Modeling studies of conformational changes in the substrate-binding loop in Drosophila alcohol dehydrogenase.
references: The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution.
references: Shaping of Drosophila alcohol dehydrogenase through evolution: relationship with enzyme functionality.
references: The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
references: The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies.
references: The Drosophila virilis alcohol dehydrogenase catalytic residues are conserved.
references: Structure-function relationships in Drosophila melanogaster alcohol dehydrogenase allozymes ADH(S), ADH(F) and ADH(UF), and distantly related forms.
references: Enzymic and structural studies on Drosophila alcohol dehydrogenase and other short-chain dehydrogenases/reductases.
references: The catalytic mechanism of Drosophila alcohol dehydrogenase: evidence for a proton relay modulated by the coupled ionization of the active site Lysine/Tyrosine pair and a NAD+ ribose OH switch.
references: Functional constraints of alcohol dehydrogenase (ADH) of tephritidae and relationships with other Dipteran species.
references: Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis.
references: Medium- and short-chain dehydrogenase/reductase gene and protein families : Structure-function relationships in short-chain alcohol dehydrogenases.
comment: (A0) Lys156 (of 1mg5) modulates the activity (or pKa) of Tyr152 via 2'-hydroxyl group of NAD, along with the N1 atom of the nicotinamide group in NAD, whereas Ser139 modulates the pKa of hydroxyl oxygen of the substrate. (A1) Tyr152 acts as a general base to deprotonate the hydroxyl oxygen of the substrate. Meanwhile, the hydride transfer (a pro-S hydride transfer) occurs from the carbon atom with the hydroxyl group of the substrate to the C4 atom of the nicotinamide. (B) Hydride transfer from NADH to substrate (Reduction): (B0) Lys156 modulates the activity (or pKa) of Tyr152 via 2'-hydroxyl group of NAD(P)H, along with the N1 atom of the nicotinamide group in NADH, whereas Ser139 modulates the pKa of carbonyl oxygen of the substrate. (B1) Tyr152 acts as a general acid to protonate the carbonyl oxygen of the substrate. Meanwhile, the hydride transfer occurs from the C4 atom of the nicotinamide to the carbonyl carbon of the substrate. Whilst this enzyme does not utilize a zinc ion for catalysis, its counterparts (homologous enzymes) from vertebrates (such as D00018 in EzCatDB) requires zinc ion for catalysis (see [5]). The catalytic mechanism of this enzyme must be similar to those of the homologous enzymes with the catalytic triad, Ser-Tyr-Lys (S00320, S00324, S00325, S00326, S00328, S00329, S00331, S00336 in EzCatDB). According to the literature [20] and [28], the reaction proceeds as follows: (A) Hydride transfer from substrate to NAD (Dehydrogenation):

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Fatty acid metabolism
type: KeggPathway
references: KEGG:MAP00071

Bile acid biosynthesis
type: KeggPathway
references: KEGG:MAP00120

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

Tyrosine metabolism
type: KeggPathway
references: KEGG:MAP00350

1- and 2-Methylnaphthalene degradation
type: KeggPathway
references: KEGG:MAP00624

3-Chloroacrylic acid degradation
type: KeggPathway
references: KEGG:MAP00641

Retinol metabolism
type: KeggPathway
references: KEGG:MAP00830

Metabolism of xenobiotics by cytochrome P450
type: KeggPathway
references: KEGG:MAP00980

Drug metabolism - cytochrome P450
type: KeggPathway
references: KEGG:MAP00982

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

Alcohol
type: KeggSubstrate
references: KEGG:C00069
compound type: carbohydrate

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

Aldehyde
type: KeggProduct
references: KEGG:C00071
compound type: carbohydrate

Ketone
type: KeggProduct
references: KEGG:C00709
compound type: carbohydrate

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

1a4uA
type: Pdb
references: 1a4u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4u
catalytic residue: SER 138;TYR 151;LYS 155

1a4uB
type: Pdb
references: 1a4u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4u
catalytic residue: SER 138;TYR 151;LYS 155

1b14A
type: Pdb
references: 1b14
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b14
catalytic residue: SER 138;TYR 151;LYS 155

1b14B
type: Pdb
references: 1b14
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b14
catalytic residue: SER 138;TYR 151;LYS 155

1b15A
type: Pdb
references: 1b15
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b15
catalytic residue: SER 138;TYR 151;LYS 155

1b15B
type: Pdb
references: 1b15
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b15
catalytic residue: SER 138;TYR 151;LYS 155

1b16A
type: Pdb
references: 1b16
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b16
catalytic residue: SER 138;TYR 151;LYS 155

1b16B
type: Pdb
references: 1b16
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b16
catalytic residue: SER 138;TYR 151;LYS 155

1b2lA
type: Pdb
references: 1b2l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b2l
catalytic residue: SER 138;TYR 151;LYS 155

1sbyA
type: Pdb
references: 1sby
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sby
catalytic residue: SER 138;TYR 151;LYS 155

1sbyB
type: Pdb
references: 1sby
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sby
catalytic residue: SER 138;TYR 151;LYS 155

1mg5A
type: Pdb
references: 1mg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg5
catalytic residue: SER 139;TYR 152;LYS 156

1mg5B
type: Pdb
references: 1mg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg5
catalytic residue: SER 139;TYR 152;LYS 156

The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6821373
journal: Biochem J
volume: 187
pages: 875-83
published year: 1980
authors:
  item: Thatcher DR

Secondary-structure prediction from the sequence of Drosophila melanogaster (fruitfly) alcohol dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6821374
journal: Biochem J
volume: 187
pages: 884-6
published year: 1980
authors:
  item: Thatcher DR
  item: Sawyer L

Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6789320
journal: Proc Natl Acad Sci U S A
volume: 78
pages: 2717-21
published year: 1981
authors:
  item: Benyajati C
  item: Place AR
  item: Powers DA
  item: Sofer W

The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3160338
journal: Biochem Genet
volume: 23
pages: 205-16
published year: 1985
authors:
  item: Winberg JO
  item: Hovik R
  item: McKinley-McKee JS

Mechanism of action of Drosophila melanogaster alcohol dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1804107
journal: Biochem Int
volume: 25
pages: 879-85
published year: 1991
authors:
  item: McKinley-McKee JS
  item: Winberg JO
  item: Pettersson G

Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1904719
journal: Biochem J
volume: 276
pages: 433-8
published year: 1991
authors:
  item: Ribas De Pouplana L
  item: Atrian S
  item: Gonzalex-Duarte R
  item: Fothergill-Gilmore LA
  item: Kelly SM
  item: Price NC

Kinetic interpretations of active site topologies and residue exchanges in Drosophila alcohol dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1733784
journal: Int J Biochem
volume: 24
pages: 169-81
published year: 1992
authors:
  item: Winberg JO
  item: McKinley-McKee JS

Preliminary X-ray crystallographic studies on alcohol dehydrogenase from Drosophila.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1522600
journal: J Mol Biol
volume: 227
pages: 356-8
published year: 1992
authors:
  item: Gordon EJ
  item: Bury SM
  item: Sawyer L
  item: Atrian S
  item: Gonzalez-Duarte R

Drosophila transcriptional repressor protein that binds specifically to negative control elements in fat body enhancers.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1508206
journal: Mol Cell Biol
volume: 12
pages: 4093-103
published year: 1992
authors:
  item: Falb D
  item: Maniatis T

Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8461298
journal: Biochemistry
volume: 32
pages: 3342-6
published year: 1993
authors:
  item: Chen Z
  item: Jiang JC
  item: Lin ZG
  item: Lee WR
  item: Baker ME
  item: Chang SH

The active site architecture of a short-chain dehydrogenase defined by site-directed mutagenesis and structure modeling.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8003469
journal: Biochemistry
volume: 33
pages: 7047-55
published year: 1994
authors:
  item: Ribas de Pouplana L
  item: Fothergill-Gilmore LA

Adding a positive charge at residue 46 of Drosophila alcohol dehydrogenase increases cofactor specificity for NADP+.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7988726
journal: FEBS Lett
volume: 356
pages: 81-5
published year: 1994
authors:
  item: Chen Z
  item: Tsigelny I
  item: Lee WR
  item: Baker ME
  item: Chang SH

Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7772022
journal: Biochem J
volume: 308
pages: 419-23
published year: 1995
authors:
  item: Chenevert SW
  item: Fossett NG
  item: Chang SH
  item: Tsigelny I
  item: Baker ME
  item: Lee WR

Involvement of the C-terminal tail in the activity of Drosophila alcohol dehydrogenase. Evaluation of truncated proteins constructed by site-directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7588794
journal: Eur J Biochem
volume: 233
pages: 498-505
published year: 1995
authors:
  item: Albalat R
  item: Valls M
  item: Fibla J
  item: Atrian S
  item: Gonzalez-Duarte R

Structures important in mammalian 11 beta- and 17 beta-hydroxysteroid dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8547186
journal: J Steroid Biochem Mol Biol
volume: 55
pages: 589-600
published year: 1995
authors:
  item: Tsigelny I
  item: Baker ME

Drosophila alcohol dehydrogenase: evaluation of Ser139 site-directed mutants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9280279
journal: FEBS Lett
volume: 413
pages: 191-3
published year: 1997
authors:
  item: Cols N
  item: Atrian S
  item: Benach J
  item: Ladenstein R
  item: Gonzalez-Duarte R

Modeling studies of conformational changes in the substrate-binding loop in Drosophila alcohol dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9562905
journal: Biochem Genet
volume: 36
pages: 37-49
published year: 1998
authors:
  item: Smilda T
  item: Reinders P
  item: Beintema JJ

The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
medline id: 98407982
references: http://www.ncbi.nlm.nih.gov/pubmed/9735295
journal: J Mol Biol
volume: 282
pages: 383-99
published year: 1998
authors:
  item: Benach J
  item: Atrian S
  item: Gonzalez-Duarte R
  item: Ladenstein R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P10807

Shaping of Drosophila alcohol dehydrogenase through evolution: relationship with enzyme functionality.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9694670
journal: J Mol Evol
volume: 47
pages: 211-21
published year: 1998
authors:
  item: Atrian S
  item: Sanchez-Pulido L
  item: Gonzalez-Duarte R
  item: Valencia A

The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
medline id: 99296633
references: http://www.ncbi.nlm.nih.gov/pubmed/10366509
journal: J Mol Biol
volume: 289
pages: 335-55
published year: 1999
authors:
  item: Benach J
  item: Atrian S
  item: Gonzalez-Duarte R
  item: Ladenstein R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P10807

The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10610783
journal: J Mol Biol
volume: 294
pages: 601-16
published year: 1999
authors:
  item: Winberg JO
  item: Brendskag MK
  item: Sylte I
  item: Lindstad RI
  item: McKinley-McKee JS

The Drosophila virilis alcohol dehydrogenase catalytic residues are conserved.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10093214
journal: J Mol Evol
volume: 48
pages: 262-3
published year: 1999
authors:
  item: Atrian S
  item: Gonzalez-Duarte R

Structure-function relationships in Drosophila melanogaster alcohol dehydrogenase allozymes ADH(S), ADH(F) and ADH(UF), and distantly related forms.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10848978
journal: Eur J Biochem
volume: 267
pages: 3613-22
published year: 2000
authors:
  item: Benach J
  item: Atrian S
  item: Fibla J
  item: Gonzalez-Duarte R
  item: Ladenstein R

Enzymic and structural studies on Drosophila alcohol dehydrogenase and other short-chain dehydrogenases/reductases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11443349
journal: J Mol Evol
volume: 52
pages: 457-66
published year: 2001
authors:
  item: Smilda T
  item: Kamminga AH
  item: Reinders P
  item: Baron W
  item: van Hylckama Vlieg JE
  item: Beintema JJ

The catalytic mechanism of Drosophila alcohol dehydrogenase: evidence for a proton relay modulated by the coupled ionization of the active site Lysine/Tyrosine pair and a NAD+ ribose OH switch.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12660997
journal: Proteins
volume: 51
pages: 289-98
published year: 2003
authors:
  item: Koumanov A
  item: Benach J
  item: Atrian S
  item: Gonzalez-Duarte R
  item: Karshikoff A
  item: Ladenstein R

Functional constraints of alcohol dehydrogenase (ADH) of tephritidae and relationships with other Dipteran species.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15170253
journal: J Mol Evol
volume: 58
pages: 493-505
published year: 2004
authors:
  item: Eliopoulos E
  item: Goulielmos GN
  item: Loukas M

Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15581900
journal: J Mol Biol
volume: 345
pages: 579-98
published year: 2005
authors:
  item: Benach J
  item: Winberg JO
  item: Svendsen JS
  item: Atrian S
  item: Gonzalez-Duarte R
  item: Ladenstein R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Medium- and short-chain dehydrogenase/reductase gene and protein families : Structure-function relationships in short-chain alcohol dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19011748
journal: Cell Mol Life Sci
volume: 65
pages: 3918-35
published year: 2008
authors:
  item: Ladenstein R
  item: Winberg JO
  item: Benach J

Analogue
compound: NAD+
pdb: 1b15A
ligand het code: NAE (NAD-Ketone)

Analogue
compound: NAD+
pdb: 1b15B
ligand het code: NAE (NAD-Ketone)

Analogue
compound: NAD+
pdb: 1b16A
ligand het code: NAQ (NAD-Ketone)

Analogue
compound: NAD+
pdb: 1b16B
ligand het code: NAQ (NAD-Ketone)

Analogue
compound: NAD+
pdb: 1b2lA
ligand het code: NDC (NAD-Ketone)

Analogue
compound: Alcohol
pdb: 1sbyA
ligand het code: ETF

Analogue
compound: Alcohol
pdb: 1sbyB
ligand het code: ETF

Analogue
compound: Ketone
pdb: 1b15A
ligand het code: NAE (NAD-Ketone)

Analogue
compound: Ketone
pdb: 1b15B
ligand het code: NAE (NAD-Ketone)

Analogue
compound: Ketone
pdb: 1b16A
ligand het code: NAQ (NAD-Ketone)

Analogue
compound: Ketone
pdb: 1b16B
ligand het code: NAQ (NAD-Ketone)

Analogue
compound: Ketone
pdb: 1b2lA
ligand het code: NDC (NAD-Ketone)

Analogue
compound: Ketone
pdb: 1mg5A
ligand het code: ACT

Analogue
compound: Ketone
pdb: 1mg5B
ligand het code: ACT

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.5, p.3345-3346
reference step: 2

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.7054

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.84

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.193

ReferenceForCatalyticMechanism
reference index: 18
reference section: p.389-391

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.10, p.346-348

ReferenceForCatalyticMechanism
reference index: 21
reference section: Fig.5, p.608-611

ReferenceForCatalyticMechanism
reference index: 25
reference section: p.296-298

ReferenceForCatalyticMechanism
reference index: 28
reference section: Fig.7, p.3927-3930