S00334
type: Enzyme
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.3.1.9
csa: 1mfp
csa: 1qsg
uniprot: P80030
uniprot: P0AEK4
uniprot: P0A5Y7
uniprot: P0A5Y6
kegg enzyme: enoyl-[acyl-carrier-protein] reductase (NADH)
kegg pathway: Fatty acid biosynthesis
kegg substrate: Acyl-[acyl-carrier protein]
kegg substrate: NAD+
kegg product: trans-2,3-Dehydroacyl-[acyl-carrier protein]
kegg product: NADH
kegg product: H+
pdb: 1bvrA
pdb: 1bvrB
pdb: 1bvrC
pdb: 1bvrD
pdb: 1bvrE
pdb: 1bvrF
pdb: 1c14A
pdb: 1c14B
pdb: 1cwuA
pdb: 1cwuB
pdb: 1d7oA
pdb: 1d8aA
pdb: 1d8aB
pdb: 1dfgA
pdb: 1dfgB
pdb: 1dfhA
pdb: 1dfhB
pdb: 1dfiA
pdb: 1dfiB
pdb: 1dfiC
pdb: 1dfiD
pdb: 1enoA
pdb: 1enpA
pdb: 1enyA
pdb: 1enzA
pdb: 1i2zA
pdb: 1i2zB
pdb: 1i30A
pdb: 1i30B
pdb: 1lx6A
pdb: 1lx6B
pdb: 1lxcA
pdb: 1lxcB
pdb: 1mfpA
pdb: 1mfpB
pdb: 1p44A
pdb: 1p44B
pdb: 1p44C
pdb: 1p44D
pdb: 1p44E
pdb: 1p44F
pdb: 1p45A
pdb: 1p45B
pdb: 1qg6A
pdb: 1qg6B
pdb: 1qg6C
pdb: 1qg6D
pdb: 1qsgA
pdb: 1qsgB
pdb: 1qsgC
pdb: 1qsgD
pdb: 1qsgE
pdb: 1qsgF
pdb: 1qsgG
pdb: 1qsgH
pdb: 1zidA
active site residues resources: Evidence for the essential histidine at the NADPH binding site of enoyl-CoA reductase domain of pigeon liver fatty acid synthetase.
active site residues resources: Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
active site residues resources: Mechanism of triclosan inhibition of bacterial fatty acid synthesis.
references: Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.
references: Crystallization of the NADH-specific enoyl acyl carrier protein reductase from Brassica napus.
references: Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli.
references: Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.
references: Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase.

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

Fatty acid biosynthesis
type: KeggPathway
references: KEGG:MAP00061

Acyl-[acyl-carrier protein]
type: KeggSubstrate
references: KEGG:C00173
compound type: carbohydrate
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group

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

trans-2,3-Dehydroacyl-[acyl-carrier protein]
type: KeggProduct
references: KEGG:C00693
compound type: carbohydrate
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group

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

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

1bvrA
type: Pdb
references: 1bvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvr
catalytic residue: TYR 158

1bvrB
type: Pdb
references: 1bvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvr
catalytic residue: TYR 158

1bvrC
type: Pdb
references: 1bvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvr
catalytic residue: TYR 158

1bvrD
type: Pdb
references: 1bvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvr
catalytic residue: TYR 158

1bvrE
type: Pdb
references: 1bvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvr
catalytic residue: TYR 158

1bvrF
type: Pdb
references: 1bvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvr
catalytic residue: TYR 158

1c14A
type: Pdb
references: 1c14
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c14
catalytic residue: TYR 156

1c14B
type: Pdb
references: 1c14
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c14
catalytic residue: TYR 1156

1cwuA
type: Pdb
references: 1cwu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cwu
catalytic residue: TYR 198
comment: mutant A138G

1cwuB
type: Pdb
references: 1cwu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cwu
catalytic residue: TYR 198
comment: mutant A138G

1d7oA
type: Pdb
references: 1d7o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7o
catalytic residue: TYR 198

1d8aA
type: Pdb
references: 1d8a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d8a
catalytic residue: TYR 156

1d8aB
type: Pdb
references: 1d8a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d8a
catalytic residue: TYR 156

1dfgA
type: Pdb
references: 1dfg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfg
catalytic residue: TYR 156

1dfgB
type: Pdb
references: 1dfg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfg
catalytic residue: TYR 156

1dfhA
type: Pdb
references: 1dfh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfh
catalytic residue: TYR 156

1dfhB
type: Pdb
references: 1dfh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfh
catalytic residue: TYR 156

1dfiA
type: Pdb
references: 1dfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfi
catalytic residue: TYR 156

1dfiB
type: Pdb
references: 1dfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfi
catalytic residue: TYR 156

1dfiC
type: Pdb
references: 1dfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfi
catalytic residue: TYR 156

1dfiD
type: Pdb
references: 1dfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dfi
catalytic residue: TYR 156

1enoA
type: Pdb
references: 1eno
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eno
catalytic residue: TYR 198
comment: mutant S1A

1enpA
type: Pdb
references: 1enp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1enp
catalytic residue: TYR 198
comment: mutant S1A

1enyA
type: Pdb
references: 1eny
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eny
catalytic residue: TYR 158

1enzA
type: Pdb
references: 1enz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1enz
catalytic residue: TYR 158
comment: mutant S94A

1i2zA
type: Pdb
references: 1i2z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i2z
catalytic residue: TYR 156

1i2zB
type: Pdb
references: 1i2z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i2z
catalytic residue: TYR 1156

1i30A
type: Pdb
references: 1i30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i30
catalytic residue: TYR 156

1i30B
type: Pdb
references: 1i30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i30
catalytic residue: TYR 1156

1lx6A
type: Pdb
references: 1lx6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lx6
catalytic residue: TYR 156

1lx6B
type: Pdb
references: 1lx6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lx6
catalytic residue: TYR 156

1lxcA
type: Pdb
references: 1lxc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxc
catalytic residue: TYR 156

1lxcB
type: Pdb
references: 1lxc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxc
catalytic residue: TYR 156

1mfpA
type: Pdb
references: 1mfp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mfp
catalytic residue: TYR 156

1mfpB
type: Pdb
references: 1mfp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mfp
catalytic residue: TYR 1156

1p44A
type: Pdb
references: 1p44
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p44
catalytic residue: TYR 158

1p44B
type: Pdb
references: 1p44
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p44
catalytic residue: TYR 158

1p44C
type: Pdb
references: 1p44
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p44
catalytic residue: TYR 158

1p44D
type: Pdb
references: 1p44
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p44
catalytic residue: TYR 158

1p44E
type: Pdb
references: 1p44
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p44
catalytic residue: TYR 158

1p44F
type: Pdb
references: 1p44
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p44
catalytic residue: TYR 158

1p45A
type: Pdb
references: 1p45
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p45
catalytic residue: TYR 158

1p45B
type: Pdb
references: 1p45
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p45
catalytic residue: TYR 158

1qg6A
type: Pdb
references: 1qg6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qg6
catalytic residue: TYR 156

1qg6B
type: Pdb
references: 1qg6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qg6
catalytic residue: TYR 156

1qg6C
type: Pdb
references: 1qg6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qg6
catalytic residue: TYR 156

1qg6D
type: Pdb
references: 1qg6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qg6
catalytic residue: TYR 156

1qsgA
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgB
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgC
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgD
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgE
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgF
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgG
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1qsgH
type: Pdb
references: 1qsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qsg
catalytic residue: TYR 156

1zidA
type: Pdb
references: 1zid
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zid
catalytic residue: TYR 158
comment: mutant T2A

Evidence for the essential histidine at the NADPH binding site of enoyl-CoA reductase domain of pigeon liver fatty acid synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9204389
journal: J Enzyme Inhib
volume: 11
pages: 209-16
published year: 1997
authors:
  item: Mukherjee S
  item: Katiyar SS

Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10521269
journal: Biochemistry
volume: 38
pages: 13623-34
published year: 1999
authors:
  item: Parikh S
  item: Moynihan DP
  item: Xiao G
  item: Tonge PJ

Mechanism of triclosan inhibition of bacterial fatty acid synthesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10196195
journal: J Biol Chem
volume: 274
pages: 11110-4
published year: 1999
authors:
  item: Heath RJ
  item: Rubin JR
  item: Holland DR
  item: Zhang E
  item: Snow ME
  item: Rock CO

Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3535882
journal: Biochemistry
volume: 25
pages: 5617-24
published year: 1986
authors:
  item: Leanz GF
  item: Hammes GG

Crystallization of the NADH-specific enoyl acyl carrier protein reductase from Brassica napus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8126737
journal: J Mol Biol
volume: 237
pages: 240-2
published year: 1994
authors:
  item: Rafferty JB
  item: Simon JW
  item: Stuitje AR
  item: Slabas AR
  item: Fawcett T
  item: Rice DW

Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7932735
journal: J Mol Biol
volume: 243
pages: 126-7
published year: 1994
authors:
  item: Wagner UG
  item: Bergler H
  item: Fuchsbichler S
  item: Turnowsky F
  item: Hogenauer G
  item: Kratky C

Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7886450
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Science
volume: 267
pages: 1638-41
published year: 1995
authors:
  item: Dessen A
  item: Quemard A
  item: Blanchard JS
  item: Jacobs WR Jr
  item: Sacchettini JC

Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-382.
medline id: 96097399
references: http://www.ncbi.nlm.nih.gov/pubmed/8535786
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P80030
journal: Structure
volume: 3
pages: 927-38
published year: 1995
authors:
  item: Rafferty JB
  item: Simon JW
  item: Baldock C
  item: Artymiuk PJ
  item: Baker PJ
  item: Stuitje AR
  item: Slabas AR
  item: Rice DW

A mechanism of drug action revealed by structural studies of enoyl reductase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 97113207
references: http://www.ncbi.nlm.nih.gov/pubmed/8953047
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AEK4
journal: Science
volume: 274
pages: 2107-10
published year: 1996
authors:
  item: Baldock C
  item: Rafferty JB
  item: Sedelnikova SE
  item: Baker PJ
  item: Stuitje AR
  item: Slabas AR
  item: Hawkes TR
  item: Rice DW

The X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9878369
journal: J Mol Biol
volume: 284
pages: 1529-46
published year: 1998
authors:
  item: Baldock C
  item: Rafferty JB
  item: Stuitje AR
  item: Slabas AR
  item: Rice DW

Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
medline id: 98079172
references: http://www.ncbi.nlm.nih.gov/pubmed/9417034
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P46533
journal: Science
volume: 279
pages: 98-102
published year: 1998
authors:
  item: Rozwarski DA
  item: Grant GA
  item: Barton DH
  item: Jacobs WR Jr
  item: Sacchettini JC

Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
medline id: 99425142
references: http://www.ncbi.nlm.nih.gov/pubmed/10493822
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AEK4
journal: Biochemistry
volume: 38
pages: 12514-25
published year: 1999
authors:
  item: Ward WH
  item: Holdgate GA
  item: Rowsell S
  item: McLean EG
  item: Pauptit RA
  item: Clayton E
  item: Nichols WW
  item: Colls JG
  item: Minshull CA
  item: Jude DA
  item: Mistry A
  item: Timms D
  item: Camble R
  item: Hales NJ
  item: Britton CJ
  item: Taylor IW

Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10521472
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Chem
volume: 274
pages: 30811-7
published year: 1999
authors:
  item: Roujeinikova A
  item: Sedelnikova S
  item: de Boer GJ
  item: Stuitje AR
  item: Slabas AR
  item: Rafferty JB
  item: Rice DW

Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
medline id: 99269096
references: http://www.ncbi.nlm.nih.gov/pubmed/10336454
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P46533
journal: J Biol Chem
volume: 274
pages: 15582-9
published year: 1999
authors:
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Molecular basis for triclosan activity involves a flipping loop in the active site.
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1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI).
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A study of the structure-activity relationship for diazaborine inhibition of Escherichia coli enoyl-ACP reductase.
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Can an optimization/scoring procedure in ligand-protein docking be employed to probe drug-resistant mutations in proteins?
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Characterization of a novel enoyl-acyl carrier protein reductase of diazaborine-resistant Rhodobacter sphaeroides mutant.
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Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase.
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Targeting tuberculosis and malaria through inhibition of Enoyl reductase: compound activity and structural data.
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Exploring the interaction energies for the binding of hydroxydiphenyl ethers to enoyl-acyl carrier protein reductases.
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Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK.
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enoyl-[acyl carrier protein] reductase
type: KeggEnzyme

enoyl-ACP reductase
type: KeggEnzyme

NADH-enoyl acyl carrier protein reductase
type: KeggEnzyme

NADH-specific enoyl-ACP reductase
type: KeggEnzyme

enoyl-[acyl-carrier-protein] reductase (NADH)
type: KeggEnzyme

acyl-[acyl-carrier-protein]:NAD+ oxidoreductase
type: KeggEnzyme

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1bvrA
ligand het code: THT

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1bvrB
ligand het code: THT

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1bvrC
ligand het code: THT

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1bvrF
ligand het code: THT

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1lx6A
ligand het code: ZAM

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1lx6B
ligand het code: ZAM

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1lxcA
ligand het code: AYM

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1lxcB
ligand het code: AYM

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1mfpA
ligand het code: IDN

Analogue
compound: Acyl-[acyl-carrier protein]
pdb: 1mfpB
ligand het code: IDN

Analogue
compound: NAD+
pdb: 1cwuA
ligand het code: NAD-TDB

Analogue
compound: NAD+
pdb: 1cwuB
ligand het code: NAD-TDB

Analogue
compound: NAD+
pdb: 1dfgA
ligand het code: NAD-NDT

Analogue
compound: NAD+
pdb: 1dfgB
ligand het code: NAD-NDT

Analogue
compound: NAD+
pdb: 1dfhA
ligand het code: NAD-TDB

Analogue
compound: NAD+
pdb: 1dfhB
ligand het code: NAD-TDB

Analogue
compound: NAD+
pdb: 1zidA
ligand het code: ZID

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.8, p.932-933

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.8, p.1539-1541

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.13628-13629

ReferenceForCatalyticMechanism
reference index: 11

ReferenceForCatalyticMechanism
reference index: 13
reference section: p.30817

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.15587-15588

ReferenceForCatalyticMechanism
reference index: 16