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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH) and Organism(s) Brassica napus and UniProt Accession P80030

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IUBMB Comments
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 . The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
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Brassica napus
UNIPROT: P80030
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The taxonomic range for the selected organisms is: Brassica napus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pfenr, enoyl-acyl carrier protein, enoyl acyl carrier protein reductase, mtinha, enoyl acp reductase, nadh-dependent enoyl-acp reductase, enoyl-reductase, fabi2, fabi1, nadh-dependent enoyl-acyl carrier protein reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cold-shock induced protein 15
-
-
-
-
CSI15
-
-
-
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enoyl-ACP reductase
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-
-
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NADH-dependent enoyl-ACP reductase
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-
-
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NADH-enoyl acyl carrier protein reductase
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-
-
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NADH-specific enoyl-ACP reductase
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-
-
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reductase, enoyl-[acyl carrier protein]
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-
-
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VEG241
-
-
-
-
vegetative protein 241
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NAD+ oxidoreductase
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
CAS REGISTRY NUMBER
COMMENTARY hide
37251-08-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + NADH
butyryl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
crotonyl-[acyl-carrier protein] + NADH
butyryl-[acyl-carrier protein] + NAD+
show the reaction diagram
-
-
-
-
?
enoyl esters of acyl-carrier protein + NADH
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
enoyl esters of acyl-carrier protein + NADH
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
absolute specificity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol
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CoASH
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competitive inhibitor with crotonyl CoA as substrate
iodoacetamide
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no inhibition at 10 mM
N-ethylmaleimide
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no inhibition at 1 mM, 97% inhibition at 10 mM, inhibition can be partially reversed by dithiothreitol
p-chloromercuribenzoate
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complete inhibition at 0.1 mM, inhibition can be prevented by preincubation with crotonyl-CoA
Phenylglyoxal
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98% inhibition at 4.8 mM within 30 min, reversible inhibition by binding at the active site, inhibition is prevented by CoA, ADP, AMP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.178
crotonyl-CoA
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-
0.001
crotonyl-[acyl-carrier protein]
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Km is 0.001mM or less
0.0076
NADH
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
CoASH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
in 3-(N-morpholino)propane sulfonate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mutant A138G
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
thylakoid membrane
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FABI_BRANA
385
0
40479
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
33600
34000
-
monomeric form, SDS-PAGE
348000
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2 * 348000 + 2 * 33600
35000
-
monomeric form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
two polypeptides which differ in molecular mass by about 1000 Da
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with NAD+ or crotonyl-CoA, hanging drop vapor diffusion method
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complexed with NAD+, NADH or thienodiazaborine, hanging drop vapor diffusion method
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, at least 3 months, survives only 1 freeze thaw cycle
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homogeneity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fisher, M.; Kroon, J.T.M.; Martindale, W.; Stuitje, A.R.; Slabas, A.R.; Rafferty, J.B.
The x-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis
Structure
8
339-347
2000
Brassica napus
Manually annotated by BRENDA team
Slabas, A.R.; Cottingham, I.R.; Austin, A.; Hellyer, A.; Safford, R.; Smith, C.G.
Immunological detection of NADH-specific enoyl-ACP reductase from rape seed (Brassica napus)-induction, relationship of alpha and beta polypeptides, mRNA translation and interaction with ACP
Biochim. Biophys. Acta
1039
181-188
1990
Brassica napus
Manually annotated by BRENDA team
Cottingham, I.R.; Austin, A.J.; Slabas, A.R.
Inhibition and covalent modification of rape seed (Brassica napus) enoyl ACP reductase by phenylglyoxal
Biochim. Biophys. Acta
995
273-278
1989
Brassica napus
Manually annotated by BRENDA team
Cottingham, I.R.; Austin, A.; Sidebottom, C.; Slabas, A.R.
Purified enoyl-[acyl-carrier-protein] reductase frome rape seed (Brassica napus) contains two closely related polypeptides which differ by a six-amino-acid N-terminal extension
Biochim. Biophys. Acta
854
201-207
1988
Brassica napus
-
Manually annotated by BRENDA team
Slabas, A.R.; Sidebottom, C.M.; Hellyer, A.; Kessell, R.M.J.; Tombs, M.P.
Induction, purification and characterization of NADH-specific enoyl acyl carrier protein reductase from developing seeds of oil seed rape (Brassica napus)
Biochim. Biophys. Acta
877
271-280
1986
Brassica napus
-
Manually annotated by BRENDA team
Slabas, A.R.; Sidebottom, C.M.; Kessell, R.M.J; Hellyer, A.; Tombs, M.P.
Oilseed rape NADH enoyl acyl-carrier protein reductase
Biochem. Soc. Trans.
14
581-582
1986
Brassica napus
Manually annotated by BRENDA team
Rafferty, J.B.; Simon, J.W.; Stuitje, A.R.; Slabas, A.R.; Fawcett, T.; Rice, D.W.
Crystallization of the NADH-specific enoyl acyl carrier protein reductase from Brassica napus
J. Mol. Biol.
237
240-242
1994
Brassica napus
Manually annotated by BRENDA team
Roujeinikova, A.; Sedelnikova, S.; De Boer, G.J.; Stuitje, A.R.; Slabas, A.R.; Rafferty, J.B.; Rice, D.W.
Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition
J. Biol. Chem.
274
30811-30817
1999
Brassica napus (P80030), Brassica napus
Manually annotated by BRENDA team