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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH) and Organism(s) Bacillus subtilis and UniProt Accession P54616

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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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Bacillus subtilis
UNIPROT: P54616
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The taxonomic range for the selected organisms is: Bacillus subtilis
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, fabi1, fabi2, nadh-dependent enoyl-acyl carrier protein reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enoyl-ACP reductase
-
enoyl-ACP reductase I
-
enoyl-[acyl-carrier-protein] reductase
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cold-shock induced protein 15
-
-
-
-
CSI15
-
-
-
-
enoyl-ACP reductase
-
-
-
-
enoyl-ACP reductase III
-
-
NADH-dependent enoyl-ACP reductase
-
-
-
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NADH-enoyl acyl carrier protein reductase
-
-
-
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NADH-ENR
-
-
NADH-specific enoyl-ACP reductase
-
-
-
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reductase, enoyl-[acyl carrier protein]
-
-
-
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trans-enoyl-[acyl-carrier-protein] reductase
-
-
VEG241
-
-
-
-
vegetative protein 241
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-but-2-enoyl-[acyl carrier protein] + NADH + H+
butanoyl-[acyl-carrier protein] + NAD+
show the reaction diagram
-
-
-
?
crotonoyl-CoA + NADH + H+
butyryl-CoA + NAD+
show the reaction diagram
-
-
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADH + H+
S-octanoyl-N-acetylcysteamine + NAD+
show the reaction diagram
-
-
-
?
acyl-[acyl-carrier protein] + NAD+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
inactive with NADPH
NAD+
-
dependent
NADH
FabI protein
NADPH
YgaA protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetra hydro-1,8-naphthyridin-3-yl)acrylamide
-
triclosan
a slow-binding inhibitor of bsFabI and formed a stable bsFabI-NAD+-triclosan ternary complex
[5-chloro-2-(2,4-dichlorophenoxy)phenol]
50% inhibition at 0.016 mM, builds a stable complex with FabI and NAD+, but inhibition of YgaA is reversible
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
triclosan
Bacillus subtilis
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.14
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate
2.3
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate
0.14
FabI protein
0.18
YgaA protein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function of the enzyme is examined by knocking out the gene and determining the effect of the gene disruptions on cell growth and triclosan sensitivity, the gene is not essential
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibiotrs triclosan and (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetra hydro-1,8-naphthyridin-3-yl)acrylamide, to 2.7 A and 1.3 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ chelation chromatography
two enzymes: FabI and YgaA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis
J. Biol. Chem.
275
40128-40133
2000
Bacillus subtilis, Bacillus subtilis (P54616)
Manually annotated by BRENDA team
Kim, K.H.; Park, J.K.; Ha, B.H.; Moon, J.H.; Kim, E.E.
Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis
Acta Crystallogr. Sect. F
63
246-248
2007
Bacillus subtilis, Bacillus subtilis 168
Manually annotated by BRENDA team
Kim, K.H.; Ha, B.H.; Kim, S.J.; Hong, S.K.; Hwang, K.Y.; Kim, E.E.
Crystal structures of enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
J. Mol. Biol.
406
403-415
2011
Bacillus subtilis (P54616), Bacillus subtilis, Bacillus subtilis 168 (P54616)
Manually annotated by BRENDA team