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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH) and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC1.3.1.9

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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.

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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
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CSI15
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enoyl-ACP reductase
enoyl-acyl carrier protein reductase
NADH-dependent enoyl-ACP reductase
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NADH-enoyl acyl carrier protein reductase
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NADH-specific enoyl-ACP reductase
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reductase, enoyl-[acyl carrier protein]
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VEG241
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vegetative protein 241
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
(5Z)-dodecenoate biosynthesis I, (5Z)-dodecenoate biosynthesis II, 8-amino-7-oxononanoate biosynthesis I, 8-amino-7-oxononanoate biosynthesis IV, anteiso-branched-chain fatty acid biosynthesis, cis-vaccenate biosynthesis, even iso-branched-chain fatty acid biosynthesis, fatty acid elongation -- saturated, gondoate biosynthesis (anaerobic), mycolate biosynthesis, odd iso-branched-chain fatty acid biosynthesis, oleate biosynthesis IV (anaerobic), palmitate biosynthesis II (type II fatty acid synthase), palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate), stearate biosynthesis II (bacteria and plants), streptorubin B biosynthesis
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
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + NAD+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
show the reaction diagram
Substrates: -
Products: -
?
crotonyl-CoA + NADH
butyryl-CoA + NAD+
show the reaction diagram
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Substrates: -
Products: -
?
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
show the reaction diagram
Substrates: -
Products: -
?
crotonyl-[acyl-carrier protein] + NADH
butyryl-[acyl-carrier protein] + NAD+
show the reaction diagram
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Substrates: activity is 5.9fold higher than with crotonyl-CoA
Products: -
?
crotonyl-[acyl-carrier protein] + NADH + H+
butyryl-[acyl-carrier protein] + NAD+
show the reaction diagram
Substrates: -
Products: -
?
trans-2-decenoyl-[acyl-carrier protein] + NADH + H+
?
show the reaction diagram
-
Substrates: -
Products: -
?
trans-2-decenoyl-[acyl-carrier protein] + NADH + H+
decanoyl-[acyl-carrier protein] + NAD+
show the reaction diagram
Substrates: -
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + NAD+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
show the reaction diagram
Substrates: -
Products: -
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activity with NADPH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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not inhibited by triclosan
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.691
crotonyl-[acyl-carrier protein]
pH 7.0, temperature not specified in the publication
0.704
trans-2-decenoyl-[acyl-carrier protein]
pH 7.0, temperature not specified in the publication
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isoform FabV confers triclosan resistance on Pseudomonas aeruginosa. Upon deletion of the fabV gene, the mutant strain becomes more than 2000fold more sensitive to triclosan than the wild-type strain. Enzyme functionally replaces Escherichia coli fabI in vivo and renders Escherichia coli resistant to triclosan
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A069QB06_PSEAI
398
0
43528
TrEMBL
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A0A069PZV2_PSEAI
265
0
28006
TrEMBL
-
A0A5E5QU99_PSEAI
265
0
27976
TrEMBL
-
A0A6A9JLU9_PSEAI
398
0
43556
TrEMBL
-
A0A6B1YCZ9_PSEAI
265
0
28036
TrEMBL
-
A0A6B1YLG3_PSEAI
259
0
27659
TrEMBL
Mitochondrion (Reliability: 5)
A0AAQ3LK21_PSEAI
259
0
27706
TrEMBL
-
A0AAQ3R5B0_PSEAI
398
0
43544
TrEMBL
-
A0ABD7JZ54_PSEAI
265
0
27888
TrEMBL
-
A0ABD7K4D7_PSEAI
398
0
43571
TrEMBL
other Location (Reliability: 2)
Q1AHB5_PSEAI
398
0
43514
TrEMBL
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with NAD+ and triclosan, hanging drop vapor diffusion method, using 0.1 M sodium malonate pH 5.0, 10% (w/v) polyethylene glycol 3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G95V
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mutant enzyme retains normal activity with enoyl-[acyl-carrier-protein], but is highly resistant to triclosan
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
polyhistidine-tagged recombinant wild-type protein and mutant enzyme G95V
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoang, T.T.; Schweizer, H.P.
Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis
J. Bacteriol.
181
5489-5497
1999
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Zhu, L.; Lin, J.; Ma, J.; Cronan, J.; Wang, H.
Triclosan resistance of Pseudomonas aeruginosa PAO1 is due to FabV, a triclosan-resistant enoyl-acyl carrier protein reductase
Antimicrob. Agents Chemother.
54
689-698
2010
Pseudomonas aeruginosa (Q9HZP8), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Lee, J.; Park, A.; Chi, Y.; Jeong, A.
Crystal structures of Pseudomonas aeruginosa enoyl-ACP reductase (FabI) in the presence and absence of NAD+ and triclosan
Bull. Korean Chem. Soc.
36
322-326
2015
Pseudomonas aeruginosa (Q9ZFE4)
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Manually annotated by BRENDA team
Huang, Y.H.; Lin, J.S.; Ma, J.C.; Wang, H.H.
Functional characterization of triclosan-resistant enoyl-acyl-carrier protein reductase (FabV) in Pseudomonas aeruginosa
Front. Microbiol.
7
1903
2016
Pseudomonas aeruginosa
Manually annotated by BRENDA team