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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH) and Organism(s) Burkholderia pseudomallei and UniProt Accession Q3JQY0

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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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This record set is specific for:
Burkholderia pseudomallei
UNIPROT: Q3JQY0
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Word Map
The taxonomic range for the selected organisms is: Burkholderia pseudomallei
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
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CSI15
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enoyl-ACP reductase
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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
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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 + H+
butyryl-CoA + NAD+
show the reaction diagram
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-
?
crotonyl-[acyl-carrier-protein] + NADH + H+
butyryl-[acyl-carrier-protein] + NAD+
show the reaction diagram
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?
trans-2-decenoyl-CoA + NADH + H+
decanoyl-CoA + NAD+
show the reaction diagram
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?
trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
show the reaction diagram
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?
trans-2-octenoyl-CoA + NADH + H+
octanoyl-CoA + NAD+
show the reaction diagram
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?
additional information
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catalyzes the NADH-dependent reduction of 2-trans-dodecenoyl-CoA via a sequential Bi Bi mechanism
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-phenoxy-5-propylphenol
minimal inhibitory concentration for Burkholderia pseudomallei growth above 250 mg/l
5-ethyl-2-phenoxyphenol
minimal inhibitory concentration for Burkholderia pseudomallei growth 70 mg/l
5-pentyl-2-phenoxyphenol
minimal inhibitory concentration for Burkholderia pseudomallei growth above 250 mg/l
triclosan
minimal inhibitory concentration for Burkholderia pseudomallei growth 30 mg/l
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.188
crotonyl-CoA
pH 6.8, 25°C
0.027
crotonyl-[acyl-carrier-protein]
pH 6.8, 25°C
0.0056
trans-2-decenoyl-CoA
pH 6.8, 25°C
0.0017
trans-2-dodecenoyl-CoA
pH 6.8, 25°C
0.16
trans-2-octenoyl-CoA
pH 6.8, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6
crotonyl-CoA
pH 6.8, 25°C
4
crotonyl-[acyl-carrier-protein]
pH 6.8, 25°C
5.6
trans-2-decenoyl-CoA
pH 6.8, 25°C
8.4
trans-2-dodecenoyl-CoA
pH 6.8, 25°C
28.3
trans-2-octenoyl-CoA
pH 6.8, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
crotonyl-CoA
pH 6.8, 25°C
150
crotonyl-[acyl-carrier-protein]
pH 6.8, 25°C
1000
trans-2-decenoyl-CoA
pH 6.8, 25°C
5000
trans-2-dodecenoyl-CoA
pH 6.8, 25°C
183
trans-2-octenoyl-CoA
pH 6.8, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000013
2-phenoxy-5-propylphenol
Burkholderia pseudomallei
pH 6.8, 25°C
0.00000051
5-ethyl-2-phenoxyphenol
Burkholderia pseudomallei
pH 6.8, 25°C
0.0000018
5-pentyl-2-phenoxyphenol
Burkholderia pseudomallei
pH 6.8, 25°C
0.00000157
triclosan
Burkholderia pseudomallei
pH 6.8, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, N.; Cummings, J.E.; England, K.; Slayden, R.A.; Tonge, P.J.
Mechanism and inhibition of the FabI enoyl-ACP reductase from Burkholderia pseudomallei
J. Antimicrob. Chemother.
66
564-573
2011
Burkholderia pseudomallei (Q3JQY0), Burkholderia pseudomallei 1710b (Q3JQY0)
Manually annotated by BRENDA team