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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH) and Organism(s) Burkholderia mallei and UniProt Accession Q62L02

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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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Burkholderia mallei
UNIPROT: Q62L02
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The taxonomic range for the selected organisms is: Burkholderia mallei
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
enoyl-ACP reductase
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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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additional information
the enzyme is a member of the short chain dehydrogenase/reductase superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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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
(2E)-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
show the reaction diagram
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?
crotonyl-[acyl-carrier protein] + NAD+
? + NADH + H+
show the reaction diagram
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?
crotonyl-[acyl-carrier protein] + NADH
butyryl-[acyl-carrier protein] + NAD+
show the reaction diagram
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?
additional information
?
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activity measurement using NAD+ cofactor and substrate 2-dodecenoyl-CoA
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
triclosan
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
optimal oionic strength 0.62 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022 - 0.028
(2E)-2-dodecenoyl-CoA
0.025
crotonyl-[acyl-carrier protein]
pH 7.9, 25°C
0.006 - 0.069
NADH
additional information
additional information
Km for NADH of 0.023 mM, a Km for 2-dodecenoyl-CoA of 0.0025 mM, and a kcat of 20.7 s-1. Steady-state kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 28.8
(2E)-2-dodecenoyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 6.5
(2E)-2-dodecenoyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
triclosan
additional information
additional information
inhibition kinetics, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
enoyl-ACP reductases catalyze the final step in the elongation cycle of the bacterial fatty acid biosynthesis, FAS-II, pathway, but FabV is distinct and belongs to another class of enoyl-acyl carrier protein reductases, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K244A
K244A/K245A
K244R
K245M
Y235A
Y235S
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fabV, expression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3), theN-terminal His-tag in bmFabv does not have a dramatic effect on catalytic activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lu, H.; Tonge, P.J.
Mechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia mallei
Biochemistry
49
1281-1289
2010
Burkholderia mallei (Q62L02), Burkholderia mallei ATCC 23344 (Q62L02)
Manually annotated by BRENDA team