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Information on EC 1.3.1.44 - trans-2-enoyl-CoA reductase (NAD+) and Organism(s) Treponema denticola and UniProt Accession Q73Q47

for references in articles please use BRENDA:EC1.3.1.44
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EC Tree
IUBMB Comments
The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
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This record set is specific for:
Treponema denticola
UNIPROT: Q73Q47
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The taxonomic range for the selected organisms is: Treponema denticola
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trans-enoyl-coa reductase, tdter, trans-2-enoyl-coa reductases, trans-2-enoyl-acp reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trans-2-enoyl-CoA reductase
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trans-enoyl-CoA reductase
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trans-2-enoyl-CoA reductase, NADH-dependent
-
-
trans-2-enoyl-CoA reductases
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
-
-
-
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dehydrogenation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:NAD+ trans-2-oxidoreductase
The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
77649-64-0
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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
(E)-2-hexanoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
show the reaction diagram
-
-
-
ir
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
show the reaction diagram
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
show the reaction diagram
NADPH is a poor cosubstrate
-
-
?
trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
show the reaction diagram
-
-
-
?
trans-2-hexenoyl-CoA + NADH + H+
hexanoyl-CoA + NAD+
show the reaction diagram
-
-
-
?
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
show the reaction diagram
high activity toward crotonyl-CoA
-
-
?
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
hexenoyl-CoA + NADH
? + NAD+
show the reaction diagram
weak activity toward crotonyl-CoA
-
-
?
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
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
show the reaction diagram
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADH is preferred over NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
crotonoyl-CoA
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-
additional information
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shows no inhibition by triclosan in a wide range of concentration (0.005-1 mM), or FAD (0.01 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
2-dodecenoyl-CoA
pH and temperature not specified in the publication, mutant I287A
0.049 - 0.21
crotonyl-CoA
0.0034 - 0.038
hexanoyl-CoA
0.0052 - 0.0697
NADH
0.19
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0011 - 0.004
trans-2-dodecenoyl-CoA
0.0034 - 0.038
trans-2-hexenoyl-CoA
0.0027
crotonoyl-CoA
-
in potassium phosphate buffer pH 6.2, at 30°C
0.0697
NADH
pH 6.2, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6 - 90
2-dodecenoyl-CoA
0.73 - 92
crotonyl-CoA
15.3 - 112
hexanoyl-CoA
385.9
NADH
wild type enzyme, at pH 6.2 and 25°C
6 - 90
trans-2-dodecenoyl-CoA
15.3 - 112
trans-2-hexenoyl-CoA
385.9
NADH
pH 6.2, 25°C, wild-type
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2000 - 30000
2-dodecenoyl-CoA
15 - 1300
crotonyl-CoA
1300 - 9000
hexanoyl-CoA
5500 - 16000
NADH
390
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
2000 - 30000
trans-2-dodecenoyl-CoA
1300 - 9000
trans-2-hexenoyl-CoA
5500
NADH
pH 6.2, 25°C, wild-type
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
butyryl-CoA
0.05 - 0.08
hexanoyl-CoA
0.00003 - 0.01
lauroyl-CoA
0.000198
crotonoyl-CoA
-
in potassium phosphate buffer pH 6.2, at 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
-
using crotonoyl-CoA and NADH as substrates, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
SDS-PAGE
44800
calculated from cDNA
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 44800, calculated from amino acid sequence
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of tdTer is determined to 2.00 A
in complex with NAD+, vapor diffusion method,
to 2.0 A resolution
TdTER is crystallized in complex with NAD+ at 3.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F295A
mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
I287A
mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket. Mutant shows a much lower Ki (lauroyl-CoA) than wild-type
L276A/V277A
mutant shows significant decreased kcat values compared to wild-type
L276A/V277A/F295A
mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket
L291A
mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
Y240F
Y240F mutation leads to a 5000fold decrease in catalytic efficiency compared to wild-type with no significant change in Km
Y370A
mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
-
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tucci, S.; Martin, W.
A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola
FEBS Lett.
581
1561-1566
2007
Treponema denticola
Manually annotated by BRENDA team
Hu, K.; Zhao, M.; Zhang, T.; Zha, M.; Zhong, C.; Jiang, Y.; Ding, J.
Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism
Biochem. J.
449
79-89
2013
Clostridium acetobutylicum (Q97LU2), Clostridium acetobutylicum, Treponema denticola, Treponema denticola (Q73Q47), Treponema denticola ATCC 35405
Manually annotated by BRENDA team
Bond-Watts, B.B.; Weeks, A.M.; Chang, M.C.
Biochemical and structural characterization of the trans-enoyl-CoA reductase from Treponema denticola
Biochemistry
51
6827-6837
2012
Treponema denticola (Q73Q47), Treponema denticola, Treponema denticola ATCC 35405 (Q73Q47)
Manually annotated by BRENDA team
Schadeweg, V.; Boles, E.
Increasing n-butanol production with Saccharomyces cerevisiae by optimizing acetyl-CoA synthesis, NADH levels and trans-2-enoyl-CoA reductase expression
Biotechnol. Biofuels
9
257
2016
Treponema denticola, Treponema denticola VSY0
Manually annotated by BRENDA team