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Enzyme Nomenclature
Information on EC 1.3.1.108 - caffeoyl-CoA reductase
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The expected taxonomic range for this enzyme is: Acetobacterium woodii
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EC NUMBER 
COMMENTARY 
1.3.1.108
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RECOMMENDED NAME
GeneOntology No.
caffeoyl-CoA reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3-(3,4-dihydroxyphenyl)propanoyl-CoA:NAD+, ferredoxin oxidoreductase
The enzyme, characterized from the bacterium Acetobacterium woodii, contains two [4Fe-4S] clusters and FAD. The enzyme couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. It also reduces 4-coumaroyl-CoA and feruloyl-CoA.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
H6LGM6: caffeoyl-CoA reductase CarC, H6LGM7: electron transfer flavoprotein beta subunit CarD, H6LGM8: electron transfer flavoprotein alpha subunit CarE
H6LGM6 and H6LGM7 and H6LGM8
UniProt
H6LGM6: caffeoyl-CoA reductase CarC, H6LGM7: electron transfer flavoprotein beta subunit CarD, H6LGM8: electron transfer flavoprotein alpha subunit CarE
H6LGM6 and H6LGM7 and H6LGM8
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
H6LGM6 and H6LGM7 and H6LGM8
the enzyme is involved in caffeate respiration
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
-
-
?
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
the caffeyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA. Reduction of caffeoyl-CoA is also catalyzed in absence of ferredoxin
-
-
?
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
-
-
?
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
the caffeyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA. Reduction of caffeoyl-CoA is also catalyzed in absence of ferredoxin
-
-
?
4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
-
-
-
?
4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
-
-
-
?
feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
-
-
-
?
feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
-
-
?
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
H6LGM6 and H6LGM7 and H6LGM8
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
H6LGM6 and H6LGM7 and H6LGM8
the enzyme contains 4 mol of FAD per of enzyme. The CarCDE complex requires FAD for catalytic activity. No activity can be detected when FAD or FMN (0.25 mM) are used alone as electron acceptor, but together with caffeyl-CoA, they are completely reduced with NADH as reductant. Caffeyl-CoA reduction is stimulated by 26- and 12fold with FAD and FMN, respectively. The Km value for both FAD and FMN is 0.1 mM. Thus, caffeyl-CoA and flavins are reduced simultaneously
FMN
H6LGM6 and H6LGM7 and H6LGM8
no activity can be detected when FAD or FMN (0.25 mM) are used alone as electron acceptor, but together with caffeyl-CoA, they are completely reduced with NADH as reductant. Caffeyl-CoA reduction is stimulated by 26- and 12-fold with FAD and FMN, respectively. The Km value for both FAD and FMN is 0.1 mM. Thus, caffeyl-CoA and flavins are reduced simultaneously
[4Fe-4S]-center
H6LGM6 and H6LGM7 and H6LGM8
the enzyme contains 2 [4Fe-4S] clusters. It contains 9 mol of iron, and 9 mol of acid-labile sulfur per mol of enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
H6LGM6 and H6LGM7 and H6LGM8
caffeoyl-CoA-dependent methyl viologen oxidation assay
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
H6LGM6 and H6LGM7 and H6LGM8
pH 6.0: about 30% of maximal activity, pH 9.0: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
H6LGM6 and H6LGM7 and H6LGM8
caffeoyl-CoA-dependent methyl viologen oxidation assay
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28200
H6LGM6 and H6LGM7 and H6LGM8
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE
41400
H6LGM6 and H6LGM7 and H6LGM8
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE
42500
H6LGM6 and H6LGM7 and H6LGM8
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE
350000
H6LGM6 and H6LGM7 and H6LGM8
caffeoyl-CoA reductase and the electron transfer flavoprotein CarDE form a stable complex
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
homotrimer
H6LGM6 and H6LGM7 and H6LGM8
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE
homotrimer
-
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.108)
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