Information on EC 1.3.1.108 - caffeoyl-CoA reductase

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The expected taxonomic range for this enzyme is: Acetobacterium woodii

EC NUMBER
COMMENTARY hide
1.3.1.108
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RECOMMENDED NAME
GeneOntology No.
caffeoyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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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.
ORGANISM
COMMENTARY hide
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
H6LGM6 and H6LGM7 and H6LGM8
caffeoyl-CoA-dependent methyl viologen oxidation assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
H6LGM6 and H6LGM7 and H6LGM8
pH 6.0: about 30% of maximal activity, pH 9.0: about 30% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
H6LGM6 and H6LGM7 and H6LGM8
caffeoyl-CoA-dependent methyl viologen oxidation assay
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
350000
H6LGM6 and H6LGM7 and H6LGM8
caffeoyl-CoA reductase and the electron transfer flavoprotein CarDE form a stable complex
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
H6LGM6 and H6LGM7 and H6LGM8