Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.1.108 extracted from

  • Bertsch, J.; Parthasarathy, A.; Buckel, W.; Müller, V.
    An electron-bifurcating caffeyl-CoA reductase (2013), J. Biol. Chem., 288, 11304-11311.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28200
-
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE Acetobacterium woodii
41400
-
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE Acetobacterium woodii
42500
-
1 * 42500 (electron transfer flavoprotein alpha subunit CarE) + 1 * 41400 (caffeoyl-CoA reductase CarC) + 1 * 28200 (electron transfer flavoprotein beta subunit CarD), SDS-PAGE Acetobacterium woodii
350000
-
caffeoyl-CoA reductase and the electron transfer flavoprotein CarDE form a stable complex Acetobacterium woodii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster Acetobacterium woodii 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 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 Acetobacterium woodii DAM 1030 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 3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
?

Organism

Organism UniProt Comment Textmining
Acetobacterium woodii H6LGM6 and H6LGM7 and H6LGM8 H6LGM6: caffeoyl-CoA reductase CarC, H6LGM7: electron transfer flavoprotein beta subunit CarD, H6LGM8: electron transfer flavoprotein alpha subunit CarE
-
Acetobacterium woodii DAM 1030 H6LGM6 and H6LGM7 and H6LGM8 H6LGM6: caffeoyl-CoA reductase CarC, H6LGM7: electron transfer flavoprotein beta subunit CarD, H6LGM8: electron transfer flavoprotein alpha subunit CarE
-

Purification (Commentary)

Purification (Comment) Organism
-
Acetobacterium woodii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster 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 Acetobacterium woodii 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 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 Acetobacterium woodii 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 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 Acetobacterium woodii DAM 1030 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 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 Acetobacterium woodii DAM 1030 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
-
Acetobacterium woodii ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
?
4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
Acetobacterium woodii DAM 1030 ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
?
feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
Acetobacterium woodii ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
?
feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
Acetobacterium woodii DAM 1030 ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
?

Subunits

Subunits Comment Organism
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 Acetobacterium woodii

Synonyms

Synonyms Comment Organism
caffeoyl-CoA reductase-Etf complex
-
Acetobacterium woodii
electron-bifurcating caffeoyl-CoA reductase
-
Acetobacterium woodii
hydrocaffeoyl-CoA:NAD+, ferredoxin oxidoreductase
-
Acetobacterium woodii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
caffeoyl-CoA-dependent methyl viologen oxidation assay Acetobacterium woodii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
caffeoyl-CoA-dependent methyl viologen oxidation assay Acetobacterium woodii

pH Range

pH Minimum pH Maximum Comment Organism
6 9 pH 6.0: about 30% of maximal activity, pH 9.0: about 30% of maximal activity Acetobacterium woodii

Cofactor

Cofactor Comment Organism Structure
FAD 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 Acetobacterium woodii
FMN 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 Acetobacterium woodii
[4Fe-4S]-center the enzyme contains 2 [4Fe-4S] clusters. It contains 9 mol of iron, and 9 mol of acid-labile sulfur per mol of enzyme Acetobacterium woodii

General Information

General Information Comment Organism
metabolism the enzyme is involved in caffeate respiration Acetobacterium woodii