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Literature summary 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.108 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
1.3.1.108 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
1.3.1.108 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
1.3.1.108 350000
-
 caffeoyl-CoA reductase and the electron transfer flavoprotein CarDE form a stable complex Acetobacterium woodii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.108 (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
-
 ?
1.3.1.108 (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

EC Number Organism UniProt Comment Textmining
1.3.1.108 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
-
1.3.1.108 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)

EC Number Purification (Comment) Organism
1.3.1.108
-
 Acetobacterium woodii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.108 (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
-
 ?
1.3.1.108 (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
-
 ?
1.3.1.108 (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
-
 ?
1.3.1.108 (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
-
 ?
1.3.1.108 4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 Acetobacterium woodii ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.108 4-coumaroyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 Acetobacterium woodii DAM 1030 ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.108 feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 Acetobacterium woodii ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.108 feruloyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 Acetobacterium woodii DAM 1030 ? + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.108 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.1.108 30
-
 caffeoyl-CoA-dependent methyl viologen oxidation assay Acetobacterium woodii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.108 7.5
-
 caffeoyl-CoA-dependent methyl viologen oxidation assay Acetobacterium woodii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.3.1.108 6 9 pH 6.0: about 30% of maximal activity, pH 9.0: about 30% of maximal activity Acetobacterium woodii

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.108 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
1.3.1.108 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
1.3.1.108 [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

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