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Literature summary for 6.2.1.12 extracted from

  • Hess, V.; Vitt, S.; Müller, V.
    A caffeyl-coenzyme A synthetase initiates caffeate activation prior to caffeate reduction in the acetogenic bacterium Acetobacterium woodii (2011), J. Bacteriol., 193, 971-978.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.12

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Acetobacterium woodii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 ATP 30°C, pH 7.0 Acetobacterium woodii
0.025
-
 caffeate 30°C, pH 7.0 Acetobacterium woodii
0.5
-
 CoA 30°C, pH 7.0 Acetobacterium woodii

Metals/Ions

Metals/Ions Comment Organism Structure
K+ strictly K+-dependent. Half-maximal activity is obtained at 6 mM K+ Acetobacterium woodii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 x * 60000, SDS-PAGE Acetobacterium woodii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + caffeate + CoA Acetobacterium woodii the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion AMP + diphosphate + caffeoyl-CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Acetobacterium woodii F1CYZ6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Acetobacterium woodii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 4-coumarate + CoA 52% of the activity with caffeate Acetobacterium woodii AMP + diphosphate + 4-coumaroyl-CoA
-
 ?
ATP + caffeate + CoA
-
 Acetobacterium woodii AMP + diphosphate + caffeoyl-CoA
-
 ?
ATP + caffeate + CoA the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion Acetobacterium woodii AMP + diphosphate + caffeoyl-CoA
-
 ?
ATP + cinnamate + CoA 9% of the activity with caffeate Acetobacterium woodii AMP + diphosphate + cinnamoyl-CoA
-
 ?
ATP + ferulate + CoA 16% of the activity with caffeate Acetobacterium woodii AMP + diphosphate + feruloyl-CoA
-
 ?
additional information no activity with either sinapate or 4-hydroxybenzoate. The more hydroxyl groups are present, the better is the activity of the enzyme. Methoxy groups on the aromatic ring have a negative effect on enzyme activity. It is possible that methoxy groups cause a steric obstruction. No activity can be measured if there is no acryl group present in the substrate Acetobacterium woodii ?
-
 ?

Subunits

Subunits Comment Organism
? x * 60000, SDS-PAGE Acetobacterium woodii

Synonyms

Synonyms Comment Organism
caffeoyl-CoA ligase
-
 Acetobacterium woodii
caffeoyl-CoA synthetase
-
 Acetobacterium woodii
caffeoyl-coenzyme A synthetase
-
 Acetobacterium woodii
CarB
-
 Acetobacterium woodii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 40
-
 Acetobacterium woodii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.5
-
 CoA 30°C, pH 7.0 Acetobacterium woodii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8
-
 Acetobacterium woodii

Expression

Organism Comment Expression
Acetobacterium woodii CarE and CarD (and thus the caffeate reduction operon) are induced in cells grown in the presence of cinnamate, sinapate, caffeate, ferulate, or 4-coumarate up

General Information

General Information Comment Organism
metabolism the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion Acetobacterium woodii