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Information on EC 2.8.3.23 - caffeate CoA-transferase and Organism(s) Acetobacterium woodii and UniProt Accession F1CYZ5

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.3 CoA-transferases
                2.8.3.23 caffeate CoA-transferase
IUBMB Comments
The enzyme, isolated from the bacterium Acetobacterium woodii, catalyses an energy-saving CoA loop for caffeate activation. In addition to caffeate, the enzyme can utilize 4-coumarate or ferulate as CoA acceptor.
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This record set is specific for:
Acetobacterium woodii
UNIPROT: F1CYZ5
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The taxonomic range for the selected organisms is: Acetobacterium woodii
The enzyme appears in selected viruses and cellular organisms
Synonyms
CarA, YdiF, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-(3,4-dihydroxyphenyl)propanoyl-CoA + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate = 3-(3,4-dihydroxyphenyl)propanoate + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA
show the reaction diagram
the enzyme uses a ping-pong mechanism for CoA transfer, it has two catalytic domains on one polypeptide chain. (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate = caffeate. 3,4-dihydroxyphenylpropanoate = hydrocaffeate
SYSTEMATIC NAME
IUBMB Comments
3-(3,4-dihydroxyphenyl)propanoyl-CoA:(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate CoA-transferase
The enzyme, isolated from the bacterium Acetobacterium woodii, catalyses an energy-saving CoA loop for caffeate activation. In addition to caffeate, the enzyme can utilize 4-coumarate or ferulate as CoA acceptor.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylpropanoyl-CoA + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
3,4-dihydroxyphenylpropanoate + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA
show the reaction diagram
3,4-dihydroxyphenylpropanoyl-CoA + 4-coumarate
3,4-dihydroxyphenylpropanoate + 4-coumaroyl-CoA
show the reaction diagram
3,4-dihydroxyphenylpropanoyl-CoA i.e. hydrocaffeoyl-CoA
-
-
?
3,4-dihydroxyphenylpropanoyl-CoA + ferulate
3,4-dihydroxyphenylpropanoate + feruloyl-CoA
show the reaction diagram
86% compared to the activity with 4-coumarate
-
-
?
additional information
?
-
no activity with cinnamate, sinapate, or 4-hydroxybenzoate as a CoA acceptor. Neither acetyl-CoA nor butanoyl-CoA serve as the CoA donor for the enzyme
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylpropanoyl-CoA + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
3,4-dihydroxyphenylpropanoate + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA
show the reaction diagram
the enzyme catalyzes an energy-saving CoA loop for caffeate activation. 3-(3,4-dihydroxyphenyl)acrylate i.e. caffeate
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 7.5, 40°C
0.008
3,4-dihydroxyphenylpropanoyl-CoA
pH 7.5, 40°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
3,4-dihydroxyphenylpropanoyl-CoA
pH 7.5, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
coenzyme A transferase CarA, acyl-CoA synthetase CarB, and acyl-CoA dehydrogenase CarC are part of the caffeate respiration pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CARA_ACEWO
524
0
56205
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
gel filtration
57700
x * 57700, calculated
60000
2 * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 57700, calculated
homodimer
2 * 60000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduction in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the car operon is induced by caffeate, p-coumarate, ferulate, and cinnamate and also by sinapate
there is no induction by p-hydroxybenzoate or syringate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hess, V.; Gonzalez, J.M.; Parthasarathy, A.; Buckel, W.; Mller, V.
Caffeate respiration in the acetogenic bacterium Acetobacterium woodii: a coenzyme A loop saves energy for caffeate activation
Appl. Environ. Microbiol.
79
1942-1947
2013
Acetobacterium woodii (F1CYZ5)
Manually annotated by BRENDA team
Hess, V.; Vitt, S.; Mller, V.
A caffeyl-coenzyme A synthetase initiates caffeate activation prior to caffeate reduction in the acetogenic bacterium Acetobacterium woodii
J. Bacteriol.
193
971-978
2011
Acetobacterium woodii (F1CYZ5)
Manually annotated by BRENDA team