Information on EC 4.1.1.102 - phenacrylate decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.1.102
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RECOMMENDED NAME
GeneOntology No.
phenacrylate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-coumarate = 4-vinylphenol + CO2
show the reaction diagram
(1)
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-
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ferulate = 4-vinylguaiacol + CO2
show the reaction diagram
(3)
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-
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trans-cinnamate = styrene + CO2
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylpropanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
3-phenylprop-2-enoate carboxy-lyase
The enzyme, found in fungi, catalyses the decarboxylation of phenacrylic acids present in plant cell walls. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumarate
4-vinylphenol + CO2
show the reaction diagram
4-hydroxycinnamate
4-hydroxystyrene + CO2
show the reaction diagram
caffeate
3,4-dihydroxystyrene + CO2
show the reaction diagram
ferulate
4-vinylguaiacol + CO2
show the reaction diagram
additional information
?
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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
4-coumarate
4-vinylphenol + CO2
show the reaction diagram
ferulate
4-vinylguaiacol + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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1 mM, 62.9% residual activity
Cu2+
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1 mM, almost complete loss of activity
Fe2+
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1 mM, 94.3% residual activity
Fe3+
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1 mM, 1.7% residual activity
Mg2+
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1 mM, 69.7% residual activity
Mn2+
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1 mM, 67.9% residual activity
Ni2+
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1 mM, 81.8% residual activity
Zn2+
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1 mM, almost complete loss of activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoic acid
0.1 mM, 55% residual activity
EDTA
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0.5 mM, 5.6% inhibition
N-ethylmaleiimide
0.1 mM, 88% residual activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteic acid
1 mM, 151% of initial activity
D-Cysteine
1 mM, 150% of initial activity
dithiothreitol
0.2-1 mM, slightly enhances decarboxylation of ferulic acid without affecteing decarboxylation of 4-coumarate
DL-homoserine
1 mM, 160% of initial activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.79
4-coumarate
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pH 6.5, 30C
0.73 - 3.52
ferulate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 2.15
ferulate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.91
ferulate
1047
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16.3
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wild-type, pH 7.0, 37C
20.1
mutant M57L, substrate ferulate, 25C, pH 6.0
378
wild-type, substrate ferulate, 25C, pH 6.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
potassium phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
complete loss of activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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isoelectric focusing
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
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2 * 21500, SDS-PAGE, 2 * 19000, calculated
19828
x * 19828, calculated
20400
2 * 20400, SDS-PAGE
21500
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2 * 21500, SDS-PAGE, 2 * 19000, calculated
23000
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x * 23000, SDS-PAGE
40400
gel filtration
42000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures in complex with substrate analogues. FADase possesses a half-opened bottom beta-barrel with the catalytic pocket located between the middle of the core beta-barrel and the helical bottom. Its structure shared a high degree of similarity with members of the phenolic acid decarboxylase (PAD) superfamily. FADase catalyzed reactions by an open-closed mechanism involving a pocket on the surface of the enzyme. During decarboxylation of ferulic acid by FADase, Trp25 and Tyr27 are required for the entering and proper orientation of the substrate while Glu134 and Asn23 participate in proton transfer
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modeling of structure based on PDB entry 2GC9. Residue Met57 is located at the entrance of the pocket and in the immediate vicinity of possible catalytic residues Arg60 and Glu82. Residue Met103 is spatially more distant from the two catalytic residues and located deeper in the active-site pocket
to 2.45 A resolution. The conformational flexibility of the beta2e-alpha5 loop allows access to the active site. The structure implicates Glu285 as the general base. An about 30-A-long pocket adjacent to the catalytic site may accommodate the isoprenoid tail of the substrate needed for ubiquinone biosynthesis in yeast
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression n Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D112N
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121% of wild-type activity
E134A
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mutation decreases the enzyme activity by more than 60%
F95A
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120% of wild-type activity
F95A/D112N
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395% of wild-type activity
F95A/S157I
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218% of wild-type activity
F95A/V151I
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333% of wild-type activity
F95E
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26% of wild-type activity
F95I
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148% of wild-type activity
F95I/D112N
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418% of wild-type activity
F95I/S157I
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299% of wild-type activity
F95I/V151I
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323% of wild-type activity
F95K
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18% of wild-type activity
F95L
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188% of wild-type activity
F95L/D112N
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485% of wild-type activity
F95L/D112N/S157I
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430% of wild-type activity
F95L/D112N/V151I
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1354% of wild-type activity; approximately 34fold higher catalytic activity than wild-type for the production of 4-vinylguaiacol from ferulic acid, possibly due to formation of a compact active site compared with that of the wild-type
F95L/S157I
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528% of wild-type activity
F95L/V151I
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746% of wild-type activity
F95L/V151I/S157I
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484% of wild-type activity
F95Q
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48% of wild-type activity
F95R
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19% of wild-type activity
S157I
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171% of wild-type activity
V151I
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174% of wild-type activity
W25A
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mutation decreases the enzyme activity by more than 95%
Y21A
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mutation abolishes the enzyme activity completely
Y27A
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mutation abolishes the enzyme activity completely
D112N
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121% of wild-type activity
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E134A
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mutation decreases the enzyme activity by more than 60%
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F95A
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120% of wild-type activity
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F95L
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188% of wild-type activity
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F95L/D112N/V151I
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1354% of wild-type activity; approximately 34fold higher catalytic activity than wild-type for the production of 4-vinylguaiacol from ferulic acid, possibly due to formation of a compact active site compared with that of the wild-type
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W25A
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mutation decreases the enzyme activity by more than 95%
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Y21A
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mutation abolishes the enzyme activity completely
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Y27A
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mutation abolishes the enzyme activity completely
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M57A
almost complete loss of activity
M57L
mutation does not increase the ratio of decarboxylation activity toward ferulate to 4-coumarate
M57T
almost complete loss of activity
M57A
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almost complete loss of activity
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M57L
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mutation does not increase the ratio of decarboxylation activity toward ferulate to 4-coumarate
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M57T
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almost complete loss of activity
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E285A
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loss of catalytic activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
brewing
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a positive relationship exists between single nucleotide polymorphisms in phenylacrylic acid decarboxylase PAD1 and ferulic acid decarboxylase FDC1 genes and the ferulic acid decarboxylation ability of industrial yeast strains. Sake, shochu, and standard top-fermenting yeasts contain a nonsense mutation of FDC1, whereas a frameshift mutation is identified in the FDC1 gene of bottom-fermenting yeast. No nonsense or frameshift mutations are detected in laboratory, wine, or weizen beer yeast strains. When FDC1 is introduced into sake and shochu yeast strains, the transformants exhibit ferulic acid decarboxylation activity
synthesis
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synthesis of vanillin by use of ferulic acid decarboxylase Fdc from Bacillus pumilus and 4-vinylguaiacol oxygenase Cso2 from Caulobacter segnis. In the first stage, Escherichia coli cells expressing Fdc rapidly decarboxylate ferulic acid and completely convert 75 mM of this substrate to 4-vinylguaiacol within 2 h at pH 9.0. In the second stage, Escherichia coli cells expressing Cso2 efficiently oxidize 4-vinylguaiacol to vanillin. The concentration of vanillin reaches 52 mM (7.8 g/l) in 24 h
Show AA Sequence (269 entries)
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