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Information on EC 4.1.1.102 - phenacrylate decarboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q03034

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.102 phenacrylate decarboxylase
IUBMB Comments
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.
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Saccharomyces cerevisiae
UNIPROT: Q03034
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phenolic acid decarboxylase, ferulic acid decarboxylase, fadase, phenacrylate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferulic acid decarboxylase
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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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-methoxycinnamic acid
3-methoxystyrene + CO2
show the reaction diagram
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-
-
?
3-nitrocinnamic acid
3-nitrostyrene + CO2
show the reaction diagram
-
-
-
?
4-aminocinnamic acid
4-aminostyrene + CO2
show the reaction diagram
-
-
-
?
4-bromocinnamic acid
4-bromostyrene + CO2
show the reaction diagram
-
-
-
?
4-chlorocinnamic acid
4-chlorostyrene + CO2
show the reaction diagram
-
-
-
?
4-coumarate
4-vinylphenol + CO2
show the reaction diagram
4-cyanocinnamic acid
4-cyanostyrene + CO2
show the reaction diagram
-
-
-
?
4-fluorocinnamic acid
4-fluorostyrene + CO2
show the reaction diagram
-
-
-
?
4-formylcinnamic acid
4-formylstyrene + CO2
show the reaction diagram
-
-
-
?
4-hydroxycinnamic acid
4-hydroxystyrene + CO2
show the reaction diagram
-
-
-
?
4-methoxycinnamic acid
4-methoxystyrene + CO2
show the reaction diagram
-
-
-
?
4-methylcinnamic acid
4-methylstyrene + CO2
show the reaction diagram
-
-
-
?
4-nitrocinnamic acid
4-nitrostyrene + CO2
show the reaction diagram
-
-
-
?
ferulate
4-vinylguaiacol + CO2
show the reaction diagram
trans-cinnamate
styrene + CO2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Z)-2-fluoro-2-nitro-vinylbenzene
potent irreversible inhibitor. At 0.05 mM, enzyme is inactive within 10 min
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 0.79
4-coumarate
0.11 - 0.92
ferulate
0.18
trans-cinnamate
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
4-coumarate
pH 7.0, 25°C
1.5
ferulate
pH 7.0, 25°C
3.8
trans-cinnamate
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27
3-methoxycinnamic acid
25°C, pH 7.0
8.7 - 14.3
3-nitrocinnamic acid
12.4
4-aminocinnamic acid
25°C, pH 7.0
21.4
4-bromocinnamic acid
25°C, pH 7.0
19.7
4-chlorocinnamic acid
25°C, pH 7.0
25.5
4-coumarate
pH 7.0, 25°C
12.8
4-cyanocinnamic acid
25°C, pH 7.0
27.5
4-fluorocinnamic acid
25°C, pH 7.0
8.7
4-formylcinnamic acid
25°C, pH 7.0
4.55
4-hydroxycinnamic acid
25°C, pH 7.0
28.1
4-methoxycinnamic acid
25°C, pH 7.0
27
4-methylcinnamic acid
25°C, pH 7.0
13.6
ferulate
pH 7.0, 25°C
21 - 24.5
trans-cinnamate
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
protein PAD1 catalyzes the formation of a diffusible cofactor required by FDC for decarboxylase activity. Escherichia coli protein UbiX can also activate FDC
physiological function
-
gene expression in Streptomyces lividans leads to expression of FDC1 and conversion of trans-cinnamic acid to styrene
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
x * 57898, mass spectrometry, x * 57898, calculated from sequence, recombinant His-tagged protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E285A
loss of catalytic activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
brewing
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
degradation
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expression of aldehyde dehydrogenase Ald5, phenylacrylic acid decarboxylase Pad1, and alcohol acetyltransferases Atf1 and Atf2 increases conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid. Combined overexpression of ALD5, PAD1, ATF1 and ATF2 helps Saccharomyces cerevisiae in phenolics conversion and tolerance
synthesis
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styrene production from biomass-derived carbon sources, by culture of Streptomyces lividans expressing FDC1 together with Streptomyces lividans/p-encP, which produces trans-cinnamic acid. The coculture system combined with the recovery of styrene using polystyrene resin beads XAD-4 allows the production of styrene from glucose, cellobiose, or xylooligosaccharides, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhuiya, M.W.; Lee, S.G.; Jez, J.M.; Yu, O.
Structure and mechanism of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae
Appl. Environ. Microbiol.
81
4216-4223
2015
Saccharomyces cerevisiae (Q03034), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mukai, N.; Masaki, K.; Fujii, T.; Iefuji, H.
Single nucleotide polymorphisms of PAD1 and FDC1 show a positive relationship with ferulic acid decarboxylation ability among industrial yeasts used in alcoholic beverage production
J. Biosci. Bioeng.
118
50-55
2014
Saccharomyces cerevisiae (Q03034)
Manually annotated by BRENDA team
Lin, F.; Ferguson, K.L.; Boyer, D.R.; Lin, X.N.; Marsh, E.N.
Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase
ACS Chem. Biol.
10
1137-1144
2015
Saccharomyces cerevisiae (Q03034), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ferguson, K.L.; Arunrattanamook, N.; Marsh, E.N.
Mechanism of the novel prenylated flavin-containing enzyme ferulic acid decarboxylase probed by isotope effects and linear free-energy relationships
Biochemistry
55
2857-2863
2016
Saccharomyces cerevisiae (Q03034), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ferguson, K.L.; Eschweiler, J.D.; Ruotolo, B.T.; Marsh, E.N.G.
Evidence for a 1,3-dipolar cyclo-addition mechanism in the decarboxylation of phenylacrylic acids catalyzed by ferulic acid decarboxylase
J. Am. Chem. Soc.
139
10972-10975
2017
Saccharomyces cerevisiae (Q03034)
Manually annotated by BRENDA team
Fujiwara, R.; Noda, S.; Tanaka, T.; Kondo, A.
Styrene production from a biomass-derived carbon source using a coculture system of phenylalanine ammonia lyase and phenylacrylic acid decarboxylase-expressing Streptomyces lividans transformants
J. Biosci. Bioeng.
122
730-735
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH499
Manually annotated by BRENDA team
Adeboye, P.; Bettiga, M.; Olsson, L.
ALD5, PAD1, ATF1 and ATF2 facilitate the catabolism of coniferyl aldehyde, ferulic acid and p-coumaric acid in Saccharomyces cerevisiae
Sci. Rep.
7
42635
2017
Saccharomyces cerevisiae
Manually annotated by BRENDA team