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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
gallate decarboxylase, gallic acid decarboxylase,
more
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Decarboxylase, gallate
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Gallic acid decarboxylase
Gallic acid decarboxylase
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Gallic acid decarboxylase
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3,4,5-trihydroxybenzoate = 1,2,3-trihydroxybenzene + CO2
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3,4,5-trihydroxybenzoate carboxy-lyase (pyrogallol-forming)
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3,4,5-Trihydroxybenzoate
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
gallic acid
pyrogallol + CO2
protocatechuic acid
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protocatechuic acid
catechol + CO2
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additional information
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no substrtaes: 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, 2,3-dihydroxybenzoic acid, 2,4-dihydroxybenzoic acid and 2,5-dihydroxybenzoic acid
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3,4,5-Trihydroxybenzoate
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inducible by protocatechuic acid, 3,5-dihydroxybenzoate, and 3-hydroxybenzoate
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3,4,5-Trihydroxybenzoate
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inducible by protocatechuic acid, 3,5-dihydroxybenzoate, and 3-hydroxybenzoate
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3,4,5-Trihydroxybenzoate
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constitutive enzyme
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3,4,5-Trihydroxybenzoate
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enzyme is involved in aromatic catabolism
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3,4,5-Trihydroxybenzoate
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enzyme is involved in aromatic catabolism
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3,4,5-Trihydroxybenzoate
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constitutive enzyme
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3,4,5-Trihydroxybenzoate
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enzyme is involved in modification of aromatic substrates and in ring cleavage
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3,4,5-Trihydroxybenzoate
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enzyme is involved in modification of aromatic substrates and in ring cleavage
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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reverse reaction not catalyzed
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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i.e. gallic acid
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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i.e. gallic acid, substrate-inducible enzyme activity
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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i.e. gallic acid
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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i.e. gallic acid, involved in degradation of tannic acid, a mechanism to reduce the inhibitory effect of tannins on cell growth
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gallic acid
pyrogallol + CO2
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gallic acid
pyrogallol + CO2
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gallic acid
pyrogallol + CO2
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gallic acid
pyrogallol + CO2
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gallic acid
pyrogallol + CO2
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gallic acid
pyrogallol + CO2
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gallic acid
pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
gallic acid
pyrogallol + CO2
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3,4,5-Trihydroxybenzoate
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inducible by protocatechuic acid, 3,5-dihydroxybenzoate, and 3-hydroxybenzoate
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3,4,5-Trihydroxybenzoate
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inducible by protocatechuic acid, 3,5-dihydroxybenzoate, and 3-hydroxybenzoate
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3,4,5-Trihydroxybenzoate
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constitutive enzyme
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3,4,5-Trihydroxybenzoate
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enzyme is involved in aromatic catabolism
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3,4,5-Trihydroxybenzoate
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enzyme is involved in aromatic catabolism
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3,4,5-Trihydroxybenzoate
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constitutive enzyme
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3,4,5-Trihydroxybenzoate
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enzyme is involved in modification of aromatic substrates and in ring cleavage
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3,4,5-Trihydroxybenzoate
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enzyme is involved in modification of aromatic substrates and in ring cleavage
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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i.e. gallic acid, substrate-inducible enzyme activity
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3,4,5-Trihydroxybenzoate
Pyrogallol + CO2
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i.e. gallic acid, involved in degradation of tannic acid, a mechanism to reduce the inhibitory effect of tannins on cell growth
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Iron
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required as cofactor, contains 0.8 mol of iron per mol of enzyme subunit
Ca2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Ca2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Cu2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Cu2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Fe2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Fe2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
K+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
K+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Mg2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Mg2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Mg2+
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dependent on, Km: 5 mM
Sn2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Sn2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Zn2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
Zn2+
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activation in decreasing order: Mg2+, Sn2+, Cu2+, Zn2+, K+, Ca2+, Fe2+
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Co2+
1 mM, 73% loss of activity
Cu2+
1 mM, 96% loss of activity
Fe2+
1 mM, complete loss of activity
Fe3+
1 mM, 76% loss of activity
Ni2+
1 mM, complete loss of activity
p-chloromercuribenzoate
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thiosulfate
1 mM, 15% loss of activity
EDTA
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
EDTA
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
SDS
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
SDS
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
Triton X-100
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
Triton X-100
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
Tween 20
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
Tween 20
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inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
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(NH4)2S2O8
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there is an activity increase of 52.7% in the presence of (NH4)2S2O8
ascorbic acid
1 mM, 107% of initial activity
dithiothreitol
1 mM, 116% of initial activity
EDTA
1 mM, 146% of initial activity
additional information
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not influenced by KCrO4
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additional information
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enzyme activity is elevated in presence of tannic acid or gallic acid in growth medium, but not of other phenolic acids
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0.96 - 3.3
3,4,5-Trihydroxybenzoate
0.7
gallic acid
pH 6.2, 40°C
3.2
protocatechuic acid
pH 6.2, 40°C
0.96
3,4,5-Trihydroxybenzoate
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3.3
3,4,5-Trihydroxybenzoate
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42
gallic acid
pH 6.2, 40°C
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protocatechuic acid
pH 6.2, 40°C
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additional information
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6
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assay at
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5 - 7
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pH 5.0: about 55% of maximal activity, pH 7.0: about 40% of maximal activity
5.6 - 7.1
more than 80% of maximum activity
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25
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assay at
35
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assay at
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25 - 45
more than 80% of maximum activity
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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i.e. Aerobacter aerogenes
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brenda
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brenda
no activity in Erwinia rhapontici
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no activity in Klebsiella terrigena
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no activity in Pantoea agglomerans
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i.e. Enterobacter agglomerans, strain T71
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brenda
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brenda
2 strains, YL-1 and ML-1, isolated from the phyllosphere of green leaves of Rosa rugosa
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brenda
type strain 2.2, formerly Streptococcus caprinus
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brenda
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no activity in the strains C14-17 and C15-41
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wild-type and mutant strain
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brenda
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physiological function
a gene deletion mutant is not able to grow on medium with gallic acid as carbon source but can grow in presence of protocatechuic acid
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LPDC_LACPL
Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
490
0
54259
Swiss-Prot
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A0A6S6XG23_9FIRM
494
0
54079
TrEMBL
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A0A7S4LX67_9GAMM
496
0
54225
TrEMBL
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A0A822IZN5_9EURY
75
0
8458
TrEMBL
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A0A653XK74_9GAMM
515
0
56191
TrEMBL
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A0A060TAG5_BLAAD
231
0
27210
TrEMBL
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57000
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6 * 57000, SDS-PAGE
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?
x * 27300, calculated from sequence, x * 25000, SDS-PAGE, recombinant protein
hexamer
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6 * 57000, SDS-PAGE
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6 - 10
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stable in the range
4733
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35
24 h, 60% loss of activity
40
stable for 7 h, rapid loss of activity thereafter
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crude enzyme is very unstable, several attempts to purify the enzyme have so far been unsuccessful
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dilution and dialysis completely inactivates
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oxygen-sensitive enzyme
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4733
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-20°C, 50 mM potassium phosphate buffer, pH 6.0, containing glycerol and reducing agents, stable for 3 weeks
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5°C, 90% loss of activity after 2 days, crude enzyme
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Talon Superflow resin column chromatography, and gel filtration
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expressed in Escherichia coli strain JW2308-4
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expression is induced by gallic acid and protocatechuic acid
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synthesis
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synthesis of pyrogallol from readily available tannic acid by using the combined action of gallate decarboxylase and tannase in a two-enzyme resting cell bioconversion
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Grant, D.J.W.; Patel, J.C.
The non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes)
Antonie van Leeuwenhoek
35
325-343
1969
Klebsiella aerogenes
brenda
Yoshida, H.; Tani, Y.; Yamada, H.
Isolation and identification of a pyrogallol producing bacterium from soil
Agric. Biol. Chem.
46
2539-2546
1982
Citrobacter sp., Citrobacter sp. 64-1
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brenda
Samain, E.; Albagnac, G.; Dubourguier, H.C.
Initial steps of catabolism of trihydroxybenzenes in Pelobacter acidigallici
Arch. Microbiol.
144
242-244
1986
Pelobacter acidigallici
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brenda
Krumholz, L.R.; Crawford, R.L.; Hemling, M.E.; Bryant, M.P.
Metabolism of gallate and phloroglucinol in Eubacterium oxidoreducens via 3-hydroxy-5-oxohexanoate
J. Bacteriol.
169
1886-1890
1987
Eubacterium oxidoreducens
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Haddock, J.D.; Ferry, J.G.
Initial steps in the anaerobic degradation of 3,4,5-trihydroxybenzoate by Eubacterium oxidoreducens: characterization of mutants and role of 1,2,3,5-tetrahydroxybenzene
J. Bacteriol.
175
669-673
1993
Eubacterium oxidoreducens
brenda
Zeida, M.; Wieser, M.; Yoshida, T.; Sugio, T.; Nagasawa, T.
Purification and characterization of gallic acid decarboxylase from Pantoea agglomerans T71
Appl. Environ. Microbiol.
64
4743-4747
1998
Pantoea agglomerans
brenda
Brune, A.; Schink, B.
Phloroglucinol pathway in the strictly anaerobic Pelobacter acidigallici: fermentation of trihydroxybenzenes to acetate via triacetic acid
Arch. Microbiol.
157
417-424
1992
Pelobacter acidigallici
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brenda
Hashidoko, Y.; Itoh, E.; Yokota, K.; Yoshida, T.; Tahara, S.
Characterization of five phyllosphere bacteria isolated from Rosa rugosa leaves, and their phenotypic and metabolic properties
Biosci. Biotechnol. Biochem.
66
2474-2478
2002
Rahnella aquatilis, no activity in Pantoea agglomerans, no activity in Klebsiella terrigena, no activity in Erwinia rhapontici
brenda
O'Donovan, L.; Brooker, J.D.
Effect of hydrolysable and condensed tannins on growth, morphology and metabolism of Streptococcus gallolyticus (S. caprinus) and Streptococcus bovis
Microbiology
147
1025-1033
2001
Streptococcus gallolyticus
brenda
Jimenez, N.; Curiel, J.A.; Reveron, I.; de Las Rivas, B.; Munoz, R.
Uncovering the Lactobacillus plantarum WCFS1 gallate decarboxylase involved in tannin degradation
Appl. Environ. Microbiol.
79
4253-4263
2013
Lactiplantibacillus plantarum
brenda
Srivastava, A.; Kar, R.
Production of gallic acid by immobilized Aspergillus niger using polyurethane foam as solid support
Int. J. Food Eng.
7
0000
2011
Aspergillus niger
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brenda
Li, W.; Wang, C.; Zhang, C.; Ye, J.
Screen the strains of producing gallic acid decarboxylase and enzymic activities
Chem. Eng. (China)
44
1-6
2016
Enterobacter cloacae, Citrobacter freundii, Enterobacter cloacae CICC 22001, Citrobacter freundii CICC 22001, Enterobacter cloacae CICC 10017
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Meier, A.; Worch, S.; Boer, E.; Hartmann, A.; Mascher, M.; Marzec, M.; Scholz, U.; Riechen, J.; Baronian, K.; Schauer, F.; Bode, R.; Kunze, G.
Agdc1p - a gallic acid decarboxylase involved in the degradation of tannic acid in the yeast Blastobotrys (Arxula) adeninivorans
Front. Microbiol.
8
1777
2017
Blastobotrys adeninivorans (A0A060TAG5)
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