We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments Contains non-heme Fe2+. The enzyme is a ring-cleavage dioxygenase that acts specifically on 3,4,5-trihydroxybenzoate to produce the keto-tautomer of 4-oxalomesaconate [1,2].
The enzyme appears in viruses and cellular organisms
Synonyms
gallate dioxygenase, ga dioxygenase,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DesB
-
-
GA dioxygenase
-
-
GALA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3,4,5-trihydroxybenzoate + O2 = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
gallate:oxygen oxidoreductase
Contains non-heme Fe2+. The enzyme is a ring-cleavage dioxygenase that acts specifically on 3,4,5-trihydroxybenzoate to produce the keto-tautomer of 4-oxalomesaconate [1,2].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3,4,5-trihydroxybenzoate + O2
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
DesB has strict substrate specificity for 3,4,5-trihydroxybenzoate (gallate). Biochemical and structural study show the substrate recognition and catalytic mechanisms of extradiol dioxygenase DesB. Mutational analysis reveals that His124 and His192 in the active site are essential to the catalytic reaction of the extradiol dioxygenase DesB. His124, which interacts with OH(4) of the bound gallate, seems to contribute to proper positioning of the substrate in the active site. His192, which is located close to OH (3) of the gallate, is likely to serve as the catalytic base. Glu377' interacts with OH(5) of the gallate and seems to play a critical role in the substrate specificity
-
?
gallate + O2
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
gallate + O2
4-oxalomesaconate
additional information
?
-
gallate + O2
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
-
gallate is also namend gallic acid or 3,4,5-trihydroxybenzoic acid
-
?
gallate + O2
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
-
gallate is also namend gallic acid or 3,4,5-trihydroxybenzoic acid
-
?
gallate + O2
4-oxalomesaconate
-
the substrate specificity is very restricted toward gallate
-
?
gallate + O2
4-oxalomesaconate
-
the substrate specificity is very restricted toward gallate
-
?
gallate + O2
4-oxalomesaconate
-
-
-
?
gallate + O2
4-oxalomesaconate
-
-
?
gallate + O2
4-oxalomesaconate
-
-
?
pyrogallol + O2
?
-
-
?
additional information
?
-
-
no activity with protocatechuate, catechol, resorcinolate, resorcinol, gentisate, hydroquinone, pyrogallol, methylgallate, or syringate
-
?
additional information
?
-
-
no activity with protocatechuate, catechol, resorcinolate, resorcinol, gentisate, hydroquinone, pyrogallol, methylgallate, or syringate
-
?
additional information
?
-
no activity with protocatechuate, 3-O-methylgallate, gentisate, 2,3-dihydroxybiphenyl, 4-methylcatechol, 2,3-dihydroxybenzoate, and methylgallate
-
?
additional information
?
-
no activity with protocatechuate, 3-O-methylgallate, gentisate, 2,3-dihydroxybiphenyl, 4-methylcatechol, 2,3-dihydroxybenzoate, and methylgallate
-
?
additional information
?
-
-
no activity with protocatechuate, 3-O-methylgallate, gentisate, 2,3-dihydroxybiphenyl, 4-methylcatechol, 2,3-dihydroxybenzoate, and methylgallate
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
required for activity
Fe2+
the catalytic reaction of the extradiol dioxygenase DesB requires the shift of the Fe(II) ion, leading to the bidentate coordination of the substrate to the Fe(II) ion
Fe2+
DesB requires Fe2+ for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,2'-dipyridyl
-
2 mM 2,2'-dipyridyl, a specific Fe2+-chelator, abolishes the gallate dioxygenase activity completely
H2O2
-
hydrogen peroxide at 1 mM reduces the gallate dioxygenase activity to 15%, and the activity can be partially restored (50% activity of the untreated enzyme) upon addition of 10 mM ascorbate
EDTA
-
complete inhibition at 1 mM, the activity is only fully recovered with Fe2+
EDTA
complete inhibition at 0.5 mM, the oxygen consumption activity after EDTA treatment is completely recovered by addition of Fe2+ (119%)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0669
gallate
in 50 mM GTA buffer (pH 8.5) consisting of 50 mM 3,3-dimethylglutarate, 50 mM Tris, and 50 mM 2-amino-2-methyl-1,3-propanediol, at 30°C
0.144
gallate
-
in 100 mM Tris-HCl, pH 7.0, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
21.4
-
crude extract, in 100 mM Tris-HCl, pH 7.0, at 30°C
42.7
-
after 2fold purification, in 100 mM Tris-HCl, pH 7.0, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 9
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30
assay at
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
formerly Sphingomonas paucimobilis strain SYK-6
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
the enzyme is involved in syringate catabolism, the pathway involving DesB plays an especially important role in the growth of Sphingomonas paucimobilis SYK-6 on syringate, and DesB is involved in gallate degradation
physiological function
-
the GalA protein is the only dioxygenase involved in gallate cleavage in Pseudomonas putida KT2440
physiological function
-
the enzyme is involved in syringate catabolism, the pathway involving DesB plays an especially important role in the growth of Sphingomonas paucimobilis SYK-6 on syringate, and DesB is involved in gallate degradation
physiological function
-
the GalA protein is the only dioxygenase involved in gallate cleavage in Pseudomonas putida KT2440
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
132000
-
molar mass obtained by sedimentation equilibrium
45000
2 * 45000, SDS-PAGE
46843
2 * 46843, calculated from amino acid sequence
47000
-
3 * 47000, SDS-PAGE
47644
-
3 * 47644, calculated from amino acid sequence
47700
-
calculated from amino acid sequence
93800
-
calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homodimer
-
x-ray crystallography
homodimer
2 * 45000, SDS-PAGE
homodimer
2 * 46843, calculated from amino acid sequence
homodimer
-
2 * 45000, SDS-PAGE
homodimer
-
2 * 46843, calculated from amino acid sequence
homotrimer
-
3 * 47000, SDS-PAGE
homotrimer
-
3 * 47644, calculated from amino acid sequence
homotrimer
-
3 * 47000, SDS-PAGE
homotrimer
-
3 * 47644, calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hanging drop vapor diffusion method, using 25% (w/v) PEG 8000, 0.1 M sodium acetate trihydrate, 0.1 M HEPES-NaOH pH 7.8, at 4°C
-
crystallographic analyses of DesB shows that gallate is recognized by several hydrogen bonds. Three groups of the hydrogen bonds recognize a substrate and place the substrate in a productive arrangement
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POROS PI column chromatography and POROS HQ column chromatography
-
POROS polyethyleneimine column chromatography
ultracentrifugation and phenyl-Sepharose column chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
the expression of the galA gene is specifically induced by gallate
the expression of the galA gene is specifically induced by gallate
-
the expression of the galA gene is specifically induced by gallate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sugimoto, K.; Yamamoto, Y.; Antoni, S.; Senda, M.; Kasai, D.; Masai, E.; Fukuda, M.; Senda, T.
Crystallization and preliminary crystallographic analysis of gallate dioxygenase DesB from Sphingobium sp. SYK-6
Acta Crystallogr. Sect. F
F65
1171-1174
2009
Sphingobium sp.
brenda
Kasai, D.; Masai, E.; Miyauchi, K.; Katayama, Y.; Fukuda, M.
Characterization of the gallate dioxygenase gene: three distinct ring cleavage dioxygenases are involved in syringate degradation by Sphingomonas paucimobilis SYK-6
J. Bacteriol.
187
5067-5074
2005
Sphingomonas paucimobilis (Q5NTE5), Sphingomonas paucimobilis SYK-6 (Q5NTE5), Sphingomonas paucimobilis SYK-6
brenda
Nogales, J.; Canales, A.; Jimenez-Barbero, J.; Garcia, J.L.; Diaz, E.
Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440. The prototype of a new subgroup of extradiol dioxygenases
J. Biol. Chem.
280
35382-35390
2005
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Nogales, J.; Canales, A.; Jimenez-Barbero, J.; Serra, B.; Pingarron, J.M.; Garcia, J.L.; Diaz, E.
Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida
Mol. Microbiol.
79
359-374
2011
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Sugimoto, K.; Senda, M.; Kasai, D.; Fukuda, M.; Masai, E.; Senda, T.
Molecular mechanism of strict substrate specificity of an extradiol dioxygenase, DesB, derived from Sphingobium sp. SYK-6
PLoS ONE
9
e92249
2014
Sphingobium sp. SYK-6 (G2IKE5)
brenda
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.13.11.57 gallate dioxygenase
more
top
Information
