Data extracted from this reference:
Crystallization (Commentary)
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
Sphingobium sp. SYK-6
Metals/Ions
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
Sphingobium sp. SYK-6
Organism
Sphingobium sp. SYK-6
G2IKE5
Substrates and Products (Substrate)
3,4,5-trihydroxybenzoate + O2
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
746263
Sphingobium sp. SYK-6
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
?
Synonyms
DesB
Sphingobium sp. SYK-6
Temperature Optimum [°C]
30
assay at
Sphingobium sp. SYK-6
pH Optimum
7.5
assay at
Sphingobium sp. SYK-6
Crystallization (Commentary) (protein specific)
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
Sphingobium sp. SYK-6
Metals/Ions (protein specific)
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
Sphingobium sp. SYK-6
Substrates and Products (Substrate) (protein specific)
3,4,5-trihydroxybenzoate + O2
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
746263
Sphingobium sp. SYK-6
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
?
Temperature Optimum [°C] (protein specific)
30
assay at
Sphingobium sp. SYK-6
pH Optimum (protein specific)
7.5
assay at
Sphingobium sp. SYK-6
Other publictions for EC
746263
Sugimoto
Molecular mechanism of strict ...
Sphingobium sp. SYK-6
PLoS ONE
9
e92249
2014
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716261
Nogales
Unravelling the gallic acid de ...
Pseudomonas putida, Pseudomonas putida KT 2240
Mol. Microbiol.
79
359-374
2011
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713675
Sugimoto
Crystallization and preliminar ...
Sphingobium sp.
Acta Crystallogr. Sect. F
F65
1171-1174
2009
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715355
Kasai
Characterization of the gallat ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis SYK-6
J. Bacteriol.
187
5067-5074
2005
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715480
Nogales
Molecular characterization of ...
Pseudomonas putida, Pseudomonas putida KT 2240
J. Biol. Chem.
280
35382-35390
2005
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