BRENDA - Reference to 1.13.11.57; Id = 746263

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

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

G2IKE5

-

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

-

?

30

-

assay at

Sphingobium sp. SYK-6

7.5

-

assay at

Sphingobium sp. SYK-6

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

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

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

-

?

30

-

assay at

Sphingobium sp. SYK-6

7.5

-

assay at

Sphingobium sp. SYK-6

746263

Sugimoto

Molecular mechanism of strict ...

Sphingobium sp. SYK-6

PLoS ONE

9

e92249

2014

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1

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1

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1

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1

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1

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1

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1

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1

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1

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1

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1

-

716261

Nogales

Unravelling the gallic acid de ...

Pseudomonas putida, Pseudomonas putida KT 2240

Mol. Microbiol.

79

359-374

2011

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1

-

1

-

42

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1

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2

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1

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1

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1

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2

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713675

Sugimoto

Crystallization and preliminar ...

Sphingobium sp.

Acta Crystallogr. Sect. F

F65

1171-1174

2009

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1

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1

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2

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1

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1

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1

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1

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1

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1

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1

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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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1

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1

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1

3

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4

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1

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6

1

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1

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1

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1

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1

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1

3

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1

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6

1

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1

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1

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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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1

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3

1

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1

3

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45

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1

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2

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4

1

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1

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1

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3

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1

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1

3

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1

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4

1

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Molecular mechanism of strict substrate specificity of an extradiol dioxygenase, DesB, derived from Sphingobium sp. SYK-6

Data extracted from this reference: