3.13.1.3: 2'-hydroxybiphenyl-2-sulfinate desulfinase
This is an abbreviated version!
For detailed information about 2'-hydroxybiphenyl-2-sulfinate desulfinase, go to the full flat file.
Word Map on EC 3.13.1.3
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3.13.1.3
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desulfurization
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dibenzothiophene
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rhodococcus
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2-hydroxybiphenyl
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erythropolis
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petroleum
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sulfur
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sulfite
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carbon-sulfur
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biodesulfurization
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thiophenic
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sulfonate
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organosulfur
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energy production
- 3.13.1.3
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desulfurization
- dibenzothiophene
- rhodococcus
- 2-hydroxybiphenyl
- erythropolis
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petroleum
- sulfur
- sulfite
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carbon-sulfur
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biodesulfurization
-
thiophenic
- sulfonate
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organosulfur
- energy production
Reaction
Synonyms
2'-hydroxybiphenyl-2-sulfinate desulfinase, 2'-hydroxybiphenyl-2-sulfinic acid desulfinase, 2-(2'-hydroxyphenyl)benzene sulfinate desulfinase, 2-(2'-hydroxyphenyl)benzene sulfinate hydrolase, 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase, 2-(2-hydroxyphenyl)benzenesulfinate:H2O hydrolase, Desulfinase, DszB, EC 3.1.2.24, gene dszB-encoded hydrolase, hydrolase, 2,(2'-hydroxyphenyl)benzene sulfinate, TdsB
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Engineering
Engineering on EC 3.13.1.3 - 2'-hydroxybiphenyl-2-sulfinate desulfinase
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C17S
C26S
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site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
Q65H
increase in thermostability, decrease in catalytic activity
R70I
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inactive mutant mostly exists in the insoluble fraction of the cell extract
R70K
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inactive mutant mostly exists in the insoluble fraction of the cell extract
Y63F
increase in catalytic activity, similar thermostability as wild-type
Y63F/Q65H
increase in thermostability without loss of catalytic activity or affinity for substrate
Y63S
affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
Q65H
Rhodococcus erythropolis IGTS8 / ATCC 53968
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increase in thermostability, decrease in catalytic activity
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Y63F
Rhodococcus erythropolis IGTS8 / ATCC 53968
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increase in catalytic activity, similar thermostability as wild-type
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Y63S
Rhodococcus erythropolis IGTS8 / ATCC 53968
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affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
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C26S
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site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
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site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
C17S
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site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
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