EC Number | Cloned (Comment) | Organism |
---|---|---|
3.8.1.5 | overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli JM109 | Sphingomonas paucimobilis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.8.1.5 | F151L | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | F151W | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | F151Y | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | F169L | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | N38D | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | N38E | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | N38F | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | N38Q | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
3.8.1.5 | W109L | site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme | Sphingomonas paucimobilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.8.1.5 | additional information | - |
additional information | kinetics of recombinant wild-type and mutant enzymes, analysis of electrostatic interaction energies | Sphingomonas paucimobilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.8.1.5 | Rhodococcus erythropolis | - |
strains Y2, m15-3, HA1, GJ70, NCIMB13064, and TB2, enzyme DhaA | - |
3.8.1.5 | Sphingomonas paucimobilis | - |
enzyme LinB | - |
3.8.1.5 | Sphingomonas paucimobilis UT26 | - |
enzyme LinB | - |
3.8.1.5 | Xanthobacter autotrophicus | P22643 | enzyme DhlA | - |
3.8.1.5 | Xanthobacter autotrophicus GJ10 | P22643 | enzyme DhlA | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.8.1.5 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli | Sphingomonas paucimobilis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.8.1.5 | 1-haloalkane + H2O = a primary alcohol + halide | 3 features are important for catalytic performance: i. a catalytic triad, ii. anoxyanion hole, and iii. the halide-stabilizing residues, which are not conserved among different haloalkane dehalogenases, active site structure, Asn38 is involved, SN2 reaction mechanism, modeling, overview | Sphingomonas paucimobilis | |
3.8.1.5 | 1-haloalkane + H2O = a primary alcohol + halide | 3 features are important for catalytic performance: i. a catalytic triad, ii. anoxyanion hole, and iii. the halide-stabilizing residues, which are not conserved among different haloalkane dehalogenases, active site structure, Asn41 is involved, SN2 reaction mechanism, modeling, overview | Rhodococcus erythropolis | |
3.8.1.5 | 1-haloalkane + H2O = a primary alcohol + halide | 3 features are important for catalytic performance: i. a catalytic triad, ii. anoxyanion hole, and iii. the halide-stabilizing residues, which are not conserved among different haloalkane dehalogenases, active site structure, Glu56 is involved, SN2 reaction mechanism, modeling, overview | Xanthobacter autotrophicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.8.1.5 | 1-chlorobutane + H2O | - |
Rhodococcus erythropolis | n-butanol + chloride | - |
? | |
3.8.1.5 | 1-chlorobutane + H2O | - |
Sphingomonas paucimobilis | n-butanol + chloride | - |
? | |
3.8.1.5 | 1-chlorobutane + H2O | - |
Xanthobacter autotrophicus | n-butanol + chloride | - |
? | |
3.8.1.5 | 1-chlorobutane + H2O | - |
Sphingomonas paucimobilis UT26 | n-butanol + chloride | - |
? | |
3.8.1.5 | 1-chlorobutane + H2O | - |
Xanthobacter autotrophicus GJ10 | n-butanol + chloride | - |
? | |
3.8.1.5 | 1-haloalkane + H2O | - |
Rhodococcus erythropolis | primary alcohol + halide | - |
? | |
3.8.1.5 | 1-haloalkane + H2O | - |
Sphingomonas paucimobilis | primary alcohol + halide | - |
? | |
3.8.1.5 | 1-haloalkane + H2O | - |
Xanthobacter autotrophicus | primary alcohol + halide | - |
? | |
3.8.1.5 | 1-haloalkane + H2O | - |
Sphingomonas paucimobilis UT26 | primary alcohol + halide | - |
? | |
3.8.1.5 | 1-haloalkane + H2O | - |
Xanthobacter autotrophicus GJ10 | primary alcohol + halide | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.8.1.5 | More | primary halide-stabilizing residues are Asn38 and Trp109, secondary halide-stabilizing residues are Trp207, Pro208, and Ile211 | Rhodococcus erythropolis |
3.8.1.5 | More | primary halide-stabilizing residues are Asn41 and Trp107, secondary halide-stabilizing residues are Phe205, Pro206, and Ile209 | Sphingomonas paucimobilis |
3.8.1.5 | More | primary halide-stabilizing residues are Trp125 and Trp175, secondary halide-stabilizing residues are Phe172, Pro223, and Val226 | Xanthobacter autotrophicus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.8.1.5 | DhaA | - |
Rhodococcus erythropolis |
3.8.1.5 | DhlA | - |
Xanthobacter autotrophicus |
3.8.1.5 | LinB | - |
Sphingomonas paucimobilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.8.1.5 | 37 | - |
assay at | Sphingomonas paucimobilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.8.1.5 | 7.5 | - |
assay at | Sphingomonas paucimobilis |