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Literature summary for 3.8.1.5 extracted from

  • Chaloupkova, R.; Sykorova, J.; Prokop, Z.; Jesenska, A.; Moninkova, M.; Pavlova, M.; Tsuda, M.; Nagata, Y.; Damborsky, J.
    Modification of acivity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26, by engineering of its entrance tunnel (2003), J. Biol. Chem., 278, 52622-52628.
    View publication on PubMed
Search for more literature for 3.8.1.5

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Sphingomonas paucimobilis

Protein Variants

Protein Variants Comment Organism
L177A site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme Sphingomonas paucimobilis
L177C site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane, bromocyclohexane and 1-bromobutane Sphingomonas paucimobilis
L177D site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Sphingomonas paucimobilis
L177E site-directed mutagenesis, mutant cannot be expressed in Escherichia coli due to incorrect protein folding Sphingomonas paucimobilis
L177F site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme Sphingomonas paucimobilis
L177H site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Sphingomonas paucimobilis
L177I site-directed mutagenesis, inactive mutant, incorrect protein folding Sphingomonas paucimobilis
L177M site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme Sphingomonas paucimobilis
L177N site-directed mutagenesis, mutant cannot be expressed in Escherichia coli due to incorrect protein folding Sphingomonas paucimobilis
L177P site-directed mutagenesis, inactive mutant, incorrect protein folding Sphingomonas paucimobilis
L177Q site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane and 1-bromobutane Sphingomonas paucimobilis
L177R site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Sphingomonas paucimobilis
L177S site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane and 1-bromobutane Sphingomonas paucimobilis
L177T site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane and 1-bromobutane Sphingomonas paucimobilis
L177V site-directed mutagenesis, altered substrate specificity, especially high activity with 1-bromobutane Sphingomonas paucimobilis
L177W site-directed mutagenesis, altered substrate specificity, specifically highly active with 1-chlorobutane Sphingomonas paucimobilis
L177Y site-directed mutagenesis, altered substrate specificity, especially low activity with 1,2-dibromoethane Sphingomonas paucimobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of wild-type and mutant enzymes using substrate 1-chlorobutane and 1,2-dibromoethane Sphingomonas paucimobilis
0.235
-
 1-Chlorobutane pH 8.6, 37°C, recombinant wild-type enzyme, data from 2 experimental sets Sphingomonas paucimobilis
5.65
-
 1,2-Dibromoethane pH 8.6, 37°C, recombinant wild-type enzyme, data from 2 experimental sets Sphingomonas paucimobilis

Organism

Organism UniProt Comment Textmining
Sphingomonas paucimobilis
-
 enzyme LinB
-
Sphingomonas paucimobilis UT26
-
 enzyme LinB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Sphingomonas paucimobilis

Reaction

Reaction Comment Organism Reaction ID
1-haloalkane + H2O = a primary alcohol + halide substrate specificity is influenced by the size and shape of their entrance tunnel, surface residue Leu177 is involved and located at the tunnel opening Sphingomonas paucimobilis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 data from 2 experimental sets, relative activity of diverse L177 mutants compared to the wild-type enzyme with the different substrates, overview Sphingomonas paucimobilis
0.16
-
 purified recombinant wild-type enzyme, substrate chlorocyclohexane Sphingomonas paucimobilis
1.54
-
 purified recombinant wild-type enzyme, substrate 1-iodobutane Sphingomonas paucimobilis
1.57
-
 purified recombinant wild-type enzyme, substrate 1-chlorohexane Sphingomonas paucimobilis
1.61
-
 purified recombinant wild-type enzyme, substrate bromocyclohexane Sphingomonas paucimobilis
1.88
-
 purified recombinant wild-type enzyme, substrate 1-chlorobutane Sphingomonas paucimobilis
2.18
-
 purified recombinant wild-type enzyme, substrate 1,3-diiodopropane Sphingomonas paucimobilis
3.33
-
 purified recombinant wild-type enzyme, substrate 1-bromoobutane Sphingomonas paucimobilis
8.03
-
 purified recombinant wild-type enzyme, substrate 3-chloro-2-methylpropene Sphingomonas paucimobilis
12.3
-
 purified recombinant wild-type enzyme, substrate 1,2-dibromoethane Sphingomonas paucimobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2,3-trichloropropane + H2O
-
 Sphingomonas paucimobilis 2,3-dichloro-1-propanol + chloride
-
 ?
1,2,3-trichloropropane + H2O
-
 Sphingomonas paucimobilis UT26 2,3-dichloro-1-propanol + chloride
-
 ?
1,2-dibromoethane + H2O
-
 Sphingomonas paucimobilis 2-bromoethanol + bromide
-
 ?
1,2-dibromoethane + H2O
-
 Sphingomonas paucimobilis UT26 2-bromoethanol + bromide
-
 ?
1,2-dichloroethane + H2O
-
 Sphingomonas paucimobilis 2-chloroethanol + chloride
-
 ?
1,2-dichloroethane + H2O
-
 Sphingomonas paucimobilis UT26 2-chloroethanol + chloride
-
 ?
1,2-dichloropropane + H2O
-
 Sphingomonas paucimobilis 2-chloropropan-1-ol + chloride
-
 ?
1,2-dichloropropane + H2O
-
 Sphingomonas paucimobilis UT26 2-chloropropan-1-ol + chloride
-
 ?
1,3-diiodopropane + H2O
-
 Sphingomonas paucimobilis 3-iodopropanol + iodide
-
 ?
1-bromobutane + H2O
-
 Sphingomonas paucimobilis n-butanol + bromide
-
 ?
1-chlorobutane + H2O
-
 Sphingomonas paucimobilis n-butanol + chloride
-
 ?
1-chlorohexane + H2O
-
 Sphingomonas paucimobilis n-hexanol + chloride
-
 ?
1-iodobutane + H2O
-
 Sphingomonas paucimobilis n-butanol + iodide
-
 ?
3-chloro-2-methylpropene + H2O
-
 Sphingomonas paucimobilis 2-methylpropene-3-ol + chloride
-
 ?
bromocyclohexane + H2O
-
 Sphingomonas paucimobilis cyclohexanol + bromide
-
 ?
chlorocyclohexane + H2O
-
 Sphingomonas paucimobilis cyclohexanol + chloride
-
 ?
additional information substrate specificity is influenced by the size and shape of their entrance tunnel, surface residue Leu177 is involved and located at the tunnel opening Sphingomonas paucimobilis ?
-
 ?
additional information substrate specificity is influenced by the size and shape of their entrance tunnel, surface residue Leu177 is involved and located at the tunnel opening Sphingomonas paucimobilis UT26 ?
-
 ?

Synonyms

Synonyms Comment Organism
LinB
-
 Sphingomonas paucimobilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Sphingomonas paucimobilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Sphingomonas paucimobilis
1.055
-
 1-Chlorobutane pH 8.6, 37°C, recombinant wild-type enzyme, data from 2 experimental sets Sphingomonas paucimobilis
26.4
-
 1,2-Dibromoethane pH 8.6, 37°C, recombinant wild-type enzyme, data from 2 experimental sets Sphingomonas paucimobilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
 assay at Sphingomonas paucimobilis