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Literature summary extracted from
- Haloalkane dehalogenase catalysed desymmetrisation and tandem kinetic resolution for the preparation of chiral haloalcohols (2012), Tetrahedron, 68, 7645-7650.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.8.1.5 | synthesis | haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols | Bradyrhizobium japonicum |
| 3.8.1.5 | synthesis | haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols | Rhodococcus rhodochrous |
| 3.8.1.5 | synthesis | haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols | Sphingomonas paucimobilis |
| 3.8.1.5 | synthesis | haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols | Mesorhizobium loti |
| 3.8.1.5 | synthesis | haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols | Xanthobacter autotrophicus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.8.1.5 | recombinant expression as N-terminally His-tagged enzyme in Escherichia coli TOP10 | Bradyrhizobium japonicum |
| 3.8.1.5 | recombinant expression as N-terminally His-tagged enzyme in Escherichia coli TOP10 | Rhodococcus rhodochrous |
| 3.8.1.5 | recombinant expression as N-terminally His-tagged enzyme in Escherichia coli TOP10 | Sphingomonas paucimobilis |
| 3.8.1.5 | recombinant expression as N-terminally His-tagged enzyme in Escherichia coli TOP10 | Mesorhizobium loti |
| 3.8.1.5 | recombinant expression as N-terminally His-tagged enzyme in Escherichia coli TOP10 | Xanthobacter autotrophicus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.8.1.5 | additional information | - |
additional information | substrate specificity and kinetics, overview | Bradyrhizobium japonicum | |
| 3.8.1.5 | additional information | - |
additional information | substrate specificity and kinetics, overview | Rhodococcus rhodochrous | |
| 3.8.1.5 | additional information | - |
additional information | substrate specificity and kinetics, overview | Sphingomonas paucimobilis | |
| 3.8.1.5 | additional information | - |
additional information | substrate specificity and kinetics, overview | Mesorhizobium loti | |
| 3.8.1.5 | additional information | - |
additional information | substrate specificity and kinetics, overview | Xanthobacter autotrophicus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.8.1.5 | Bradyrhizobium japonicum | - |
- |
- |
| 3.8.1.5 | Bradyrhizobium japonicum USDA 110 | - |
- |
- |
| 3.8.1.5 | Mesorhizobium loti | - |
- |
- |
| 3.8.1.5 | Mesorhizobium loti MAFF303099 | - |
- |
- |
| 3.8.1.5 | Rhodococcus rhodochrous | - |
- |
- |
| 3.8.1.5 | Rhodococcus rhodochrous NCIMB13064 | - |
- |
- |
| 3.8.1.5 | Sphingomonas paucimobilis | - |
- |
- |
| 3.8.1.5 | Sphingomonas paucimobilis UT26 | - |
- |
- |
| 3.8.1.5 | Xanthobacter autotrophicus | - |
- |
- |
| 3.8.1.5 | Xanthobacter autotrophicus GJ10 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.8.1.5 | recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography | Bradyrhizobium japonicum |
| 3.8.1.5 | recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography | Rhodococcus rhodochrous |
| 3.8.1.5 | recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography | Sphingomonas paucimobilis |
| 3.8.1.5 | recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography | Mesorhizobium loti |
| 3.8.1.5 | recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography | Xanthobacter autotrophicus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.8.1.5 | 1,2,3-tribromopropane + H2O | - |
Rhodococcus rhodochrous | ? | - |
? |  |
| 3.8.1.5 | 1,2,3-tribromopropane + H2O | - |
Rhodococcus rhodochrous NCIMB13064 | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | - |
Bradyrhizobium japonicum | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | - |
Sphingomonas paucimobilis | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | low activity | Xanthobacter autotrophicus | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane | Rhodococcus rhodochrous | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | - |
Bradyrhizobium japonicum USDA 110 | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | - |
Sphingomonas paucimobilis UT26 | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane | Rhodococcus rhodochrous NCIMB13064 | ? | - |
? | |
| 3.8.1.5 | 1,2,3-trichloropropane + H2O | low activity | Xanthobacter autotrophicus GJ10 | ? | - |
? | |
| 3.8.1.5 | 1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O | - |
Sphingomonas paucimobilis | ? | - |
? | |
| 3.8.1.5 | 1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O | - |
Sphingomonas paucimobilis UT26 | ? | - |
? | |
| 3.8.1.5 | 1,3-dibromo-2-methylpropane + H2O | desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol | Bradyrhizobium japonicum | 3-bromo-2-methylpropan-1-ol + bromide | - |
? | |
| 3.8.1.5 | 1,3-dibromo-2-methylpropane + H2O | desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol | Bradyrhizobium japonicum USDA 110 | 3-bromo-2-methylpropan-1-ol + bromide | - |
? | |
| 3.8.1.5 | 1,3-dibromo-2-phenylpropane + H2O | desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol | Sphingomonas paucimobilis | ? | - |
? | |
| 3.8.1.5 | 1,3-dibromo-2-phenylpropane + H2O | desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol | Sphingomonas paucimobilis UT26 | ? | - |
? | |
| 3.8.1.5 | meso-2,3-dibromobutane + H2O | - |
Bradyrhizobium japonicum | ? | - |
? | |
| 3.8.1.5 | meso-2,3-dibromobutane + H2O | - |
Bradyrhizobium japonicum USDA 110 | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview | Bradyrhizobium japonicum | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview | Rhodococcus rhodochrous | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview | Sphingomonas paucimobilis | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,2,3-trichloropropane, 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane | Mesorhizobium loti | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane | Xanthobacter autotrophicus | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview | Bradyrhizobium japonicum USDA 110 | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview | Sphingomonas paucimobilis UT26 | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,2,3-trichloropropane, 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane | Mesorhizobium loti MAFF303099 | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview | Rhodococcus rhodochrous NCIMB13064 | ? | - |
? | |
| 3.8.1.5 | additional information | the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane | Xanthobacter autotrophicus GJ10 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.8.1.5 | DbjA | - |
Bradyrhizobium japonicum |
| 3.8.1.5 | DhaA | - |
Rhodococcus rhodochrous |
| 3.8.1.5 | DhaA31 | - |
Rhodococcus rhodochrous |
| 3.8.1.5 | DhlA | - |
Xanthobacter autotrophicus |
| 3.8.1.5 | dmlA | - |
Mesorhizobium loti |
| 3.8.1.5 | LinB | - |
Sphingomonas paucimobilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.8.1.5 | 30 | - |
assay at | Bradyrhizobium japonicum |
| 3.8.1.5 | 30 | - |
assay at | Rhodococcus rhodochrous |
| 3.8.1.5 | 30 | - |
assay at | Sphingomonas paucimobilis |
| 3.8.1.5 | 30 | - |
assay at | Mesorhizobium loti |
| 3.8.1.5 | 30 | - |
assay at | Xanthobacter autotrophicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.8.1.5 | 8.2 | - |
assay at | Bradyrhizobium japonicum |
| 3.8.1.5 | 8.2 | - |
assay at | Rhodococcus rhodochrous |
| 3.8.1.5 | 8.2 | - |
assay at | Sphingomonas paucimobilis |
| 3.8.1.5 | 8.2 | - |
assay at | Mesorhizobium loti |
| 3.8.1.5 | 8.2 | - |
assay at | Xanthobacter autotrophicus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.8.1.5 | malfunction | DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane | Rhodococcus rhodochrous |
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