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Enzyme Nomenclature
Information on EC 3.8.1.5 - haloalkane dehalogenase
for references in articles please use BRENDA:EC3.8.1.5
Word Map on EC 3.8.1.5
- 3.8.1.5
- xanthobacter
- autotrophicus
-
dehalogenation
- 1,2-dichloroethane
- halide
- 1,2-dibromoethane
- paucimobilis
-
carbon-halogen
- sphingomonas
- rhodochrous
- 1,2,3-trichloropropane
- synthesis
-
alkyl-enzyme
- environmental protection
- hexachlorocyclohexane
- sphingobium
-
haloacid
- 1-chlorobutane
- 2-chloroethanol
- 1,3-dibromopropane
- epichlorohydrine
- gamma-hexachlorocyclohexane
- biotechnology
-
alpha/beta-hydrolase
-
halide-binding
-
haloalcohols
-
beta-hch
- agriculture
- dehydrochlorinase
- degradation
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.8.1.5
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RECOMMENDED NAME
GeneOntology No.
haloalkane dehalogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-haloalkane + H2O = a primary alcohol + halide
two-step mechanism involving an ester intermediate covalently bound at Asp124, His 289 is important for hydrolysis
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1-haloalkane + H2O = a primary alcohol + halide
GJ10, four-step reaction mechanism with covalent ester intermediate
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1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
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1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction
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1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; two-step mechanism involving an ester intermediate covalently bound at Asp124, His 289 is important for hydrolysis
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1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; GJ10, three-step reaction mechanism with covalent alkyl-enzyme ester intermediate
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1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; GJ10, four-step reaction mechanism with covalent ester intermediate
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1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; GJ10, detailed reaction mechanism and energetics calculated from computational model
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1-haloalkane + H2O = a primary alcohol + halide
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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
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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
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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
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1-haloalkane + H2O = a primary alcohol + halide
low activity with small, chlorinated alkanes, importance of active site water molecules and reaction products in molecular docking
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1-haloalkane + H2O = a primary alcohol + halide
catalytic nucleophile Asp108, which is the most disordered catalytic residue, catalytic base His272, structure-based reaction mechanism, active site structure, overview; H272 singly protonated at Ndelta1 and D108 in conformation A give the most exothermic reactionwith DeltaH of -22 kcal/mol
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1-haloalkane + H2O = a primary alcohol + halide
acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds
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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
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1-haloalkane + H2O = a primary alcohol + halide
hydrogen bond interactions between substrate and the environment are significantly different in aqueous solution and in the enzyme. Structure of the enzyme active site provides a more adequate interaction pattern for the reaction process
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1-haloalkane + H2O = a primary alcohol + halide
catalytic triad consists of D123, H279, D250, with a first halide-stabilizing W124 and a secong stabilizing residue W164. Two-step reaction mechanism
1-haloalkane + H2O = a primary alcohol + halide
activation energy of reaction 59.5 kJ/mol
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1-haloalkane + H2O = a primary alcohol + halide
Asp103, Glu127 and His280 are involved in the catalytic reaction, and two H-bond donating residues, Asn38 and Trp104, are involved in stabilization of a halogen group of the substrate
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1-haloalkane + H2O = a primary alcohol + halide
reaction mechanism, overview. The bromide release is the rate-limiting step of the catalytic cycle, overview
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1-haloalkane + H2O = a primary alcohol + halide
structural basis for its reaction mechanism
1-haloalkane + H2O = a primary alcohol + halide
structural basis for its reaction mechanism
Agrobacterium tumefaciens C58 / ATCC 33970
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1-haloalkane + H2O = a primary alcohol + halide
Asp103, Glu127 and His280 are involved in the catalytic reaction, and two H-bond donating residues, Asn38 and Trp104, are involved in stabilization of a halogen group of the substrate
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1-haloalkane + H2O = a primary alcohol + halide
catalytic triad consists of D123, H279, D250, with a first halide-stabilizing W124 and a secong stabilizing residue W164. Two-step reaction mechanism
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1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
-
1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
-
1-haloalkane + H2O = a primary alcohol + halide
activation energy of reaction 59.5 kJ/mol
-
-
1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
-
1-haloalkane + H2O = a primary alcohol + halide
reaction mechanism, overview. The bromide release is the rate-limiting step of the catalytic cycle, overview
-
-
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; alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; catalytic nucleophile Asp108, which is the most disordered catalytic residue, catalytic base His272, structure-based reaction mechanism, active site structure, overview; H272 singly protonated at Ndelta1 and D108 in conformation A give the most exothermic reactionwith DeltaH of -22 kcal/mol; low activity with small, chlorinated alkanes, importance of active site water molecules and reaction products in molecular docking; substrate specificity is influenced by the size and shape of their entrance tunnel, surface residue Leu177 is involved and located at the tunnel opening
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1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction; GJ10, four-step reaction mechanism with covalent ester intermediate; GJ10, four-step reaction mechanism with covalent ester intermediate; two-step mechanism involving an ester intermediate covalently bound at Asp124, His 289 is important for hydrolysis; two-step mechanism involving an ester intermediate covalently bound at Asp124, His 289 is important for hydrolysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-halide hydrolysis
hydrolysis of C-halide
hydrolysis of C-halide
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
1-haloalkane halidohydrolase
Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.
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CAS REGISTRY NUMBER
COMMENTARY
95990-29-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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Agrobacterium tumefaciens C58 / ATCC 33970
isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from contaminated sites in Africa, growth on 1,2-dichloroethane as sole carbon source
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isolated from contaminated sites in Africa, growth on 1,2-dichloroethane as sole carbon source
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from contaminated sites in Africa, growth on 1,2-dichloroethane as sole carbon source
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from mangrove soil from two sites in the same mangrove separated by a small stream affected by oil contamination (petroleum), Brazil
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isolated from contaminated sites in Africa, growth on 1,2-dichloroethane as sole carbon source
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derived from a vinylchloride contaminated site, using vinylchloride as the sole carbon and energy source for enrichment and isolation, gene dmrA
UniProt
derived from a vinylchloride contaminated site, using vinylchloride as the sole carbon and energy source for enrichment and isolation, gene dmrB
UniProt
derived from a vinylchloride contaminated site, using vinylchloride as the sole carbon and energy source for enrichment and isolation, gene dmrA
UniProt
derived from a vinylchloride contaminated site, using vinylchloride as the sole carbon and energy source for enrichment and isolation, gene dmrB
UniProt
isolated from contaminated sites in Africa, growth on 1,2-dichloroethane as sole carbon source
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induction by growth in minimal salt medium and by addition of up to 0.05% 1-chlorobutane to medium; lyophilized cells
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SwissProt
GJ10
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GJ10
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
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DpcA is a member of the haloalkane dehalogenase family
evolution
DppA is a member of the haloalkane dehalogenase subfamily HLD-I
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
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the haloalkane dehalogenases form a subclass of enzymes in the alpha/beta-hydrolase fold superfamily
evolution
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DmmA belongs to the haloalkane dehalogenase family, subfamily-II, structure comparisons, overview
evolution
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the enzyme belongs to the superfamily of alpha/beta-hydrolases
evolution
haloalkane dehalogenase DatA from Agrobacterium tumefaciens strain C58 belongs to the HLD-II subfamily. Enzyme DatA possesses a unique Asn-Tyr pair instead of the Asn-Trp pair conserved among the subfamily members, which keeps the released halide ion stable
evolution
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the enzyme belongs to the alpha/beta hydrolase fold family
evolution
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the enzyme belongs to the alpha/beta hydrolase fold family
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs. Q293 is the single amino acid difference with enzyme DmtA from Mycobacterium tuberculosis strain H37Rv; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs. R293 is the single amino acid difference with enzyme DmbA from Mycobacterium bovis strain 5033/66
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
P51698;
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme possesses a unique halide-stabilizing tyrosine residue, Y109, in place of the conventional tryptophan. Enzyme DatA is unique in stabilizing its substrate in the active site using only a single hydrogen bond, which is a distinct paradigm in catalysis by this enzyme family
evolution
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the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
evolution
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the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
evolution
the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs; the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs. The major structural difference between DmrA (HLD subfamily I) and the well-studied enzymes of HLD subfamily II is the different arrangement of helices in the cap domain
evolution
enzyme DadB likely belongs to the HLD-II subfamily, closely related with LinB and DmbA, while DadA appears to be relatively independent from the HLD-II subfamily. This pentad includes the nucleophile residue D108, the basic residue H271, the acid catalytic residue E132, and the halide-binding residues N37 and W109. DadB possesses a large main tunnel opening, but it prefers small substrates
evolution
the enzyme belongs to the alpha/beta hydrolase family with a catalytic triad composed of Asp-His-Asp in its active site
evolution
Agrobacterium tumefaciens C58 / ATCC 33970
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comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; haloalkane dehalogenase DatA from Agrobacterium tumefaciens strain C58 belongs to the HLD-II subfamily. Enzyme DatA possesses a unique Asn-Tyr pair instead of the Asn-Trp pair conserved among the subfamily members, which keeps the released halide ion stable; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs; the enzyme possesses a unique halide-stabilizing tyrosine residue, Y109, in place of the conventional tryptophan. Enzyme DatA is unique in stabilizing its substrate in the active site using only a single hydrogen bond, which is a distinct paradigm in catalysis by this enzyme family
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evolution
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enzyme DadB likely belongs to the HLD-II subfamily, closely related with LinB and DmbA, while DadA appears to be relatively independent from the HLD-II subfamily. This pentad includes the nucleophile residue D108, the basic residue H271, the acid catalytic residue E132, and the halide-binding residues N37 and W109. DadB possesses a large main tunnel opening, but it prefers small substrates; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
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evolution
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the enzyme belongs to the alpha/beta hydrolase family with a catalytic triad composed of Asp-His-Asp in its active site
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evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
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evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
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evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
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evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs. Q293 is the single amino acid difference with enzyme DmtA from Mycobacterium tuberculosis strain H37Rv; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
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evolution
-
the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs; the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs. The major structural difference between DmrA (HLD subfamily I) and the well-studied enzymes of HLD subfamily II is the different arrangement of helices in the cap domain
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evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
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evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs. R293 is the single amino acid difference with enzyme DmbA from Mycobacterium bovis strain 5033/66
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evolution
-
DpcA is a member of the haloalkane dehalogenase family; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs; the enzyme belongs to the superfamily of alpha/beta-hydrolases
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evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs; the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs; the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview; the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
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malfunction
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the single mutation in a tunnel to the active site changes the mechanism and kinetics of product release in LinB. Interactions of the bromide ion with the tryptophan increase free energy barrier for its passage, causing the reaction mechanism change
malfunction
-
DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
malfunction
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DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
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malfunction
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the single mutation in a tunnel to the active site changes the mechanism and kinetics of product release in LinB. Interactions of the bromide ion with the tryptophan increase free energy barrier for its passage, causing the reaction mechanism change
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physiological function
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haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds
physiological function
-
haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds
physiological function
the enzyme is involved in 1,2-dichloroethane degradation
physiological function
-
the enzyme is involved in 1-haloalkanes degradation
physiological function
P51698;
the enzyme is involved in gamma-HCH degradation
physiological function
-
the enzyme is involved in 1,2-dichloroethane degradation
physiological function
haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources; haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources
physiological function
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the enzyme is involved in 1,2-dichloroethane degradation
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physiological function
-
haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources; haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources
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physiological function
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the enzyme is involved in 1-haloalkanes degradation
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physiological function
-
the enzyme is involved in gamma-HCH degradation
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physiological function
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the enzyme is involved in 1,2-dichloroethane degradation
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additional information
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DatA possesses a unique pair of halide-stabilizing residues, Asn-Tyr, not reported in other known haloalkane dehalogenases
additional information
active site residues are Asp123, His278, and Asp249, and Trp124 and Trp163 as halide-stabilizing residues, and a catalytic triad Asp-His-Asp
additional information
-
the active site is formed by a pentad consisting of halide-stabilizing Asn78 and Trp145, nucleophile Asp144, base His315, and acid Glu168. DmmA possesses a larg active site binding pocket allowing to accept a range of linear and cyclic substrates including include chlorinated, brominated, and iodinated alkanes of varying length, structure, overview
additional information
docking models of enzyme DatA complexed with 1,3-dibromopropane and 2-bromohexane, the docking pose shows the highest score for each enantiomer of 2-bromohexane, only the (R)-form of 2-bromohexane can be in a near-attack conformation for the SN2 reaction. Location of the active site, and overall structure of the wild-type DatA, overview
additional information
-
the enzyme has a core domain bearing the catalytic triad of Asp-His-Asp/Glu and a variable, mostly helical cap domain, which provides essential residues to stabilize the transition state, bind substrates and products and determine the selectivity. The essential residues D106 (nucleophile) and H272 (base) are involved in the catalytic mechanism of DhaA
additional information
-
the enzyme has a core domain bearing the catalytic triad of Asp-His-Asp/Glu and a variable, mostly helical cap domain, which provides essential residues to stabilize the transition state, bind substrates and products and determine the selectivity. The essential residues D124 (nucleophile) and H289 (base) are involved in the catalytic mechanism of DhlA
additional information
-
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
additional information
-
the active sites of Han enzymes are characterised by a catalytic pentad. This consists of a catalytic triad and a stabilizing pair of residues. The catalytic triad consists of Asp106 (located between beta-strand 5 and alpha-helix 2), His271 (located between beta-strand 8 and 310 helix 9) and Glu130 (located within beta-strand 6). The side chains of Trp107 and Asn36 bind the substrate halogen, while their main chain nitrogen atoms form the oxyanion hole. The HLD active site is built up of an entrance tunnel and a hydrophobic pocket for substrate binding. The residues lining the substrate pocket mainly belong to the cap domain and define substrate specificity. Minor differences in the substrate pocket can dramatically affect the substrate specificity of very similar HLDs
additional information
-
enzyme ligand docking and molecular dynamics simulations, structure comparisons of wild-type and mutant enzymes, effects of different residues located near the active site on the specificity constants, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
DadB has an open active cavity with a large access tunnel, which is supposed important for larger molecules as opposed to C2-C3 substrates, homology modeling, residue I247 plays an important role in substrate selection. Homology modeling and structural analysis, overview. Enzyme DadB is composed of a core domain and a cap domain, identical catalytic pentad of HLD-II subfamily
additional information
-
three-dimensional enzyme structure analysis modeling
additional information
three-dimensional enzyme structure analysis modeling
additional information
Agrobacterium tumefaciens C58 / ATCC 33970
-
DatA possesses a unique pair of halide-stabilizing residues, Asn-Tyr, not reported in other known haloalkane dehalogenases; docking models of enzyme DatA complexed with 1,3-dibromopropane and 2-bromohexane, the docking pose shows the highest score for each enantiomer of 2-bromohexane, only the (R)-form of 2-bromohexane can be in a near-attack conformation for the SN2 reaction. Location of the active site, and overall structure of the wild-type DatA, overview
-
additional information
-
DadB has an open active cavity with a large access tunnel, which is supposed important for larger molecules as opposed to C2-C3 substrates, homology modeling, residue I247 plays an important role in substrate selection. Homology modeling and structural analysis, overview. Enzyme DadB is composed of a core domain and a cap domain, identical catalytic pentad of HLD-II subfamily
-
additional information
-
three-dimensional enzyme structure analysis modeling
-
additional information
-
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
-
additional information
-
enzyme ligand docking and molecular dynamics simulations, structure comparisons of wild-type and mutant enzymes, effects of different residues located near the active site on the specificity constants, overview
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + H2O
cis-2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
(RS)-3-chloropropane-1,2-diol + NAD+
(R)-3-chloropropane-1,2-diol + 2-oxo-propionaldehyde + CH3COOH + Cl- + HCOOH + NADH
-
-
-
-
-
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol
-
prefered formation of R-enantiomer due to a specific interaction of substrate with residue N41
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropanol + chloride
-
-
-
?
1,2,3-trichloropropene + H2O
2,3-dichloropropenol + chloride
-
-
-
?
1,2-dibromopropane + H2O
2-bromopropan-1-ol + bromide
-
-
-
?
1,2-dichlorobutane + H2O
?
-
7.8% of the activity with 4-chlorobutanol
-
-
?
1,2-dichloropropane + H2O
2-chloropropanol + chloride
-
-
-
?
1,3,4,6-tetrachloro-1,4,cyclohexadiene + 2 H2O
2,5-dichloro-2,5-cyclohexadiene-1,4-diol + 2 chloride
1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O
2,4,5-trichloro-2,5-cyclohexadiene-1-ol + chloride
-
-
-
?
1,3-dichlorobutane + H2O
?
-
12% of the activity with 4-chlorobutanol
-
-
?
1,3-dichloropropane + H2O
3-chloropropan-1-ol + chloride
-
-
-
?
1,3-dichloropropene + H2O
3-chloropropenol + chloride
-
-
-
?
1,4-dichlorobutane + H2O
?
-
27% of the activity with 4-chlorobutanol
-
-
?
1,5-dichloropentane + H2O
?
-
20% of the activity with 4-chlorobutanol
-
-
?
1,6-dibromohexane + H2O
6-bromohexane + bromide
-
low activity
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
-
-
-
?
1,6-dichlorohexane + H2O
6-chlorohexane + bromide
-
low activity
-
-
?
1,6-dichlorohexane + H2O
?
-
32% of the activity with 4-chlorobutanol
-
-
?
1,6-diiodohexane + H2O
6-iodohexane + iodide
-
low activity
-
-
?
1,7-dichloroheptane + H2O
?
-
20% of the activity with 4-chlorobutanol
-
-
?
1,8-dichlorooctane + H2O
?
-
32% of the activity with 4-chlorobutanol
-
-
?
1,9-dichlorononane + H2O
?
-
14% of the activity with 4-chlorobutanol
-
-
?
1-bromo-2-chloroethane + H2O
1-bromo-2-ethanol + chloride
-
low activity
-
-
?
1-bromo-2-chloroethane + H2O
?
-
76% of the activity with 1,2-dichloroethane
-
-
?
1-chloro-2-(2-chloroethoxy)ethane + H2O
2-(2-chloroethoxy)ethanol + chloride
-
-
-
?
1-chloro-2-bromoethane + H2O
2-bromoethanol + chloride
-
-
-
-
?
1-chloro-2-fluoroethane + H2O
?
-
no release of fluoride, 25% of the activity with 1,2-dichloroethane
-
-
?
1-chloro-4-methylbutane + H2O
pentanol + chloride
-
42% of the activity with 4-chlorobutanol
-
-
?
1-chlorononane + H2O
nonanol + chloride
-
13% of the activity with 4-chlorobutanol
-
-
?
2,3,4,5,6-pentachlorocyclohexanol + H2O
2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
2-bromoacetamide + H2O
acetamide + bromide
poor substrate
-
-
?
2-chloroacetamide + H2O
acetamide + chloride
poor substrate
-
-
?
2-chloroacetonitrile + H2O
acetonitrile + chloride
-
-
-
?
2-chloroethanol + H2O
ethanol + chloride
very poor substrate
-
-
?
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + H2O
2,5,6-trichloro-2-cyclohexene-1,4-diol + chloride
3-chloro-2-(chloromethyl)-1-propene + H2O
2-chloromethyl-2-propen-1-ol + Cl-
-
-
-
-
?
3-chloro-2-methylpropene + H2O
2-methylpropene + chloride
-
-
-
-
?
3-chloropropene + H2O
propenol + chloride
-
45% of the activity with 1,2-dichloroethane
-
-
?
4-chlorobutanol + H2O
butane-1,4-diol + chloride
-
highest activity
-
-
?
bromochloromethane + H2O
?
-
99% of the activity with 1,2-dichloroethane
-
-
?
delta-hexachlorocyclohexane + H2O
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
delta-pentachlorocyclohexene + H2O
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + chloride
-
-
-
-
?
dichloromethane + H2O
chloromethanol + chloride
poor substrate
-
-
?
epsilon-hexachlorocyclohexane + H2O
pentachlorocyclohexanol + tetrachlorocyclohexane-1,4-diol + chloride
gamma-pentachlorocyclohexene + H2O
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + 2,5,6-trichloro-2-cyclohexene-1,4-diol + chloride
-
-
-
-
?
pentachlorocyclohexanol + H2O
tetrachlorocyclohexanediol + chloride
-
-
-
-
?
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + H2O
cis-2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
-
?
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + H2O
cis-2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
-
?
(bromomethyl)cyclohexane + H2O
cyclohexylmethanol + bromide
-
-
-
?
(bromomethyl)cyclohexane + H2O
cyclohexylmethanol + bromide
-
-
-
-
?
1,1,2,3,4,5,6-heptachlorocyclohexane + H2O
2,3,4,4,5,6-hexachlorocyclohexanol + chloride
-
-
-
-
?
1,1,2,3,4,5,6-heptachlorocyclohexane + H2O
2,3,4,4,5,6-hexachlorocyclohexanol + chloride
-
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
-
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
-
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
-
high activity
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
-
-
-
?
1,2,3-trichloropropane + H2O
(RS)-2,3-dichloropropan-1-ol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
(RS)-2,3-dichloropropan-1-ol + chloride
-
structural model of DhaA31 with TCP docked in the active site, comparison with DhaA31 mutant enzyme docking models, overview. The pentad is made up of an Asp-His-Asp catalytic triad and a Trp-Trp or Trp-Asn diad for halide binding. An aspartate residue acts as the nucleophile to displace a halide ion from the substrate. By hydrolysis of the resulting covalent alkyl-enzyme intermediate, alcohol is released
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
low activity
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
low activity
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
-
substrate, but not the product, adsorbs with high affinity onto the polyethylenimine impregnated gamma-alumina support used for enzyme immobilization
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,2,3-trichloropropane + H2O
?
-
substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
-
-
?
1,2,3-trichloropropane + H2O
?
-
substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
-
high activity
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
-
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
Agrobacterium tumefaciens C58 / ATCC 33970
-
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
1100% of the activity with 1-chlorobutane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
1100% of the activity with 1-chlorobutane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
42% of the activity with 4-chlorobutanol
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
P51698;
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
94% of the activity with 1,2-dichloroethane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
78% of the activity with 1,2-dichloroethane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
low activity
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
low activity
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
-
high activity
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
-
-
-
?
1,2-dichloroethane + H2O
1,2-ethanediol + chloride
-
-
-
?
1,2-dichloroethane + H2O
1,2-ethanediol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethane + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
highest activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
analysis of dynamic and electrostatic effects
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
highest activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
low activity
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
low activity
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
-
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
-
-
?
1,3,4,6-tetrachloro-1,4,cyclohexadiene + 2 H2O
2,5-dichloro-2,5-cyclohexadiene-1,4-diol + 2 chloride
-
-
-
-
?
1,3,4,6-tetrachloro-1,4,cyclohexadiene + 2 H2O
2,5-dichloro-2,5-cyclohexadiene-1,4-diol + 2 chloride
-
-
-
-
?
1,3-dibromo-2-methylpropane + H2O
3-bromo-2-methylpropan-1-ol + bromide
-
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
-
-
?
1,3-dibromo-2-methylpropane + H2O
3-bromo-2-methylpropan-1-ol + bromide
-
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
-
-
?
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
-
-
?
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
-
-
?
1,3-dibromo-2-propanol + H2O
3-bromo-1,2-propandiol
-
-
-
-
?
1,3-dibromopropane + H2O
1,3-propanediol + bromide
-
-
-
?
1,3-dibromopropane + H2O
1,3-propanediol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
best substrate, the release of product 3-bromo-1-propanol is the rate limiting step
-
-
?
1,3-dibromopropane + H2O
3-bromo-propanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropane + bromide
-
preferred substrate
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
420% of the activity with 1-chlorobutane
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
700% of the activity with 1-chlorobutane
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
high activity
-
-
?
1,3-dichloropropane + H2O
3-chloropropanol + chloride
-
-
-
?
1,3-dichloropropane + H2O
?
-
21% of the activity with 4-chlorobutanol
-
-
?
1,3-dichloropropane + H2O
?
-
21% of the activity with 4-chlorobutanol
-
-
?
1,3-dichloropropane + H2O
?
-
80% of the activity with 1,2-dichloroethane
-
-
?
1,5-dichloropentane + H2O
5-chloro-1-pentanol + chloride
-
low activity
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
high activity
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
-
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
high activity
-
-
?
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
-
-
-
?
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
-
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
best substrate
-
-
?
1-bromobutane + H2O
1-butanol + bromide
best substrate
-
-
?
1-bromobutane + H2O
1-butanol + bromide
preferred substrate
-
-
?
1-bromobutane + H2O
butanol + bromide
-
25% of the activity with 4-chlorobutanol
-
-
?
1-bromobutane + H2O
butanol + bromide
-
reaction in aqueous phase, 98% of the activity with 1-chlorobutane, reaction in gaseous phase, 98% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
butanol + bromide
-
reaction in aqueous phase, 98% of the activity with 1-chlorobutane, reaction in gaseous phase, 98% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
180% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
180% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
630% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
630% of the activity with 1-chlorobutane
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
best substrate
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
best substrate
-
-
?
1-bromohexane + H2O
hexanol + bromide
-
reaction in aqueous phase, 87% of the activity with 1-chlorobutane, reaction in gaseous phase, 301% of the activity with 1-chlorobutane
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
low activity
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
low activity
-
-
?
1-bromopropane + H2O
propanol + bromide
-
29% of the activity with 1,2-dichloroethane
-
-
?
1-chloro-2,2-dimethylpropane + H2O
2,2-dimethylpropan-1-ol + chloride
-
-
-
-
?
1-chloro-2,2-dimethylpropane + H2O
2,2-dimethylpropan-1-ol + chloride
-
-
-
-
?
1-chloro-2-methylpropane + H2O
2-methylpropanol + chloride
-
-
-
?
1-chloro-2-methylpropane + H2O
2-methylpropanol + chloride
-
20% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
22% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
22% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
31% of the activity with 1,2-dichloroethane
-
-
?
1-chlorodecane + H2O
n-decanol + chloride
-
52% of the activity with 1-chlorobutane
-
-
?
1-chlorodecane + H2O
n-decanol + chloride
-
110% of the activity with 1-chlorobutane
-
-
?
1-chloroheptane + H2O
heptanol + chloride
-
22% of the activity with 4-chlorobutanol
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
15% of the activity with 4-chlorobutanol
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
reaction in aqueous phase, 100% of the activity with 1-chlorobutane, reaction in gaseous phase, 194% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
reaction in aqueous phase, 100% of the activity with 1-chlorobutane, reaction in gaseous phase, 194% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
best substrate
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
210% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
210% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
110% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
110% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
low activity
-
-
?
1-chlorooctane + H2O
octanol + chloride
-
18% of the activity with 4-chlorobutanol
-
-
?
1-chloropentane + H2O
n-pentanol + chloride
-
140% of the activity with 1-chlorobutane
-
-
?
1-chloropentane + H2O
n-pentanol + chloride
-
120% of the activity with 1-chlorobutane
-
-
?
1-chloropentane + H2O
pentanol + chloride
-
20% of the activity with 4-chlorobutanol
-
-
?
1-chloropentane + H2O
pentanol + chloride
-
reaction in aqueous phase, 101% of the activity with 1-chlorobutane, reaction in gaseous phase, 186% of the activity with 1-chlorobutane
-
-
?
1-chloropentane + H2O
pentanol + chloride
-
reaction in aqueous phase, 101% of the activity with 1-chlorobutane, reaction in gaseous phase, 186% of the activity with 1-chlorobutane
-
-
?
1-chloropropane + H2O
propanol + chloride
-
5% of the activity with 4-chlorobutanol
-
-