3.8.1.5: haloalkane dehalogenase
This is an abbreviated version!
For detailed information about haloalkane dehalogenase, go to the full flat file.
Word Map on EC 3.8.1.5
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3.8.1.5
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xanthobacter
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autotrophicus
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dehalogenation
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1,2-dichloroethane
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halide
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carbon-halogen
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1,2-dibromoethane
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sphingomonas
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paucimobilis
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1,2,3-trichloropropane
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synthesis
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hexachlorocyclohexane
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rhodochrous
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sphingobium
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environmental protection
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alkyl-enzyme
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haloacid
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1-chlorobutane
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2-chloroethanol
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ncimb
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chloroalkane
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dehydrochlorinase
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epichlorohydrine
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gamma-hexachlorocyclohexane
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halotag
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biotechnology
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alpha/beta-hydrolase
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haloalcohols
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agriculture
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halide-binding
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degradation
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industry
- 3.8.1.5
- xanthobacter
- autotrophicus
-
dehalogenation
- 1,2-dichloroethane
- halide
-
carbon-halogen
- 1,2-dibromoethane
- sphingomonas
- paucimobilis
- 1,2,3-trichloropropane
- synthesis
- hexachlorocyclohexane
- rhodochrous
- sphingobium
- environmental protection
-
alkyl-enzyme
-
haloacid
- 1-chlorobutane
- 2-chloroethanol
-
ncimb
-
chloroalkane
- dehydrochlorinase
- epichlorohydrine
- gamma-hexachlorocyclohexane
-
halotag
- biotechnology
-
alpha/beta-hydrolase
- haloalcohols
- agriculture
-
halide-binding
- degradation
- industry
Reaction
Synonyms
1,3,4,6,-tetrachloro-1,4-cyclohexadiene halidohydrolase, 1-chlorohexane halidohydrolase, 1-haloalkane dehalogenase, DadB, DatA, DbeA, DbjA, DccA, DhaA, DhaA31, DhaB, DhaC, DhAf, DhlA, DhmA, DmaA, dmbA, DmbB, DmbC, dmlA, DmmA, DmrA, DmrB, DmsA, DmtA, DmxA, DpcA, DppA, DrbA, DsaA, DspA, EC 3.8.1.1, eHLD-B, eHLD-C, haloalkane dehalogenase, haloalkane dehalogenase LinB, HanR, HLD, HLD-I, LinB, LinBMI, LinBUT, metallo-haloalkane dehalogenase, protein XP_504164, Rv2579, Ylehd
ECTree
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General Information
General Information on EC 3.8.1.5 - haloalkane dehalogenase
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evolution
malfunction
physiological function
additional information
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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
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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DmmA belongs to the haloalkane dehalogenase family, subfamily-II, structure comparisons, overview
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
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the haloalkane dehalogenases form a subclass of enzymes in the alpha/beta-hydrolase fold superfamily
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
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
the enzyme belongs to the alpha/beta hydrolase family with a catalytic triad composed of Asp-His-Asp in its active site
evolution
the enzyme belongs to the alpha/beta hydrolase fold family
evolution
the enzyme belongs to the alpha/beta hydrolase fold family
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 belongs to the alpha/beta-hydrolase superfamily
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 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 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 II 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
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 II of HLDs. Q293 is the single amino acid difference with enzyme DmtA from Mycobacterium tuberculosis strain H37Rv
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 III of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
evolution
-
the enzyme belongs to the superfamily of alpha/beta-hydrolases
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
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 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
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
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
-
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
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
-
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
-
DpcA is a member of the haloalkane dehalogenase family
-
evolution
-
the enzyme belongs to the superfamily of alpha/beta-hydrolases
-
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 family with a catalytic triad composed of Asp-His-Asp in its active site
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
Agrobacterium tumefaciens C58 / ATCC 33970
-
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
Agrobacterium tumefaciens C58 / ATCC 33970
-
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
Agrobacterium tumefaciens C58 / ATCC 33970
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
Agrobacterium tumefaciens C58 / ATCC 33970
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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 superfamily, subgroup II of HLDs
-
evolution
-
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
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
-
evolution
-
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
-
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
-
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
-
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 I of HLDs
-
evolution
-
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
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
-
DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
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
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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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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
haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources
physiological function
the enzyme is involved in 1,2-dichloroethane degradation
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
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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-haloalkanes degradation
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physiological function
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the enzyme is involved in 1,2-dichloroethane degradation
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physiological function
-
the enzyme is involved in 1,2-dichloroethane degradation
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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
DatA possesses a unique pair of halide-stabilizing residues, Asn-Tyr, not reported in other known haloalkane dehalogenases
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
-
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
-
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
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
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
-
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
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
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the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
additional information
P51698
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
additional information
three-dimensional enzyme structure analysis modeling
additional information
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three-dimensional enzyme structure analysis modeling
additional information
-
three-dimensional enzyme structure analysis modeling
-
additional information
Agrobacterium tumefaciens C58 / ATCC 33970
-
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
Agrobacterium tumefaciens C58 / ATCC 33970
-
DatA possesses a unique pair of halide-stabilizing residues, Asn-Tyr, not reported in other known haloalkane dehalogenases
-
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
-
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
-
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
-