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Literature summary for 3.8.1.5 extracted from

  • Guan, L.; Yabuki, H.; Okai, M.; Ohtsuka, J.; Tanokura, M.
    Crystal structure of the novel haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 reveals a special halide-stabilizing pair and enantioselectivity mechanism (2014), Appl. Microbiol. Biotechnol., 98, 8573-8582.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of wild-tye and mutant enzymes in Escherichia coli strain Rosetta (DE3) Agrobacterium tumefaciens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified wild-type and mutant Y109W enzymes, sitting drop vapor diffusion method, mixing of 10 mg/mL protein in 10 mM Tris-HCl, pH 8.0, and 1 mM DTT with an equal volume of reservoir solution containing 0.1 M CHES, pH 8.6, 1.0 M potassium sodium tartrate, 0.2 M lithium sulfate, 0.01 M barium chloride, 20°C X-ray diffraction structure determination and analysis at 1.70 A and 1.95 A resolution, respectively, molecular replacement method using the crystal structure of Rv2579 from Mycobacterium tuberculosis, PDB ID 2qvb Agrobacterium tumefaciens

Protein Variants

Protein Variants Comment Organism
Y109W site-directed mutagenesis, crystal structure determination Agrobacterium tumefaciens

Inhibitors

Inhibitors Comment Organism Structure
N-cyclohexyl-2-aminoethanesulfonic acid CHES, competitive inhibition, CHES binds to the active site of DatA, the sulfate moiety of CHES is bound by Asn43, and the other parts are bound by Asp108 and His274 of the catalytic triad Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Agrobacterium tumefaciens enzyme DatA hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton ?
-
?
additional information Agrobacterium tumefaciens C58 / ATCC 33970 enzyme DatA hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton ?
-
?

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens E2RV69
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-
Agrobacterium tumefaciens C58 / ATCC 33970 E2RV69
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-tye and mutant enzymes from Escherichia coli strain Rosetta (DE3) Agrobacterium tumefaciens

Reaction

Reaction Comment Organism Reaction ID
1-haloalkane + H2O = a primary alcohol + halide structural basis for its reaction mechanism Agrobacterium tumefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,3-dibromopropane + H2O
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Agrobacterium tumefaciens 3-bromopropanol + bromide
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?
1,3-dibromopropane + H2O
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Agrobacterium tumefaciens C58 / ATCC 33970 3-bromopropanol + bromide
-
?
additional information enzyme DatA hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton Agrobacterium tumefaciens ?
-
?
additional information enzyme DatA hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton Agrobacterium tumefaciens C58 / ATCC 33970 ?
-
?

Synonyms

Synonyms Comment Organism
DatA
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Agrobacterium tumefaciens
HLD
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Agrobacterium tumefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Agrobacterium tumefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
95
-
purified recombinant enzyme, 5 min, inactivation Agrobacterium tumefaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Agrobacterium tumefaciens

General Information

General Information Comment Organism
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 Agrobacterium tumefaciens
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 Agrobacterium tumefaciens