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Literature summary for 3.8.1.5 extracted from

  • Fibinger, M.P.; Davids, T.; Boettcher, D.; Bornscheuer, U.T.
    A selection assay for haloalkane dehalogenase activity based on toxic substrates (2015), Appl. Microbiol. Biotechnol., 99, 8955-8962.
    View publication on PubMed
Search for more literature for 3.8.1.5

Cloned(Commentary)

Cloned (Comment) Organism
gene dhaA, expression of a saturation mutagenesis library in Escherichia coli strain BL21(DE3) Rhodococcus rhodochrous
gene dhlA, expression of a saturation mutagenesis library in Escherichia coli strain BL21(DE3) Xanthobacter autotrophicus

Protein Variants

Protein Variants Comment Organism
D106A site-directed mutagenesis, inactive mutant Rhodococcus rhodochrous
D106A/H272A site-directed mutagenesis, inactive mutant Rhodococcus rhodochrous
D124A site-directed mutagenesis, inactive mutant Xanthobacter autotrophicus
D124A/H289A site-directed mutagenesis, inactive mutant Xanthobacter autotrophicus
H271A site-directed mutagenesis, inactive mutant Rhodococcus rhodochrous
H289A site-directed mutagenesis, inactive mutant Xanthobacter autotrophicus
additional information development and evaluation of a high-throughput system to select active haloalkane dehalogenase variants from a large mutant library, enrichment of the active wild-type enzyme in contrast to the inactive variants is about 340fold. Three saturation libraries, with a size of more than 106 cells, based on inactive variants of the haloalkane dehalogenases DhaA are successfully screened to retrieve active enzymes Rhodococcus rhodochrous
additional information development and evaluation of a high-throughput system to select active haloalkane dehalogenase variants from a large mutant library, enrichment of the active wild-type enzyme in contrast to the inactive variants is about 340fold. Three saturation libraries, with a size of more than 106 cells, based on inactive variants of the haloalkane dehalogenases DhlA are successfully screened to retrieve active enzymes Xanthobacter autotrophicus

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous P0A3G2 gene dhaA
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Xanthobacter autotrophicus P22643 gene dhlA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information development and evaluation of a high-throughput system to select active haloalkane dehalogenase variants from a large mutant library, enrichment of the active wild-type enzyme in contrast to the inactive variants is about 340fold Xanthobacter autotrophicus ?
-
 ?
additional information development and evaluation of a high-throughput system to select active haloalkane dehalogenase variants from a large mutant library, enrichment of the active wild-type enzyme in contrast to the inactive variants is about 340fold Rhodococcus rhodochrous ?
-
 ?

Synonyms

Synonyms Comment Organism
DhaA
-
 Rhodococcus rhodochrous
DhlA
-
 Xanthobacter autotrophicus
HLD
-
 Xanthobacter autotrophicus
HLD
-
 Rhodococcus rhodochrous

General Information

General Information Comment Organism
evolution the enzyme belongs to the alpha/beta hydrolase fold family Xanthobacter autotrophicus
evolution the enzyme belongs to the alpha/beta hydrolase fold family Rhodococcus rhodochrous
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 Rhodococcus rhodochrous
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 Xanthobacter autotrophicus
physiological function haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds Xanthobacter autotrophicus
physiological function haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds Rhodococcus rhodochrous