Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.8.1.5 D106A site-directed mutagenesis, inactive mutant Rhodococcus rhodochrous
3.8.1.5 D106A/H272A site-directed mutagenesis, inactive mutant Rhodococcus rhodochrous
3.8.1.5 D124A site-directed mutagenesis, inactive mutant Xanthobacter autotrophicus
3.8.1.5 D124A/H289A site-directed mutagenesis, inactive mutant Xanthobacter autotrophicus
3.8.1.5 H271A site-directed mutagenesis, inactive mutant Rhodococcus rhodochrous
3.8.1.5 H289A site-directed mutagenesis, inactive mutant Xanthobacter autotrophicus
3.8.1.5 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
3.8.1.5 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

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.8.1.5 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 ?
-
 ?
3.8.1.5 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

EC Number Synonyms Comment Organism
3.8.1.5 DhaA
-
 Rhodococcus rhodochrous
3.8.1.5 DhlA
-
 Xanthobacter autotrophicus
3.8.1.5 HLD
-
 Xanthobacter autotrophicus
3.8.1.5 HLD
-
 Rhodococcus rhodochrous

General Information

EC Number General Information Comment Organism
3.8.1.5 evolution the enzyme belongs to the alpha/beta hydrolase fold family Xanthobacter autotrophicus
3.8.1.5 evolution the enzyme belongs to the alpha/beta hydrolase fold family Rhodococcus rhodochrous
3.8.1.5 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
3.8.1.5 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
3.8.1.5 physiological function haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds Xanthobacter autotrophicus
3.8.1.5 physiological function haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds Rhodococcus rhodochrous