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

BRENDA support

Literature summary extracted from

  • Nagata, Y.; Ohtsubo, Y.; Tsuda, M.
    Properties and biotechnological applications of natural and engineered haloalkane dehalogenases (2015), Appl. Microbiol. Biotechnol., 99, 9865-9881.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.8.1.5 phylogenetic analysis and tree Corynebacterium sp.
3.8.1.5 phylogenetic analysis and tree Arthrobacter sp.
3.8.1.5 phylogenetic analysis and tree Rhodococcus sp.
3.8.1.5 phylogenetic analysis and tree Strongylocentrotus purpuratus
3.8.1.5 phylogenetic analysis and tree Sphingomonas sp.
3.8.1.5 phylogenetic analysis and tree Mycobacterium tuberculosis variant bovis
3.8.1.5 phylogenetic analysis and tree Sphingobium indicum
3.8.1.5 phylogenetic analysis and tree Xanthobacter autotrophicus
3.8.1.5 phylogenetic analysis and tree Bradyrhizobium japonicum
3.8.1.5 phylogenetic analysis and tree Mesorhizobium loti
3.8.1.5 phylogenetic analysis and tree Sphingobium sp.
3.8.1.5 phylogenetic analysis and tree Mycobacterium tuberculosis
3.8.1.5 phylogenetic analysis and tree Rhodococcus rhodochrous
3.8.1.5 phylogenetic analysis and tree Agrobacterium tumefaciens
3.8.1.5 phylogenetic analysis and tree Plesiocystis pacifica
3.8.1.5 phylogenetic analysis and tree Alcanivorax dieselolei
3.8.1.5 phylogenetic analysis and tree Mycobacterium sp.
3.8.1.5 phylogenetic analysis and tree Bradyrhizobium elkanii
3.8.1.5 phylogenetic analysis and tree Mycobacterium avium
3.8.1.5 phylogenetic analysis and tree Rhodopirellula baltica
3.8.1.5 phylogenetic analysis and tree Marinobacter sp.
3.8.1.5 phylogenetic analysis and tree Psychrobacter cryohalolentis
3.8.1.5 phylogenetic analysis and tree Rhodobacteraceae bacterium UDC319

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.8.1.5 crystal structure determination and analysis Marinobacter sp.
3.8.1.5 crystal structure determination and analysis, PDB ID 1CIJ Xanthobacter autotrophicus
3.8.1.5 crystal structure determination and analysis, PDB ID 1CIJ Rhodobacteraceae bacterium UDC319
3.8.1.5 crystal structure determination and analysis, PDB ID 1CQW Rhodococcus rhodochrous
3.8.1.5 crystal structure determination and analysis, PDB ID 1CV2/2BFN Sphingobium indicum
3.8.1.5 crystal structure determination and analysis, PDB ID 2QVB Mycobacterium tuberculosis
3.8.1.5 crystal structure determination and analysis, PDB ID 2XT0 Plesiocystis pacifica
3.8.1.5 crystal structure determination and analysis, PDB ID 3WI7 for the wild-type and PDB ID 3WIB for the mutant enzyme Agrobacterium tumefaciens
3.8.1.5 crystal structure determination and analysis, PDB ID 4H77 Sphingobium sp.
3.8.1.5 crystal structure determination and analysis, PDB ID 4K2A Bradyrhizobium elkanii
3.8.1.5 crystal structure determination and analysis, PDB IDs 3A2M and 3AFI for te wild-type, and PDB ID 3A2L for the mutant Bradyrhizobium japonicum
3.8.1.5 crystal structure determination and analysis, PDB IDs 4BRZ and 4C6H Psychrobacter cryohalolentis
3.8.1.5 mutant crystal structure determination and analysis, PDB IDs 4FWB and 3SK0 Mycobacterium sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.8.1.5 C176Y/Y273F site-directed mutagenesis, the mutant enzyme is 3.5fold higher activity toward TCP than DhaA wild-type Mycobacterium sp.
3.8.1.5 H139A site-directed mutagenesis Bradyrhizobium japonicum
3.8.1.5 additional information construction of deletion mutant DbeADELTACl, mutation in the second halide-binding site Bradyrhizobium elkanii
3.8.1.5 additional information construction of deletion mutants DbjADELTA and DbjADELTA H139A Bradyrhizobium japonicum
3.8.1.5 additional information construction of engineered enzyme variants: the more thermostable Dhla5/Dhla8, the more active DhaAM2(C176Y/Y273F), the DhaA31 mutant that is 32fold higher activity toward TCP than DhaA wild-type, te mutant DhaA12 mimicking DbjA active (insertion of ERB), and the DhaA31 mutant that has higher enantioselectivity toward TCP than the wild-type Mycobacterium sp.
3.8.1.5 additional information construction of LinB variants, that mimick the DmtA active site, shows higher activity toward beta- and delta-HCH than LinBMI. Mutant 4H7D/4H7E/4H7F/4H7H/4H7I/4H7J/4H7K are intermediates between LinBUT and LinBMI Sphingobium sp.
3.8.1.5 additional information construction of LinBUT variants, 4H7D/4H7E/4H7F/4H7H/4H7I/4H7J/4H7K are intermediates between LinBUT and LinBMI Sphingobium indicum
3.8.1.5 additional information engineered enzyme variants are constructed for in vivo evolution for activity toward 1-chlorohexane, more activity toward 1,6-dichlorohexane than DhlA wild-type, and increased activity toward 1,2-dibromoethane/1-bromobutane the wild-type Xanthobacter autotrophicus
3.8.1.5 Y109W site-directed mutagenesis, mutant DatA01 Agrobacterium tumefaciens

Organism

EC Number Organism UniProt Comment Textmining
3.8.1.5 Agrobacterium tumefaciens E2RV69 gene datA
-
3.8.1.5 Agrobacterium tumefaciens C58 / ATCC 33970 E2RV69 gene datA
-
3.8.1.5 Alcanivorax dieselolei
-
-
-
3.8.1.5 Alcanivorax dieselolei B-5
-
-
-
3.8.1.5 Arthrobacter sp.
-
 gene dhaA
-
3.8.1.5 Bradyrhizobium elkanii E2RV62
-
-
3.8.1.5 Bradyrhizobium elkanii USDA94 E2RV62
-
-
3.8.1.5 Bradyrhizobium japonicum P59337
-
-
3.8.1.5 Bradyrhizobium japonicum USDA 110 P59337
-
-
3.8.1.5 Corynebacterium sp.
-
 gene dhaA
-
3.8.1.5 Marinobacter sp. A3JB27 a psychrophilic organism
-
3.8.1.5 Mesorhizobium loti Q98C03
-
-
3.8.1.5 Mesorhizobium loti MAFF303099 Q98C03
-
-
3.8.1.5 Mycobacterium avium Q93K00 gene dhmA
-
3.8.1.5 Mycobacterium avium N85 Q93K00 gene dhmA
-
3.8.1.5 Mycobacterium sp. Q9ZER0 gene dhaAF
-
3.8.1.5 Mycobacterium sp. GP1 Q9ZER0 gene dhaAF
-
3.8.1.5 Mycobacterium tuberculosis P9WMR9 dhaA
-
3.8.1.5 Mycobacterium tuberculosis H37Rv P9WMR9 dhaA
-
3.8.1.5 Mycobacterium tuberculosis variant bovis A4Q9R7 gene dmbC
-
3.8.1.5 Mycobacterium tuberculosis variant bovis Q6EUU8 gene dmbB
-
3.8.1.5 Mycobacterium tuberculosis variant bovis Q9XB14 gene dhaA
-
3.8.1.5 Mycobacterium tuberculosis variant bovis 5033/66 A4Q9R7 gene dmbC
-
3.8.1.5 Mycobacterium tuberculosis variant bovis 5033/66 Q6EUU8 gene dmbB
-
3.8.1.5 Mycobacterium tuberculosis variant bovis 5033/66 Q9XB14 gene dhaA
-
3.8.1.5 Plesiocystis pacifica A6G7B1
-
-
3.8.1.5 Psychrobacter cryohalolentis Q1QBB9 gene dhmA, a psychrophilic organism
-
3.8.1.5 Psychrobacter cryohalolentis K5 Q1QBB9 gene dhmA, a psychrophilic organism
-
3.8.1.5 Rhodobacteraceae bacterium UDC319 A0A023I2Y1
-
-
3.8.1.5 Rhodococcus rhodochrous P0A3G2 gene dhaA
-
3.8.1.5 Rhodococcus rhodochrous NCIMB 13064 P0A3G2 gene dhaA
-
3.8.1.5 Rhodococcus sp.
-
 gene dhaA
-
3.8.1.5 Rhodopirellula baltica G3XCP3 gene drbA
-
3.8.1.5 Rhodopirellula baltica SH1 G3XCP3 gene drbA
-
3.8.1.5 Sphingobium indicum
-
-
-
3.8.1.5 Sphingobium indicum P51698 gene linB
-
3.8.1.5 Sphingobium indicum B90A
-
-
-
3.8.1.5 Sphingobium indicum UT26 P51698 gene linB
-
3.8.1.5 Sphingobium sp. A4PEU6
-
-
3.8.1.5 Sphingobium sp. MI1205 A4PEU6
-
-
3.8.1.5 Sphingomonas sp.
-
-
-
3.8.1.5 Sphingomonas sp. BHC-A
-
-
-
3.8.1.5 Strongylocentrotus purpuratus
-
-
-
3.8.1.5 Xanthobacter autotrophicus P22643 gene dhlA
-
3.8.1.5 Xanthobacter autotrophicus GJ10 P22643 gene dhlA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.8.1.5 additional information no activity with chlorinated compounds Plesiocystis pacifica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.8.1.5 DadB
-
 Alcanivorax dieselolei
3.8.1.5 DatA
-
 Agrobacterium tumefaciens
3.8.1.5 DbeA
-
 Bradyrhizobium elkanii
3.8.1.5 DbjA
-
 Bradyrhizobium japonicum
3.8.1.5 DhaA
-
 Corynebacterium sp.
3.8.1.5 DhaA
-
 Arthrobacter sp.
3.8.1.5 DhaA
-
 Rhodococcus sp.
3.8.1.5 DhaA
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 DhaA
-
 Mycobacterium tuberculosis
3.8.1.5 DhaA
-
 Rhodococcus rhodochrous
3.8.1.5 DhaB
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 DhaC
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 DhAf
-
 Mycobacterium sp.
3.8.1.5 DhlA
-
 Xanthobacter autotrophicus
3.8.1.5 DhmA
-
 Mycobacterium avium
3.8.1.5 DhmA
-
 Psychrobacter cryohalolentis
3.8.1.5 DmaA
-
 Marinobacter sp.
3.8.1.5 dmbA
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 DmbB
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 DmbC
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 dmlA
-
 Mesorhizobium loti
3.8.1.5 DmtA
-
 Mycobacterium tuberculosis
3.8.1.5 DmxA
-
 Marinobacter sp.
3.8.1.5 DpcA
-
 Psychrobacter cryohalolentis
3.8.1.5 DppA
-
 Plesiocystis pacifica
3.8.1.5 DrbA
-
 Rhodopirellula baltica
3.8.1.5 DspA
-
 Strongylocentrotus purpuratus
3.8.1.5 HanR
-
 Rhodobacteraceae bacterium UDC319
3.8.1.5 HLD
-
 Corynebacterium sp.
3.8.1.5 HLD
-
 Arthrobacter sp.
3.8.1.5 HLD
-
 Rhodococcus sp.
3.8.1.5 HLD
-
 Strongylocentrotus purpuratus
3.8.1.5 HLD
-
 Sphingomonas sp.
3.8.1.5 HLD
-
 Mycobacterium tuberculosis variant bovis
3.8.1.5 HLD
-
 Sphingobium indicum
3.8.1.5 HLD
-
 Xanthobacter autotrophicus
3.8.1.5 HLD
-
 Bradyrhizobium japonicum
3.8.1.5 HLD
-
 Mesorhizobium loti
3.8.1.5 HLD
-
 Sphingobium sp.
3.8.1.5 HLD
-
 Mycobacterium tuberculosis
3.8.1.5 HLD
-
 Rhodococcus rhodochrous
3.8.1.5 HLD
-
 Agrobacterium tumefaciens
3.8.1.5 HLD
-
 Plesiocystis pacifica
3.8.1.5 HLD
-
 Alcanivorax dieselolei
3.8.1.5 HLD
-
 Mycobacterium sp.
3.8.1.5 HLD
-
 Bradyrhizobium elkanii
3.8.1.5 HLD
-
 Mycobacterium avium
3.8.1.5 HLD
-
 Rhodopirellula baltica
3.8.1.5 HLD
-
 Marinobacter sp.
3.8.1.5 HLD
-
 Psychrobacter cryohalolentis
3.8.1.5 HLD
-
 Rhodobacteraceae bacterium UDC319
3.8.1.5 LinBMI
-
 Sphingomonas sp.
3.8.1.5 LinBMI
-
 Sphingobium indicum
3.8.1.5 LinBMI
-
 Sphingobium sp.
3.8.1.5 LinBUT
-
 Sphingobium indicum
3.8.1.5 Rv2579
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs Xanthobacter autotrophicus
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs Plesiocystis pacifica
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs Mycobacterium tuberculosis variant bovis
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs Mycobacterium avium
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs Psychrobacter cryohalolentis
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Corynebacterium sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Arthrobacter sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Rhodococcus sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Strongylocentrotus purpuratus
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Sphingomonas sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Sphingobium indicum
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Bradyrhizobium japonicum
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Mesorhizobium loti
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Sphingobium sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Rhodococcus rhodochrous
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Agrobacterium tumefaciens
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Alcanivorax dieselolei
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Mycobacterium sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Bradyrhizobium elkanii
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Marinobacter sp.
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs Rhodobacteraceae bacterium UDC319
3.8.1.5 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 Mycobacterium tuberculosis variant bovis
3.8.1.5 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 Mycobacterium tuberculosis
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs Mycobacterium tuberculosis variant bovis
3.8.1.5 evolution the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs Rhodopirellula baltica
3.8.1.5 additional information the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26 Sphingobium indicum
3.8.1.5 physiological function the enzyme is involved in 1,2-dichloroethane degradation Xanthobacter autotrophicus
3.8.1.5 physiological function the enzyme is involved in 1,2-dichloroethane degradation Bradyrhizobium elkanii
3.8.1.5 physiological function the enzyme is involved in 1-haloalkanes degradation Rhodococcus rhodochrous
3.8.1.5 physiological function the enzyme is involved in gamma-HCH degradation Sphingobium indicum