3.8.1.2: (S)-2-haloacid dehalogenase
This is an abbreviated version!
For detailed information about (S)-2-haloacid dehalogenase, go to the full flat file.
Word Map on EC 3.8.1.2
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3.8.1.2
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dehalogenation
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synthesis
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haloacids
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l-2-haloacids
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bioremediation
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l-2-chloropropionate
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2-chloropropionic
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halide
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hymeniacidon
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monochloroacetic
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xanthobacter
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dechlorination
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autotrophicus
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monobromoacetic
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chloroacetate
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haloalkane
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analysis
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environmental protection
- 3.8.1.2
-
dehalogenation
- synthesis
-
haloacids
- l-2-haloacids
-
bioremediation
- l-2-chloropropionate
-
2-chloropropionic
- halide
- hymeniacidon
-
monochloroacetic
-
xanthobacter
-
dechlorination
- autotrophicus
-
monobromoacetic
- chloroacetate
- haloalkane
- analysis
- environmental protection
Reaction
Synonyms
2-HAD, 2-halo acid dehalogenase, 2-haloacid dehalogenase, 2-haloacid dehalogenase[ambiguous], 2-haloacid halidohydrolase[ambiguous], 2-haloalkanoate dehalogenase, 2-haloalkanoic acid dehalogenase, 2-haloalkanoid acid halidohydrolase, 2-halocarboxylic acid dehalogenase II, DEH99, dehalogenase IVa, DehL, DL-2-haloacid dehalogenase [ambiguous], HADIIBSW, HadL AJ1, L-2-DhlB, L-2-haloacid dehalogenase, L-2-MCPA dehalogenase, L-2_HAD, L-DEX, L-DEX YL, L-DEXs, L-HAD, L-HADST, L-haloacid dehalogenase, PH1421, Rhodobacteraceae family L-haloacid dehalogenase, S-2-haloacid dehalogenase, STK_25700
ECTree
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Subunits
Subunits on EC 3.8.1.2 - (S)-2-haloacid dehalogenase
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dimer
homodimer
monomer
tetramer
additional information
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x * 27800, about, sequence calculation, x * 25600-35600, recombinant tagged enzyme, SDS-PAGE, x * 32500, about, recombinant tagged enzyme, sequence calculation
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x * 27800, about, sequence calculation, x * 25600-35600, recombinant tagged enzyme, SDS-PAGE, x * 32500, about, recombinant tagged enzyme, sequence calculation
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dimer
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the subunit consists of two structurally distinct domains: the core domain and the subdomain
homodimer
2 * 25000, SDS-PAGE, 2 * 25600, about, sequence calculation
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
tetramer
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1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
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docking and structure analysis of enzyme mutants K151A and D180A in complex with substrate (S)-2-chloropropionic acid, molecular dynamics, overview
additional information
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docking and structure analysis of enzyme mutants K151A and D180A in complex with substrate (S)-2-chloropropionic acid, molecular dynamics, overview
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additional information
enzyme structure comparisons, overview. The two subunits of DehRhb are related by a molecular twofold axis to which the a2 helices from each subunit are parallel, folding of the DehRhb monomer and active site structure, structure modeling