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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

Reaction

(S)-2-haloacid
+
H2O
=
(R)-2-hydroxyacid
 +
halide

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

     3 Hydrolases
         3.8 Acting on halide bonds
             3.8.1 In carbon-halide compounds
                3.8.1.2 (S)-2-haloacid dehalogenase

Engineering

Engineering on EC 3.8.1.2 - (S)-2-haloacid dehalogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D11E
-
totally inactive in catalysis
D11N
-
totally inactive in catalysis
D11S
-
totally inactive in catalysis
D181N
-
totally inactive in catalysis
N178D
-
defective in catalysis
D11E
-
totally inactive in catalysis
-
D11N
-
totally inactive in catalysis
-
D11S
-
totally inactive in catalysis
-
D181N
-
totally inactive in catalysis
-
D180A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
K151A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
S118A
-
mutant with lower specific activity and higher KM-value
S175A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
D180A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
K151A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
S118A
-
mutant with lower specific activity and higher KM-value
-
S175A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
D13A
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site
H184A
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site
H184Y
mutation significantly increases the binding strength of the enzyme towards D-2-chloropropionate
I186Y
mutation significantly increases the binding strength of the enzyme towards D-2-chloropropionate
M48A
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site
R51A
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site
R51L
mutation cancells out the dehalogenation activity of DehL towards it natural substrate, L-2-chloropropionate
R51L/M48R
mutation introduces a new activity towards D-2-chloropropionate, conveying the possibility of inverting the enantiospecificity of the enzyme from L-to D-enantiomer
T17A
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site
additional information