3.8.1.9: (R)-2-haloacid dehalogenase
This is an abbreviated version!
For detailed information about (R)-2-haloacid dehalogenase, go to the full flat file.
Word Map on EC 3.8.1.9
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3.8.1.9
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dehalogenation
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putida
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dexamethasone
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rhizobium
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2-haloalkanoic
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l-enantiomer
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2-chloropropionate
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enantiomers
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2-haloacids
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dl-2-haloacid
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monobromoacetate
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monochloroacetate
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dendrimer
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tear
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halide
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inflamed
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subconjunctival
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biodistribution
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halogenated
- 3.8.1.9
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dehalogenation
- putida
- dexamethasone
-
rhizobium
-
2-haloalkanoic
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l-enantiomer
- 2-chloropropionate
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enantiomers
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2-haloacids
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dl-2-haloacid
- monobromoacetate
- monochloroacetate
- dendrimer
-
tear
- halide
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inflamed
-
subconjunctival
-
biodistribution
-
halogenated
Reaction
Synonyms
2-haloalkanoic acid dehalogenase, 2-haloalkanoid acid halidohydrolase, D-2-haloacid dehalogenase, D-2-MCPA dehalogenase, D-DEX, D-specific dehalogenase, D-specific mono chloro propionoic acid dehalogenase, DEH138, DehD, DehIII, HadD AJ1, R-2-haloacid dehalogenase
ECTree
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Engineering
Engineering on EC 3.8.1.9 - (R)-2-haloacid dehalogenase
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D205E
activity with D-2-chloropropionate is 10.1% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 13fold higher compared to mutant enzyme
D205N
F281A
activity with D-2-chloropropionate is 54.7% compared to activity of the wild-type enzyme
G50A
activity with D-2-chloropropionate is 5.1% compared to activity of the wild-type enzyme
I52G
activity with D-2-chloropropionate is 1.5% compared to activity of the wild-type enzyme
L285I
activity with D-2-chloropropionate is 24.4% compared to activity of the wild-type enzyme
L288A
the mutant enzyme is active toward L-enantiomers. The catalytic efficiency is less than 30% of mutant enzyme L288I
L288I
L288V
kcat/Km of the L288V mutant displays over 80% of that of the L288I mutant
M284C
activity with D-2-chloropropionate is 7.0% compared to activity of the wild-type enzyme
M284F
mutant enzyme shows no enantioselective changes in contrast to the wild-type enzyme
N131D
activity with D-2-chloropropionate is 4.4% compared to activity of the wild-type enzyme
N203A
N203S
activity with D-2-chloropropionate is 0.4% compared to activity of the wild-type enzyme
S204A
activity with D-2-chloropropionate is 4.9% compared to activity of the wild-type enzyme
S204T
activity with D-2-chloropropionate is 41.8% compared to activity of the wild-type enzyme
V51F
activity with D-2-chloropropionate is 36.6% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 4fold higher compared to mutant enzyme
W48A
activity with D-2-chloropropionate is 0.2% compared to activity of the wild-type enzyme
Y134F
activity with D-2-chloropropionate is 0.1% compared to activity of the wild-type enzyme
G50A
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activity with D-2-chloropropionate is 5.1% compared to activity of the wild-type enzyme
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N131D
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activity with D-2-chloropropionate is 4.4% compared to activity of the wild-type enzyme
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S204A
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activity with D-2-chloropropionate is 4.9% compared to activity of the wild-type enzyme
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W48A
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activity with D-2-chloropropionate is 0.2% compared to activity of the wild-type enzyme
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R134A
site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates
Y135A
site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates
activity with D-2-chloropropionate is 37.2% compared to activity of the wild-type enzyme
L288I
the mutation enlarges the size of the channel and allows the enzyme to accommodate L-enantiomers (L-2-bromopropionate). The wing flip of I288 induces hydrophobic interactions with the L-enantiomer and directly affects the catalytic efficiency
activity with D-2-chloropropionate is 1.2% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 355fold higher compared to mutant enzyme
N203A
mutant enzyme shows no enantioselective changes in contrast to the wild-type enzyme