3.8.1.5: haloalkane dehalogenase
This is an abbreviated version!
For detailed information about haloalkane dehalogenase, go to the full flat file.
Word Map on EC 3.8.1.5
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3.8.1.5
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xanthobacter
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autotrophicus
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dehalogenation
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1,2-dichloroethane
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halide
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carbon-halogen
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1,2-dibromoethane
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sphingomonas
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paucimobilis
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1,2,3-trichloropropane
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synthesis
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hexachlorocyclohexane
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rhodochrous
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sphingobium
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environmental protection
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alkyl-enzyme
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haloacid
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1-chlorobutane
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2-chloroethanol
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ncimb
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chloroalkane
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dehydrochlorinase
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epichlorohydrine
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gamma-hexachlorocyclohexane
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halotag
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biotechnology
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alpha/beta-hydrolase
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haloalcohols
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agriculture
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halide-binding
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degradation
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industry
- 3.8.1.5
- xanthobacter
- autotrophicus
-
dehalogenation
- 1,2-dichloroethane
- halide
-
carbon-halogen
- 1,2-dibromoethane
- sphingomonas
- paucimobilis
- 1,2,3-trichloropropane
- synthesis
- hexachlorocyclohexane
- rhodochrous
- sphingobium
- environmental protection
-
alkyl-enzyme
-
haloacid
- 1-chlorobutane
- 2-chloroethanol
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ncimb
-
chloroalkane
- dehydrochlorinase
- epichlorohydrine
- gamma-hexachlorocyclohexane
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halotag
- biotechnology
-
alpha/beta-hydrolase
- haloalcohols
- agriculture
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halide-binding
- degradation
- industry
Reaction
Synonyms
1,3,4,6,-tetrachloro-1,4-cyclohexadiene halidohydrolase, 1-chlorohexane halidohydrolase, 1-haloalkane dehalogenase, DadB, DatA, DbeA, DbjA, DccA, DhaA, DhaA31, DhaB, DhaC, DhAf, DhlA, DhmA, DmaA, dmbA, DmbB, DmbC, dmlA, DmmA, DmrA, DmrB, DmsA, DmtA, DmxA, DpcA, DppA, DrbA, DsaA, DspA, EC 3.8.1.1, eHLD-B, eHLD-C, haloalkane dehalogenase, haloalkane dehalogenase LinB, HanR, HLD, HLD-I, LinB, LinBMI, LinBUT, metallo-haloalkane dehalogenase, protein XP_504164, Rv2579, Ylehd
ECTree
3.8.1.5 haloalkane dehalogenaseAdvanced search results
results (
results (KM Value
KM Value on EC 3.8.1.5 - haloalkane dehalogenase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
11.33
3-chloro-2-methylprop-1-ene
pH 8.6, 37°C, recombinant enzyme
4.3
1,2-Dibromoethane
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GJ10, calculated from rate constants for four-steps reaction mechanism
5.65
1,2-Dibromoethane
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pH 8.6, 37°C, recombinant wild-type enzyme, data from 2 experimental sets
29
1,2-Dibromoethane
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GJ10, F172W mutant, calculated from rate constants for four-steps reaction mechanism
59
1,2-Dibromoethane
GJ10mutant W175Y, calculated from rate constants
60
1,2-Dibromoethane
GJ10 mutant W175Y, steady state experiments
0.001
1,2-Dichloroethane
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GJ10, calculated from rate constants for four-steps reaction mechanism
0.008
1,2-Dichloroethane
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GJ10, F172W mutant, calculated from rate constants for four-steps reaction mechanism
0.24
1,3-dibromopropane
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pH and temperature not specified in the publication
0.82
1,3-dibromopropane
recombinant mutant Y109W, pH 8.6, 37°C
0.92
1,3-dibromopropane
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pH 8.6, 37°C, recombinant His-tagged enzyme
2.2
1,3-dibromopropane
recombinant wild-type enzyme, pH 8.6, 37°C
4
1,3-Dichloropropane
above, recombinant wild-type enzyme and mutant Y109W, pH 8.6, 37°C
0.16
1,3-diiodopropane
recombinant mutant Y109W, pH 8.6, 37°C
0.2
1,3-diiodopropane
recombinant wild-type enzyme, pH 8.6, 37°C
0.53
1-bromobutane
recombinant wild-type enzyme, pH 8.6, 37°C
0.14
1-bromohexane
recombinant wild-type enzyme, pH 8.6, 37°C
0.235
1-Chlorobutane
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pH 8.6, 37°C, recombinant wild-type enzyme, data from 2 experimental sets
0.07
1-Chlorohexane
recombinant wild-type enzyme, pH 8.6, 37°C
1.9
4-bromobutyronitrile
pH 8.0, 25°C, recombinant enzyme
4.9
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker
6.9
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker
additional information
additional information
steady-state kinetics
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additional information
additional information
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steady-state kinetics
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additional information
additional information
kinetics and binding energy analysis, wild-type and mutant F172W
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additional information
additional information
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kinetics of recombinant wild-type and mutant enzymes, analysis of electrostatic interaction energies
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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steady-state and pre-steady-state kintic analysis, kinetic mechanism of dehalogenation
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additional information
additional information
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steady-state kinetics of wild-type and mutant enzymes using substrate 1-chlorobutane and 1,2-dibromoethane
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additional information
additional information
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steady-state kinetics, overview
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additional information
additional information
DatA shows substrate-dependent and cooperative kinetics
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additional information
additional information
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steady-state and transient kinetics, kinetics of bromide ion binding, overview. Two distinct binding phases that suggest a two-step mechanism of bromide ion binding
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additional information
additional information
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steady-state kinetic analysis with substrates 1-bromobutane and 1,3-dibromopropane, positive cooperative substrate binding, overview
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additional information
additional information
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steady-state kinetics with substrate1,2,3-trichloropropane, wild-type and mutant enzymes, overview
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additional information
additional information
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substrate specificity and kinetics, overview
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additional information
additional information
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substrate specificity and kinetics, overview
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additional information
additional information
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substrate specificity and kinetics, overview
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additional information
additional information
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substrate specificity and kinetics, overview
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additional information
additional information
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substrate specificity and kinetics, overview
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additional information
additional information
pre-steady-state and steady-state kinetics, both the wild-type and the mutant yield hyperbolic kinetic profiles for their reactions with 1,3-dibromopropane and 1-bromohexane, suggesting classical Michaelis-Menten kinetics. The sigmoidal profiles obtained in experiments using 1,3-diiodopropane, 1-chlorohexane and 1-bromobutane indicate that these substrates are hydrolyzed via a cooperative Hill mechanism, KM values for the mutant are lower than for the wild-type enzyme. Substrate binding and the cleavage of the carbon-halogen bond are fast steps, and that hydrolysis of the alkyl-enzyme intermediate is the rate-determining step in the conversion of 1-bromobutane by both enzymes
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additional information
additional information
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steady-state kinetic analysis, kinetic resolution of 2-bromobutane and 2-bromopentane
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