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(1-bromomethyl)cyclohexane + H2O
?
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + H2O
cis-2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
(bromomethyl)cyclohexane + H2O
cyclohexylmethanol + bromide
(RS)-3-chloropropane-1,2-diol + NAD+
(R)-3-chloropropane-1,2-diol + 2-oxo-propionaldehyde + CH3COOH + Cl- + HCOOH + NADH
-
-
-
-
?
1,1,2,3,4,5,6-heptachlorocyclohexane + H2O
2,3,4,4,5,6-hexachlorocyclohexanol + chloride
1,1,2-trichloroethane + H2O
? + chloride
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
1,2,3-tribromopropane + H2O
?
1,2,3-trichloropropane + H2O
(RS)-2,3-dichloropropan-1-ol + chloride
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
1,2,3-trichloropropane + H2O
2,3-dichloropropanol + chloride
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
1,2,3-trichloropropane + H2O
?
1,2,3-trichloropropene + H2O
2,3-dichloropropenol + chloride
-
-
-
?
1,2-dibromo-3-chloropropane
2-bromo-3-chloro-1-propanol + bromide
about 35% of the activity compared to 4-bromobutyronitrile
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloro-1-propanol + bromide
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
1,2-dibromoethane + H2O
2-bromo-1-ethanol + bromide
1,2-dibromoethane + H2O
2-bromoethanol + bromide
1,2-dibromoethane + H2O
bromoethanol + bromide
-
-
-
?
1,2-dibromohexane + H2O
2-bromohexanol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
1,2-dibromopropane + H2O
2-bromopropan-1-ol + bromide
1,2-dibromopropane + H2O
2-bromopropanol + bromide
1,2-dibromopropane + H2O
? + bromide
-
-
-
-
?
1,2-dichlorobutane + H2O
?
-
7.8% of the activity with 4-chlorobutanol
-
-
?
1,2-dichloroethane + 2 H2O
1,2-ethanediol + 2 chloride
1,2-dichloroethane + H2O
2-chloro-1-ethanol + chloride
1,2-dichloroethane + H2O
2-chloroethanol + chloride
1,2-dichloroethane + H2O
?
1,2-dichloropropane + H2O
2-chloro-1-propanol + chloride
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
1,2-dichloropropane + H2O
2-chloropropanol + chloride
-
-
-
?
1,2-dichloropropane + H2O
?
1,3,4,6-tetrachloro-1,4,cyclohexadiene + 2 H2O
2,5-dichloro-2,5-cyclohexadiene-1,4-diol + 2 chloride
1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O
2,4,5-trichloro-2,5-cyclohexadiene-1-ol + chloride
-
-
-
?
1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O
?
1,3-dibromo-2-methylpropane + H2O
3-bromo-2-methylpropan-1-ol + bromide
1,3-dibromo-2-phenylpropane + H2O
?
1,3-dibromo-2-propanol + H2O
3-bromo-1,2-propandiol
1,3-dibromobutane + H2O
3-bromo-1-propanol + bromide
about 20% of the activity compared to 4-bromobutyronitrile
-
-
?
1,3-dibromopropane + 2 H2O
1,3-propanediol + 2 bromide
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
1,3-dibromopropane + H2O
3-bromo-propanol + bromide
1,3-dibromopropane + H2O
3-bromopropanol + bromide
1,3-dichlorobutane + H2O
?
-
12% of the activity with 4-chlorobutanol
-
-
?
1,3-dichloropropane + H2O
3-chloro-1-propanol + chloride
1,3-dichloropropane + H2O
3-chloropropan-1-ol + chloride
-
-
-
?
1,3-dichloropropane + H2O
3-chloropropanol + chloride
1,3-dichloropropane + H2O
?
1,3-dichloropropene + H2O
3-chloropropenol + chloride
-
-
-
?
1,3-diiodopropane + H2O
3-iodo-1-propanol + iodide
1,3-diiodopropane + H2O
3-iodopropanol + iodide
1,4-dichlorobutane + H2O
4-chlorobutanol + chloride
-
-
-
-
?
1,4-dichlorobutane + H2O
?
-
27% of the activity with 4-chlorobutanol
-
-
?
1,5-dichloropentane + H2O
5-chloro-1-pentanol + chloride
1,5-dichloropentane + H2O
5-chloropentanol + chloride
1,5-dichloropentane + H2O
?
-
20% of the activity with 4-chlorobutanol
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
1,6-dichlorohexane + H2O
6-chlorohexanol + chloride
1,6-dichlorohexane + H2O
?
-
32% of the activity with 4-chlorobutanol
-
-
?
1,6-diiodohexane + H2O
6-iodohexane + iodide
-
low activity
-
-
?
1,7-dichloroheptane + H2O
?
-
20% of the activity with 4-chlorobutanol
-
-
?
1,8-dichlorooctane + H2O
?
-
32% of the activity with 4-chlorobutanol
-
-
?
1,9-dichlorononane + H2O
?
-
14% of the activity with 4-chlorobutanol
-
-
?
1-bromo-2-chloroethane
2-chloro-1-ethanol + bromide
about 50% of the activity compared to 4-bromobutyronitrile
-
-
?
1-bromo-2-chloroethane + H2O
2-chloro-1-ethanol + bromide
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
1-bromo-2-chloroethane + H2O
?
-
76% of the activity with 1,2-dichloroethane
-
-
?
1-bromo-2-methylpropane + H2O
2-methylpropanol + bromide
1-bromo-3-chloropropane + H2O
3-chloro-1-propanol + bromide
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
1-bromo-3-chloropropane + H2O
?
-
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
1-bromobutane + H2O
butanol + bromide
1-bromobutane + H2O
n-butanol + bromide
1-bromodecane + H2O
1-decanol + bromide
1-bromododecane + H2O
1-dodecanol + bromide
1-bromoheptane + H2O
1-heptanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
1-bromohexane + H2O
hexanol + bromide
1-bromohexane + H2O
n-hexanol + bromide
1-bromononane + H2O
1-nonanol + bromide
-
-
-
?
1-bromooctane + H2O
1-octanol + bromide
-
-
-
?
1-bromooctane + H2O
octanol + bromide
-
-
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
1-bromopropane + H2O
1-propanol + bromide
1-bromopropane + H2O
propanol + bromide
1-chloro-2,2-dimethylpropane + H2O
2,2-dimethylpropan-1-ol + chloride
1-chloro-2-(2-chloroethoxy)ethane + H2O
2-(2-chloroethoxy)ethanol + chloride
-
-
-
?
1-chloro-2-(2-chloroethoxy)ethane + H2O
?
1-chloro-2-bromoethane + H2O
2-bromoethanol + chloride
-
-
-
-
?
1-chloro-2-bromoethane + H2O
?
-
-
-
-
?
1-chloro-2-fluoroethane + H2O
?
-
no release of fluoride, 25% of the activity with 1,2-dichloroethane
-
-
?
1-chloro-2-methylpropane + H2O
2-methylpropanol + chloride
1-chloro-4-methylbutane + H2O
pentanol + chloride
-
42% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
1-chlorobutane + H2O
butanol + chloride
1-chlorobutane + H2O
n-butanol + chloride
1-chlorodecane + H2O
decanol + chloride
1-chlorodecane + H2O
n-decanol + chloride
1-chlorododecane + H2O
dodecanol + chloride
-
-
-
?
1-chloroheptane + H2O
heptanol + chloride
1-chlorohexane + H2O
1-hexanol + chloride
1-chlorohexane + H2O
hexanol + chloride
1-chlorohexane + H2O
n-hexanol + chloride
1-chlorononane + H2O
nonanol + chloride
-
13% of the activity with 4-chlorobutanol
-
-
?
1-chlorooctane + H2O
octanol + chloride
1-chloropentane + H2O
1-pentanol + chloride
-
-
-
-
?
1-chloropentane + H2O
n-pentanol + chloride
1-chloropentane + H2O
pentanol + chloride
1-chloropropane + H2O
propanol + chloride
1-chlorotetradecane + H2O
tetradecanol + chloride
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
1-haloalkane + H2O
primary alcohol + halide
1-iodobutane + H2O
1-butanol + iodide
1-iodobutane + H2O
butanol + iodide
1-iodobutane + H2O
n-butanol + iodide
1-iodoethane + H2O
ethanol + iodide
-
-
-
-
?
1-iodohexane + H2O
1-hexanol + iodide
1-iodohexane + H2O
hexanol + iodide
1-iodohexane + H2O
n-hexanol + iodide
1-iodopropane + H2O
1-propanol + iodide
1-iodopropane + H2O
n-propanol + iodide
-
-
-
-
?
1-iodopropane + H2O
propanol + iodide
2,3,4,5,6-pentachlorocyclohexanol + H2O
2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
2,3,4,5,6-pentachlorohexanol + H2O
tetrachlorocyclohexanediol + chloride
2,3-dichloroprop-1-ene + H2O
?
2,3-dichloropropene + H2O
?
2-bromo-1-chloropropane + H2O
2-bromo-1-propanol + chloride
2-bromo-1-chloropropane + H2O
?
-
high activity
-
-
?
2-bromoacetamide + H2O
acetamide + bromide
poor substrate
-
-
?
2-bromoacetonitrile + H2O
acetonitrile + bromide
-
-
-
?
2-bromobutane + H2O
2-butanol + bromide
2-bromoethanol + H2O
ethanol + bromide
2-bromohexane + H2O
2-hexanol + bromide
-
-
-
?
2-bromopentane + H2O
2-pentanol + bromide
2-chloroacetamide + H2O
acetamide + chloride
poor substrate
-
-
?
2-chloroacetonitrile + H2O
acetonitrile + chloride
-
-
-
?
2-chlorobutane + H2O
2-butanol + chloride
2-chloroethanol + H2O
ethanol + chloride
very poor substrate
-
-
?
2-chloropropane + H2O
ethanol + chloride
-
-
-
-
?
2-iodobutane + H2O
2-butanol + iodide
2-iodobutane + H2O
?
-
-
-
-
?
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + H2O
2,5,6-trichloro-2-cyclohexene-1,4-diol + chloride
3-bromo-1-propanol + H2O
?
-
-
-
?
3-bromo-1-propanol + H2O
? + bromide
low activity
-
-
?
3-bromo-1-propanol + H2O
ethanol + bromide
-
-
-
-
?
3-chloro-2-(chloromethyl)-1-propene + H2O
2-chloromethyl-2-propen-1-ol + Cl-
-
-
-
-
?
3-chloro-2-(chloromethyl)-1-propene + H2O
?
-
-
-
?
3-chloro-2-methylprop-1-ene + H2O
?
3-chloro-2-methylpropene + H2O
2-methylpropene-3-ol + chloride
3-chloro-2-methylpropene + H2O
?
3-chloropropene + H2O
propenol + chloride
-
45% of the activity with 1,2-dichloroethane
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
4-bromobutyronitrile + H2O
?
4-bromobutyronitrile + H2O
? + bromide
4-chlorobutanol + H2O
butane-1,4-diol + chloride
-
highest activity
-
-
?
alpha-hexachlorocyclohexane + H2O
beta-pentachlorocyclohexene + chloride
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
beta-hexachlorocyclohexane + H2O
?
beta-hexachlorocyclohexane + H2O
pentachlorocyclohexanol + chloride
-
-
-
?
bis(2-chloroethyl) ether + H2O
?
-
-
-
?
bis(2-chloroethyl)ether + H2O
?
bromochloromethane + H2O
?
-
99% of the activity with 1,2-dichloroethane
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
bromoethane + H2O
ethanol + bromide
chlorocyclohexane + H2O
cyclohexanol + chloride
chlorocyclopentane + H2O
cyclopentanol + chloride
chlorocyclopentane + H2O
hydroxycyclopentane + chloride
-
-
-
-
?
chloroethane + H2O
ethanol + chloride
chloromethane + H2O
methanol + chloride
cyclohexylbromide + H2O
cyclohexanol + bromide
-
-
-
-
?
cyclohexylchloride + H2O
cyclohexanol + chloride
-
-
-
-
?
delta-hexachlorocyclohexane + H2O
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
delta-hexachlorocyclohexane + H2O
pentachlorocyclohexanol + chloride
-
-
-
?
delta-pentachlorocyclohexene + H2O
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + chloride
-
-
-
-
?
dibromomethane + H2O
bromomethanol + bromide
dichloromethane + H2O
?
-
-
-
?
dichloromethane + H2O
? + chloride
dichloromethane + H2O
chloromethanol + chloride
poor substrate
-
-
?
epibromohydrine + H2O
?
-
-
-
?
epichlorohydrin + H2O
?
poor substrate
-
-
?
epsilon-hexachlorocyclohexane + H2O
pentachlorocyclohexanol + tetrachlorocyclohexane-1,4-diol + chloride
ethyl 2-bromobutyrate + H2O
?
gamma-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
gamma-hexachlorocyclohexane + H2O
?
gamma-pentachlorocyclohexene + H2O
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + 2,5,6-trichloro-2-cyclohexene-1,4-diol + chloride
-
-
-
-
?
haloalkane + H2O
alcohol + halide
meso-2,3-dibromobutane + H2O
?
methyl 2-bromopropionate + H2O
?
-
-
-
?
monochloroacetic acid + H2O
glycolate + chloride
n-haloalkanes + H2O
primary alcohols + halide
pentachlorocyclohexanol + H2O
tetrachlorocyclohexanediol + chloride
-
-
-
?
rac-1,3-dibromobutane + H2O
(S)-butane-1,3-diol + bromide
secondary haloalkanes + H2O
?
-
-
-
-
?
tetrachloromethane + H2O
? + chloride
trichloroacetic acid + H2O
? + chloride
trichloromethane + H2O
? + chloride
additional information
?
-
(1-bromomethyl)cyclohexane + H2O
?
-
low activity
-
-
?
(1-bromomethyl)cyclohexane + H2O
?
-
2.5% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
(1-bromomethyl)cyclohexane + H2O
?
-
less than 1% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + H2O
cis-2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
-
?
(1S,3S)-2,3,4,5,6-pentachlorocyclohexanol + H2O
cis-2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
-
?
(bromomethyl)cyclohexane + H2O
cyclohexylmethanol + bromide
-
-
-
?
(bromomethyl)cyclohexane + H2O
cyclohexylmethanol + bromide
-
-
-
-
?
1,1,2,3,4,5,6-heptachlorocyclohexane + H2O
2,3,4,4,5,6-hexachlorocyclohexanol + chloride
-
-
-
-
?
1,1,2,3,4,5,6-heptachlorocyclohexane + H2O
2,3,4,4,5,6-hexachlorocyclohexanol + chloride
-
-
-
-
?
1,1,2-trichloroethane + H2O
? + chloride
-
-
-
-
?
1,1,2-trichloroethane + H2O
? + chloride
-
-
-
-
?
1,1,2-trichloroethane + H2O
? + chloride
-
-
-
-
?
1,1,2-trichloroethane + H2O
? + chloride
-
-
-
-
?
1,1,2-trichloroethane + H2O
? + chloride
-
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
about 10% of the activity compared to 4-bromobutyronitrile
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
-
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
-
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
-
about 50% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
high activity
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
-
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
low activity
-
-
?
1,2,3-tribromopropane + H2O
2,3-dibromopropanol + bromide
-
-
-
-
?
1,2,3-tribromopropane + H2O
?
-
-
-
-
?
1,2,3-tribromopropane + H2O
?
-
-
-
-
?
1,2,3-trichloropropane + H2O
(RS)-2,3-dichloropropan-1-ol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
(RS)-2,3-dichloropropan-1-ol + chloride
-
structural model of DhaA31 with TCP docked in the active site, comparison with DhaA31 mutant enzyme docking models, overview. The pentad is made up of an Asp-His-Asp catalytic triad and a Trp-Trp or Trp-Asn diad for halide binding. An aspartate residue acts as the nucleophile to displace a halide ion from the substrate. By hydrolysis of the resulting covalent alkyl-enzyme intermediate, alcohol is released
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
low activity
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
low activity
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
-
substrate, but not the product, adsorbs with high affinity onto the polyethylenimine impregnated gamma-alumina support used for enzyme immobilization
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
1,2,3-trichloropropane is a persistent anthropogenic toxic pollutant that can be converted to the less toxic 2,3-dichloropropan-1-ol
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
-
prefered formation of R-enantiomer due to a specific interaction of substrate with residue N41
-
?
1,2,3-trichloropropane + H2O
2,3-dichloropropan-1-ol + chloride
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,2,3-trichloropropane + H2O
?
-
-
-
-
?
1,2,3-trichloropropane + H2O
?
-
-
-
-
?
1,2,3-trichloropropane + H2O
?
-
-
-
?
1,2,3-trichloropropane + H2O
?
-
substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
-
-
?
1,2,3-trichloropropane + H2O
?
-
substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
-
-
?
1,2,3-trichloropropane + H2O
?
-
-
-
-
?
1,2,3-trichloropropane + H2O
?
-
-
-
-
?
1,2,3-trichloropropane + H2O
?
-
low activity
-
-
?
1,2,3-trichloropropane + H2O
?
-
low activity
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloro-1-propanol + bromide
-
about 40% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloro-1-propanol + bromide
-
about 5% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
high activity
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
-
-
-
?
1,2-dibromo-3-chloropropane + H2O
2-bromo-3-chloropropanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromo-1-ethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromo-1-ethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromo-1-ethanol + bromide
-
about 25% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1,2-dibromoethane + H2O
2-bromo-1-ethanol + bromide
-
the highest specific activity of enzyme form eHLD-C is determined for 1,2-dibromoethane and 1-bromo-2-chloroethane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
1100% of the activity with 1-chlorobutane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
1100% of the activity with 1-chlorobutane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
42% of the activity with 4-chlorobutanol
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
about 45% of the activity compared to 4-bromobutyronitrile
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
about 45% of the specific activity compared to 1-bromohexane, enzyme form DmrB
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
about 90% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
strong dehalogenase activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
about 90% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
high activity
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
about 45% of the specific activity compared to 1-bromohexane, enzyme form DmrB
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
P51698
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
P51698
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
94% of the activity with 1,2-dichloroethane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
78% of the activity with 1,2-dichloroethane
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
about 15% of the activity compared to 4-bromobutyronitrile
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
low activity
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
low activity
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
-
-
-
?
1,2-dibromopropane + H2O
2-bromo-1-propanol + bromide
-
about 65% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,2-dibromopropane + H2O
2-bromopropan-1-ol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromopropan-1-ol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
high activity
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
low activity
-
-
?
1,2-dibromopropane + H2O
2-bromopropanol + bromide
-
-
-
-
?
1,2-dichloroethane + 2 H2O
1,2-ethanediol + 2 chloride
-
-
-
?
1,2-dichloroethane + 2 H2O
1,2-ethanediol + 2 chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloro-1-ethanol + chloride
-
less than 1% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,2-dichloroethane + H2O
2-chloro-1-ethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloro-1-ethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
low activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
highest activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
analysis of dynamic and electrostatic effects
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
highest activity
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
?
-
-
-
?
1,2-dichloroethane + H2O
?
-
-
-
?
1,2-dichloroethane + H2O
?
-
high activity
-
-
?
1,2-dichloroethane + H2O
?
-
high activity
-
-
?
1,2-dichloropropane + H2O
2-chloro-1-propanol + chloride
-
-
-
-
?
1,2-dichloropropane + H2O
2-chloro-1-propanol + chloride
-
based on the SN2 nucleophilic substitution mechanism, the dechlorination process is identified as the rate-determining step in LinB-catalyzed degradation of 1,2-dichloropropane. LinB is enantioselective when metabolizing the racemic mixture 1,2-dichloropropane. The overall activation barrier for degradation of (S)-1,2-dichloropropane is 5.2 kcal/mol higher than that of (R)-1,2-dichloropropane
-
-
?
1,2-dichloropropane + H2O
2-chloro-1-propanol + chloride
-
based on the SN2 nucleophilic substitution mechanism, the dechlorination process is identified as the rate-determining step in LinB-catalyzed degradation of 1,2-dichloropropane. LinB is enantioselective when metabolizing the racemic mixture 1,2-dichloropropane. The overall activation barrier for degradation of (S)-1,2-dichloropropane is 5.2 kcal/mol higher than that of (R)-1,2-dichloropropane
-
-
?
1,2-dichloropropane + H2O
2-chloro-1-propanol + chloride
-
less than 1% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
-
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
low activity
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
low activity
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
-
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
-
-
?
1,2-dichloropropane + H2O
?
-
-
-
-
?
1,2-dichloropropane + H2O
?
-
-
-
-
?
1,3,4,6-tetrachloro-1,4,cyclohexadiene + 2 H2O
2,5-dichloro-2,5-cyclohexadiene-1,4-diol + 2 chloride
-
-
-
-
?
1,3,4,6-tetrachloro-1,4,cyclohexadiene + 2 H2O
2,5-dichloro-2,5-cyclohexadiene-1,4-diol + 2 chloride
-
-
-
-
?
1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O
?
-
-
-
-
?
1,3,4,6-tetrachloro-1,4-cyclohexadiene + H2O
?
-
-
-
-
?
1,3-dibromo-2-methylpropane + H2O
3-bromo-2-methylpropan-1-ol + bromide
-
desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol
-
-
?
1,3-dibromo-2-methylpropane + H2O
3-bromo-2-methylpropan-1-ol + bromide
-
desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol
-
-
?
1,3-dibromo-2-phenylpropane + H2O
?
-
desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol
-
-
?
1,3-dibromo-2-phenylpropane + H2O
?
-
desymmetrisation of a dihaloalkane is followed by kinetic resolution of the chiral haloalcohol that is produced in the first step, increase of the enantiomeric excess of the respective haloalcohol
-
-
?
1,3-dibromo-2-propanol + H2O
3-bromo-1,2-propandiol
-
-
-
-
?
1,3-dibromo-2-propanol + H2O
3-bromo-1,2-propandiol
-
-
-
-
?
1,3-dibromo-2-propanol + H2O
3-bromo-1,2-propandiol
-
-
-
-
?
1,3-dibromopropane + 2 H2O
1,3-propanediol + 2 bromide
-
-
-
?
1,3-dibromopropane + 2 H2O
1,3-propanediol + 2 bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
best substrate, the release of product 3-bromo-1-propanol is the rate limiting step
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
about 40% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
the highest specific activity of enzyme form eHLD-B is determined for 1,3-dibromopropane and 1-bromo-3-chloropropane
-
-
?
1,3-dibromopropane + H2O
3-bromo-propanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromo-propanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
420% of the activity with 1-chlorobutane
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
700% of the activity with 1-chlorobutane
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
high activity
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
preferred substrate
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
?
1,3-dibromopropane + H2O
3-bromopropanol + bromide
-
-
-
?
1,3-dichloropropane + H2O
3-chloro-1-propanol + chloride
-
-
-
-
?
1,3-dichloropropane + H2O
3-chloro-1-propanol + chloride
-
about 10% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,3-dichloropropane + H2O
3-chloropropanol + chloride
-
-
-
?
1,3-dichloropropane + H2O
3-chloropropanol + chloride
-
-
-
?
1,3-dichloropropane + H2O
?
-
21% of the activity with 4-chlorobutanol
-
-
?
1,3-dichloropropane + H2O
?
-
21% of the activity with 4-chlorobutanol
-
-
?
1,3-dichloropropane + H2O
?
-
high activity
-
-
?
1,3-dichloropropane + H2O
?
-
80% of the activity with 1,2-dichloroethane
-
-
?
1,3-dichloropropane + H2O
?
-
high activity
-
-
?
1,3-diiodopropane + H2O
3-iodo-1-propanol + iodide
-
-
-
?
1,3-diiodopropane + H2O
3-iodo-1-propanol + iodide
about 25% of the activity compared to 4-bromobutyronitrile
-
-
?
1,3-diiodopropane + H2O
3-iodo-1-propanol + iodide
-
-
-
-
?
1,3-diiodopropane + H2O
3-iodo-1-propanol + iodide
-
4% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,3-diiodopropane + H2O
3-iodo-1-propanol + iodide
-
about 35% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1,3-diiodopropane + H2O
3-iodopropanol + iodide
-
-
-
?
1,3-diiodopropane + H2O
3-iodopropanol + iodide
-
-
-
?
1,3-diiodopropane + H2O
3-iodopropanol + iodide
-
-
-
-
?
1,3-diiodopropane + H2O
3-iodopropanol + iodide
-
-
-
-
?
1,5-dichloropentane + H2O
5-chloro-1-pentanol + chloride
-
low activity
-
-
?
1,5-dichloropentane + H2O
5-chloro-1-pentanol + chloride
-
-
-
-
?
1,5-dichloropentane + H2O
5-chloro-1-pentanol + chloride
-
3% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1,5-dichloropentane + H2O
5-chloro-1-pentanol + chloride
-
about 45% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
low activity
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
-
?
1,5-dichloropentane + H2O
5-chloropentanol + chloride
-
-
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
-
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
-
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
about 25% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
about 45% of the specific activity compared to 1-bromohexane, enzyme form DmrB
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
about 45% of the specific activity compared to 1-bromohexane, enzyme form DmrB
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
-
-
-
?
1,6-dibromohexane + H2O
6-bromohexanol + bromide
-
low activity
-
-
?
1,6-dichlorohexane + H2O
6-chlorohexanol + chloride
-
-
-
-
?
1,6-dichlorohexane + H2O
6-chlorohexanol + chloride
-
low activity
-
-
?
1-bromo-2-chloroethane + H2O
2-chloro-1-ethanol + bromide
-
about 10% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-bromo-2-chloroethane + H2O
2-chloro-1-ethanol + bromide
-
about 85% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
high activity
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
low activity
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
-
-
-
?
1-bromo-2-chloroethane + H2O
2-chloroethanol + bromide
-
high activity
-
-
?
1-bromo-2-methylpropane + H2O
2-methylpropanol + bromide
-
-
-
-
?
1-bromo-2-methylpropane + H2O
2-methylpropanol + bromide
-
-
-
-
?
1-bromo-3-chloropropane + H2O
3-chloro-1-propanol + bromide
about 25% of the activity compared to 4-bromobutyronitrile
-
-
?
1-bromo-3-chloropropane + H2O
3-chloro-1-propanol + bromide
-
about 75% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-bromo-3-chloropropane + H2O
3-chloro-1-propanol + bromide
-
about 80% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
-
-
-
?
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
high activity
-
-
?
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
-
-
-
-
?
1-bromo-3-chloropropane + H2O
3-chloropropanol + bromide
-
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
high activity
-
-
?
1-bromobutane + H2O
1-butanol + bromide
high activity
-
-
?
1-bromobutane + H2O
1-butanol + bromide
about 10% of the activity compared to 4-bromobutyronitrile
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
best substrate
-
-
?
1-bromobutane + H2O
1-butanol + bromide
strong dehalogenase activity
-
-
?
1-bromobutane + H2O
1-butanol + bromide
best substrate
-
-
?
1-bromobutane + H2O
1-butanol + bromide
preferred substrate
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
high activity
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
high activity
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
-
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
about 35% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-bromobutane + H2O
1-butanol + bromide
-
about 60% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-bromobutane + H2O
butanol + bromide
-
-
-
?
1-bromobutane + H2O
butanol + bromide
-
-
-
?
1-bromobutane + H2O
butanol + bromide
-
25% of the activity with 4-chlorobutanol
-
-
?
1-bromobutane + H2O
butanol + bromide
-
reaction in aqueous phase, 98% of the activity with 1-chlorobutane, reaction in gaseous phase, 98% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
butanol + bromide
-
reaction in aqueous phase, 98% of the activity with 1-chlorobutane, reaction in gaseous phase, 98% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
180% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
180% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
630% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
630% of the activity with 1-chlorobutane
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
-
-
-
?
1-bromobutane + H2O
n-butanol + bromide
-
-
-
?
1-bromodecane + H2O
1-decanol + bromide
-
-
-
?
1-bromodecane + H2O
1-decanol + bromide
-
-
-
?
1-bromododecane + H2O
1-dodecanol + bromide
-
-
-
?
1-bromododecane + H2O
1-dodecanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
highest activity
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
the enzyme shows highest activity toward 1-bromohexane
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
best substrate
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
about 35% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
clearly preferred substrate
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
enzyme form DmrB
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
best substrate
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
high activity
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
highest activity
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
best substrate
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
4% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-bromohexane + H2O
1-hexanol + bromide
-
about 20% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-bromohexane + H2O
hexanol + bromide
-
-
-
-
?
1-bromohexane + H2O
hexanol + bromide
-
reaction in aqueous phase, 87% of the activity with 1-chlorobutane, reaction in gaseous phase, 301% of the activity with 1-chlorobutane
-
-
?
1-bromohexane + H2O
n-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
n-hexanol + bromide
-
-
-
?
1-bromohexane + H2O
n-hexanol + bromide
-
-
-
-
?
1-bromohexane + H2O
n-hexanol + bromide
-
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
-
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
-
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
low activity
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
about 15% of the specific activity compared to 1-bromohexane, enzyme form DmrB
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
about 85% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
strong dehalogenase activity
-
-
?
1-bromopentane + H2O
1-pentanol + bromide
-
-
-
?
1-bromopropane + H2O
1-propanol + bromide
-
-
-
?
1-bromopropane + H2O
1-propanol + bromide
-
-
-
?
1-bromopropane + H2O
1-propanol + bromide
about 60% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1-bromopropane + H2O
1-propanol + bromide
-
-
-
?
1-bromopropane + H2O
1-propanol + bromide
-
-
-
?
1-bromopropane + H2O
1-propanol + bromide
-
-
-
?
1-bromopropane + H2O
propanol + bromide
-
-
-
-
?
1-bromopropane + H2O
propanol + bromide
-
-
-
-
?
1-bromopropane + H2O
propanol + bromide
-
-
-
-
?
1-bromopropane + H2O
propanol + bromide
-
-
-
-
?
1-bromopropane + H2O
propanol + bromide
-
29% of the activity with 1,2-dichloroethane
-
-
?
1-chloro-2,2-dimethylpropane + H2O
2,2-dimethylpropan-1-ol + chloride
-
-
-
-
?
1-chloro-2,2-dimethylpropane + H2O
2,2-dimethylpropan-1-ol + chloride
-
-
-
-
?
1-chloro-2-(2-chloroethoxy)ethane + H2O
?
-
-
-
-
?
1-chloro-2-(2-chloroethoxy)ethane + H2O
?
-
-
-
-
?
1-chloro-2-methylpropane + H2O
2-methylpropanol + chloride
-
-
-
?
1-chloro-2-methylpropane + H2O
2-methylpropanol + chloride
-
20% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
less than 5% of the activity compared to 4-bromobutyronitrile
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
less than 1% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
1-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
22% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
22% of the activity with 4-chlorobutanol
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
r
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
r
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
r
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
P51698
-
-
-
r
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
P51698
-
-
-
r
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
r
1-chlorobutane + H2O
butanol + chloride
-
31% of the activity with 1,2-dichloroethane
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
?
1-chlorobutane + H2O
n-butanol + chloride
-
-
-
?
1-chlorodecane + H2O
decanol + chloride
-
-
-
?
1-chlorodecane + H2O
decanol + chloride
-
-
-
-
?
1-chlorodecane + H2O
decanol + chloride
-
-
-
-
?
1-chlorodecane + H2O
n-decanol + chloride
-
52% of the activity with 1-chlorobutane
-
-
?
1-chlorodecane + H2O
n-decanol + chloride
-
110% of the activity with 1-chlorobutane
-
-
?
1-chloroheptane + H2O
heptanol + chloride
-
22% of the activity with 4-chlorobutanol
-
-
?
1-chloroheptane + H2O
heptanol + chloride
-
-
-
-
?
1-chloroheptane + H2O
heptanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
-
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
-
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
-
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
low activity
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
-
about 20% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-chlorohexane + H2O
1-hexanol + chloride
-
less than 1% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
15% of the activity with 4-chlorobutanol
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
reaction in aqueous phase, 100% of the activity with 1-chlorobutane, reaction in gaseous phase, 194% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
reaction in aqueous phase, 100% of the activity with 1-chlorobutane, reaction in gaseous phase, 194% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
best substrate
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
best substrate
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
hexanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
210% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
210% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
110% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
110% of the activity with 1-chlorobutane
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
low activity
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
low activity
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
-
-
-
?
1-chlorohexane + H2O
n-hexanol + chloride
-
-
-
?
1-chlorooctane + H2O
octanol + chloride
-
-
-
?
1-chlorooctane + H2O
octanol + chloride
-
18% of the activity with 4-chlorobutanol
-
-
?
1-chlorooctane + H2O
octanol + chloride
-
-
-
-
?
1-chlorooctane + H2O
octanol + chloride
-
-
-
-
?
1-chloropentane + H2O
n-pentanol + chloride
-
140% of the activity with 1-chlorobutane
-
-
?
1-chloropentane + H2O
n-pentanol + chloride
-
120% of the activity with 1-chlorobutane
-
-
?
1-chloropentane + H2O
pentanol + chloride
-
20% of the activity with 4-chlorobutanol
-
-
?
1-chloropentane + H2O
pentanol + chloride
-
reaction in aqueous phase, 101% of the activity with 1-chlorobutane, reaction in gaseous phase, 186% of the activity with 1-chlorobutane
-
-
?
1-chloropentane + H2O
pentanol + chloride
-
reaction in aqueous phase, 101% of the activity with 1-chlorobutane, reaction in gaseous phase, 186% of the activity with 1-chlorobutane
-
-
?
1-chloropropane + H2O
propanol + chloride
-
-
-
-
?
1-chloropropane + H2O
propanol + chloride
-
-
-
-
?
1-chloropropane + H2O
propanol + chloride
-
5% of the activity with 4-chlorobutanol
-
-
?
1-chloropropane + H2O
propanol + chloride
-
5% of the activity with 4-chlorobutanol
-
-
?
1-chloropropane + H2O
propanol + chloride
-
-
-
-
?
1-chloropropane + H2O
propanol + chloride
-
-
-
-
?
1-chloropropane + H2O
propanol + chloride
-
51% of the activity with 1,2-dichloroethane
-
-
?
1-chloropropane + H2O
propanol + chloride
-
51% of the activity with 1,2-dichloroethane
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
subfamily HLD-I, substrates small, terminally halogenated
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
subfamily HLD-I, substrates small, terminally halogenated
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
subfamily HLD-III, unknown substrates
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-III, unknown substrates
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-II, substrates larger, beta-substituted
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
-
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
P51698
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-I, substrates small, terminally halogenated
-
-
?
1-haloalkane + H2O
primary alcohol + halide
-
-
-
-
?
1-haloalkane + H2O
primary alcohol + halide
-
-
-
-
?
1-haloalkane + H2O
primary alcohol + halide
-
-
-
-
?
1-haloalkane + H2O
primary alcohol + halide
-
-
-
?
1-haloalkane + H2O
primary alcohol + halide
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
low activity
-
-
?
1-iodobutane + H2O
1-butanol + iodide
about 5% of the activity compared to 4-bromobutyronitrile
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
about 50% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
4% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
about 25% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
1-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
butanol + iodide
-
-
-
?
1-iodobutane + H2O
butanol + iodide
-
-
-
?
1-iodobutane + H2O
butanol + iodide
-
-
-
?
1-iodobutane + H2O
butanol + iodide
-
12% of the activity with 4-chlorobutanol
-
-
?
1-iodobutane + H2O
butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
n-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
n-butanol + iodide
-
-
-
-
?
1-iodobutane + H2O
n-butanol + iodide
-
-
-
-
?
1-iodohexane + H2O
1-hexanol + iodide
-
-
-
?
1-iodohexane + H2O
1-hexanol + iodide
-
-
-
?
1-iodohexane + H2O
1-hexanol + iodide
-
2.5% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-iodohexane + H2O
1-hexanol + iodide
-
less than 1% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-iodohexane + H2O
hexanol + iodide
-
-
-
?
1-iodohexane + H2O
hexanol + iodide
-
-
-
-
?
1-iodohexane + H2O
n-hexanol + iodide
-
-
-
?
1-iodohexane + H2O
n-hexanol + iodide
-
-
-
?
1-iodohexane + H2O
n-hexanol + iodide
-
-
-
-
?
1-iodohexane + H2O
n-hexanol + iodide
-
-
-
-
?
1-iodopropane + H2O
1-propanol + iodide
-
-
-
?
1-iodopropane + H2O
1-propanol + iodide
about 10% of the activity compared to 4-bromobutyronitrile
-
-
?
1-iodopropane + H2O
1-propanol + iodide
-
-
-
?
1-iodopropane + H2O
1-propanol + iodide
-
-
-
?
1-iodopropane + H2O
1-propanol + iodide
about 50% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
1-iodopropane + H2O
1-propanol + iodide
-
-
-
-
?
1-iodopropane + H2O
1-propanol + iodide
-
5% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
1-iodopropane + H2O
1-propanol + iodide
-
about 15% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
1-iodopropane + H2O
propanol + iodide
-
-
-
?
1-iodopropane + H2O
propanol + iodide
-
-
-
?
1-iodopropane + H2O
propanol + iodide
-
-
-
?
1-iodopropane + H2O
propanol + iodide
-
-
-
?
1-iodopropane + H2O
propanol + iodide
-
-
-
-
?
1-iodopropane + H2O
propanol + iodide
-
-
-
-
?
1-iodopropane + H2O
propanol + iodide
-
14% of the activity with 1,2-dichloroethane
-
-
?
2,3,4,5,6-pentachlorocyclohexanol + H2O
2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
-
?
2,3,4,5,6-pentachlorocyclohexanol + H2O
2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
-
?
2,3,4,5,6-pentachlorocyclohexanol + H2O
2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
?
2,3,4,5,6-pentachlorocyclohexanol + H2O
2,3,5,6-tetrachlorocyclohexane-1,4-diol + chloride
-
-
-
?
2,3,4,5,6-pentachlorohexanol + H2O
tetrachlorocyclohexanediol + chloride
-
-
-
?
2,3,4,5,6-pentachlorohexanol + H2O
tetrachlorocyclohexanediol + chloride
-
-
-
-
?
2,3,4,5,6-pentachlorohexanol + H2O
tetrachlorocyclohexanediol + chloride
-
-
-
-
?
2,3,4,5,6-pentachlorohexanol + H2O
tetrachlorocyclohexanediol + chloride
-
-
-
-
?
2,3-dichloroprop-1-ene + H2O
?
-
-
-
?
2,3-dichloroprop-1-ene + H2O
?
about 15% of the activity compared to 4-bromobutyronitrile
-
-
?
2,3-dichloropropene + H2O
?
-
-
-
-
?
2,3-dichloropropene + H2O
?
-
about 15% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
2,3-dichloropropene + H2O
?
-
about 5% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
2-bromo-1-chloropropane + H2O
2-bromo-1-propanol + chloride
-
about 50% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
2-bromo-1-chloropropane + H2O
2-bromo-1-propanol + chloride
-
about 60% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
2-bromobutane + H2O
2-butanol + bromide
-
-
-
?
2-bromobutane + H2O
2-butanol + bromide
-
-
-
?
2-bromobutane + H2O
2-butanol + bromide
-
-
-
?
2-bromobutane + H2O
2-butanol + bromide
-
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
-
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
low activity
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
low activity
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
-
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
-
-
-
?
2-bromoethanol + H2O
ethanol + bromide
-
-
-
?
2-bromopentane + H2O
2-pentanol + bromide
-
-
-
?
2-bromopentane + H2O
2-pentanol + bromide
-
-
-
?
2-bromopentane + H2O
2-pentanol + bromide
-
-
-
?
2-chlorobutane + H2O
2-butanol + chloride
-
-
-
-
?
2-chlorobutane + H2O
2-butanol + chloride
-
-
-
-
?
2-iodobutane + H2O
2-butanol + iodide
-
-
-
?
2-iodobutane + H2O
2-butanol + iodide
-
-
-
-
?
2-iodobutane + H2O
2-butanol + iodide
-
-
-
-
?
2-iodobutane + H2O
2-butanol + iodide
-
-
-
-
?
2-iodobutane + H2O
2-butanol + iodide
-
3% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
2-iodobutane + H2O
2-butanol + iodide
-
7.5% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + H2O
2,5,6-trichloro-2-cyclohexene-1,4-diol + chloride
-
-
-
-
?
3,4,5,6-tetrachloro-2-cyclohexene-1-ol + H2O
2,5,6-trichloro-2-cyclohexene-1,4-diol + chloride
-
-
-
-
?
3-chloro-2-methylprop-1-ene + H2O
?
-
-
-
?
3-chloro-2-methylprop-1-ene + H2O
?
about 5% of the activity compared to 4-bromobutyronitrile
-
-
?
3-chloro-2-methylprop-1-ene + H2O
?
-
-
-
-
?
3-chloro-2-methylpropene + H2O
2-methylpropene-3-ol + chloride
-
320% of the activity with 1-chlorobutane
-
-
?
3-chloro-2-methylpropene + H2O
2-methylpropene-3-ol + chloride
-
320% of the activity with 1-chlorobutane
-
-
?
3-chloro-2-methylpropene + H2O
2-methylpropene-3-ol + chloride
-
270% of the activity with 1-chlorobutane
-
-
?
3-chloro-2-methylpropene + H2O
2-methylpropene-3-ol + chloride
-
270% of the activity with 1-chlorobutane
-
-
?
3-chloro-2-methylpropene + H2O
2-methylpropene-3-ol + chloride
-
-
-
-
?
3-chloro-2-methylpropene + H2O
?
high activity
-
-
?
3-chloro-2-methylpropene + H2O
?
-
low activity
-
-
?
3-chloro-2-methylpropene + H2O
?
-
about 15% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
3-chloro-2-methylpropene + H2O
?
-
about 15% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
-
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
best substrate
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
-
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
low activity
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
high activity
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
strong dehalogenase activity
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
-
about 25% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
4-bromobutyronitrile + H2O
4-hydroxybutyronitrile + bromide
-
about 75% of the activity compared to 1,3-dibromopropane, enzyme form eHLD-B
-
-
?
4-bromobutyronitrile + H2O
?
high activity
-
-
?
4-bromobutyronitrile + H2O
?
-
-
-
-
?
4-bromobutyronitrile + H2O
?
-
-
-
-
?
4-bromobutyronitrile + H2O
? + bromide
about 20% of the specific activity compared to 1-bromohexane, enzyme form DmrB
-
-
?
4-bromobutyronitrile + H2O
? + bromide
about 85% of the specific activity compared to 1-bromobutane, enzyme form DmrA
-
-
?
alpha-hexachlorocyclohexane + H2O
beta-pentachlorocyclohexene + chloride
-
-
-
-
?
alpha-hexachlorocyclohexane + H2O
beta-pentachlorocyclohexene + chloride
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
no further degradation of product
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
no further degradation of product
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
no further degradation of product
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
no further degradation of product
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
two-step conversion of beta-HCH to TCDL
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
two-step conversion of beta-HCH to TCDL
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
ratio kcat/KM is two orders of magnitude lower than for best substrate 1-chlorohexane. Product is not further degraded
-
-
?
beta-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
ratio kcat/KM is two orders of magnitude lower than for best substrate 1-chlorohexane. Product is not further degraded
-
-
?
beta-hexachlorocyclohexane + H2O
?
-
-
-
-
?
beta-hexachlorocyclohexane + H2O
?
-
-
-
-
?
bis(2-chloroethyl)ether + H2O
?
high activity
-
-
?
bis(2-chloroethyl)ether + H2O
?
-
4% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
84% of the activity with 1-chlorobutane
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
about 20% of the activity compared to 4-bromobutyronitrile
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
420% of the activity with 1-chlorobutane
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
420% of the activity with 1-chlorobutane
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
low activity
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
low activity
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
low activity
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
-
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
4% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
bromocyclohexane + H2O
cyclohexanol + bromide
-
-
-
-
?
bromoethane + H2O
ethanol + bromide
-
32% of the activity with 4-chlorobutanol
-
-
?
bromoethane + H2O
ethanol + bromide
-
32% of the activity with 4-chlorobutanol
-
-
?
bromoethane + H2O
ethanol + bromide
-
24% of the activity with 1,2-dichloroethane
-
-
?
chlorocyclohexane + H2O
cyclohexanol + chloride
-
30% of the activity with 1-chlorobutane
-
-
?
chlorocyclohexane + H2O
cyclohexanol + chloride
-
620% of the activity with 1-chlorobutane
-
-
?
chlorocyclohexane + H2O
cyclohexanol + chloride
-
-
-
-
?
chlorocyclopentane + H2O
cyclopentanol + chloride
-
-
-
?
chlorocyclopentane + H2O
cyclopentanol + chloride
-
high activity
-
-
?
chlorocyclopentane + H2O
cyclopentanol + chloride
about 10% of the activity compared to 4-bromobutyronitrile
-
-
?
chlorocyclopentane + H2O
cyclopentanol + chloride
-
-
-
-
?
chlorocyclopentane + H2O
cyclopentanol + chloride
-
about 10% of the activity compared to 1,2-dibromoethane, enzyme form eHLD-C
-
-
?
chloroethane + H2O
ethanol + chloride
-
24% of the activity with 1,2-dichloroethane
-
-
?
chloroethane + H2O
ethanol + chloride
-
24% of the activity with 1,2-dichloroethane
-
-
?
chloromethane + H2O
methanol + chloride
-
28% of the activity with 1,2-dichloroethane
-
-
?
chloromethane + H2O
methanol + chloride
-
28% of the activity with 1,2-dichloroethane
-
-
?
dibromomethane + H2O
bromomethanol + bromide
-
-
-
?
dibromomethane + H2O
bromomethanol + bromide
-
71% of the activity with 1,2-dichloroethane
-
-
?
dichloromethane + H2O
? + chloride
-
-
-
-
?
dichloromethane + H2O
? + chloride
-
-
-
-
?
dichloromethane + H2O
? + chloride
-
-
-
-
?
dichloromethane + H2O
? + chloride
-
-
-
-
?
dichloromethane + H2O
? + chloride
-
-
-
-
?
epsilon-hexachlorocyclohexane + H2O
pentachlorocyclohexanol + tetrachlorocyclohexane-1,4-diol + chloride
-
reaction modeling, overview
-
-
?
epsilon-hexachlorocyclohexane + H2O
pentachlorocyclohexanol + tetrachlorocyclohexane-1,4-diol + chloride
-
reaction modeling, overview
-
-
?
ethyl 2-bromobutyrate + H2O
?
-
-
-
?
ethyl 2-bromobutyrate + H2O
?
-
-
-
?
gamma-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
-
?
gamma-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
no further degradation of product
-
?
gamma-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
no further degradation of product
-
?
gamma-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
no further degradation of product
-
?
gamma-hexachlorocyclohexane + H2O
2,3,4,5,6-pentachlorocyclohexanol + chloride
-
-
no further degradation of product
-
?
gamma-hexachlorocyclohexane + H2O
?
-
-
-
-
?
gamma-hexachlorocyclohexane + H2O
?
-
-
-
?
gamma-hexachlorocyclohexane + H2O
?
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
overview
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
substrate range includes at least 50 halogenated compounds, 1-chloroalkanes C3 to C10, 1-bromoalkanes C1 to C9, 1-iodoalkanes C1 to C7, no 1-fluoroalkane, subterminally substituted, branched-chain and non-saturated haloalkanes, halogenated aromatic substrates, e.g. bromobenzene and benzyl bromide, several alpha,omega-dihaloalkanes are subject to double dehalogenation
-
-
?
haloalkane + H2O
alcohol + halide
-
overview
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
substrate range includes at least 50 halogenated compounds, 1-chloroalkanes C3 to C10, 1-bromoalkanes C1 to C9, 1-iodoalkanes C1 to C7, no 1-fluoroalkane, subterminally substituted, branched-chain and non-saturated haloalkanes, halogenated aromatic substrates, e.g. bromobenzene and benzyl bromide, several alpha,omega-dihaloalkanes are subject to double dehalogenation
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
overview
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
highest activity towards alpha,omega disubstituted chloro-C2-C6 and bromo-C2-C6 alkanes and 4-chlorobutanol
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
overview
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
highest activity towards alpha,omega disubstituted chloro-C2-C6 and bromo-C2-C6 alkanes and 4-chlorobutanol
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
comparison of substrate specificities and classification
-
-
?
haloalkane + H2O
alcohol + halide
-
comparison of substrate specificities and classification
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
comparison of substrate specificities and classification
-
-
?
haloalkane + H2O
alcohol + halide
-
alpha,omega-dihalogenated ethanes, preference for long-chain haloalkanes
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
alpha,omega-dihalogenated ethanes, preference for long-chain haloalkanes
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
comparison of substrate specificities and classification
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
n-halogenated C1 to C4 alkanes, including chlorinated, brominated and iodinated compounds
-
?
haloalkane + H2O
alcohol + halide
-
comparison of substrate specificities and classification
-
-
?
haloalkane + H2O
alcohol + halide
comparison of substrate specificities and classification
-
-
?
haloalkane + H2O
alcohol + halide
-
n-halogenated C1 to C4 alkanes, including chlorinated, brominated and iodinated compounds
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
broad specificity
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
?
haloalkane + H2O
alcohol + halide
comparison of substrate specificities and classification
-
-
?
meso-2,3-dibromobutane + H2O
?
-
-
-
-
?
meso-2,3-dibromobutane + H2O
?
-
-
-
-
?
monochloroacetic acid + H2O
glycolate + chloride
-
-
-
-
?
monochloroacetic acid + H2O
glycolate + chloride
-
-
-
-
?
monochloroacetic acid + H2O
glycolate + chloride
-
-
-
-
?
monochloroacetic acid + H2O
glycolate + chloride
-
-
-
-
?
monochloroacetic acid + H2O
glycolate + chloride
-
-
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
broad substrate range
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
broad substrate range
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
broad substrate range
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
broad substrate range
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
broad substrate range
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
broad substrate range
-
-
?
rac-1,3-dibromobutane + H2O
(S)-butane-1,3-diol + bromide
hydrolytic dehalogenation of rac-1,3-dibromobutane proceeds in a sequential fashion: initial formation of intermediate haloalcohols followed by a second hydrolytic step to produce the final diol. Intermediate haloalcohols formed with moderate to good enantiomeric excess ((S)-4-bromobutan-2-ol: up to 87%). (S)-butane-1,3-diol is formed at a maximum enantiomeric excess of 35% before full hydrolysis furnished the racemic diol product
-
-
?
rac-1,3-dibromobutane + H2O
(S)-butane-1,3-diol + bromide
hydrolytic dehalogenation of rac-1,3-dibromobutane proceeds in a sequential fashion: initial formation of intermediate haloalcohols followed by a second hydrolytic step to produce the final diol. Intermediate haloalcohols formed with moderate to good enantiomeric excess ((S)-4-bromobutan-2-ol: up to 87%). (S)-butane-1,3-diol is formed at a maximum enantiomeric excess of 35% before full hydrolysis furnished the racemic diol product
-
-
?
tetrachloromethane + H2O
? + chloride
-
-
-
-
?
tetrachloromethane + H2O
? + chloride
-
-
-
-
?
tetrachloromethane + H2O
? + chloride
-
-
-
-
?
tetrachloromethane + H2O
? + chloride
-
-
-
-
?
tetrachloromethane + H2O
? + chloride
-
-
-
-
?
trichloroacetic acid + H2O
? + chloride
-
-
-
-
?
trichloroacetic acid + H2O
? + chloride
-
-
-
-
?
trichloroacetic acid + H2O
? + chloride
-
-
-
-
?
trichloroacetic acid + H2O
? + chloride
-
-
-
-
?
trichloroacetic acid + H2O
? + chloride
-
-
-
-
?
trichloromethane + H2O
? + chloride
-
-
-
-
?
trichloromethane + H2O
? + chloride
-
-
-
-
?
trichloromethane + H2O
? + chloride
-
-
-
-
?
trichloromethane + H2O
? + chloride
-
-
-
-
?
trichloromethane + H2O
? + chloride
-
-
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
DatA shows excellent enantioselectivity toward racemic mixtures of chiral brominated alkanes and esters, racemic beta-bromoalkanes and alpha-bromoesters, overview. No activity with methyl and ethyl 2-bromobutyrate
-
-
?
additional information
?
-
enzyme DatA hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton
-
-
?
additional information
?
-
substrate specificity, substrate docking and molecular modelling, overview. No activity with 2,3-dichloropropene, chlorocyclohexane, 1,2,3-trichloropropane, 1,2-dichloropropane, and 1,2-dichloroethane
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
enzyme DatA hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton
-
-
?
additional information
?
-
DatA shows excellent enantioselectivity toward racemic mixtures of chiral brominated alkanes and esters, racemic beta-bromoalkanes and alpha-bromoesters, overview. No activity with methyl and ethyl 2-bromobutyrate
-
-
?
additional information
?
-
substrate specificity, substrate docking and molecular modelling, overview. No activity with 2,3-dichloropropene, chlorocyclohexane, 1,2,3-trichloropropane, 1,2-dichloropropane, and 1,2-dichloroethane
-
-
?
additional information
?
-
enzyme DadB possesses broad substrate range and has the highest overall activity among the identified haloalkanes dehalogenases. The enzyme prefers brominated substrates, chlorinated alkenes, and the C2-C3 substrates, including the persistent pollutants of 1,2-dichloroethane, 1,2-dichloropropane and 1,2,3-trichloropropane, but displays no detectable activity toward long-chain haloalkanes such as 1-chlorohexadecane and 1-chlorooctadecane
-
-
?
additional information
?
-
-
enzyme DadB possesses broad substrate range and has the highest overall activity among the identified haloalkanes dehalogenases. The enzyme prefers brominated substrates, chlorinated alkenes, and the C2-C3 substrates, including the persistent pollutants of 1,2-dichloroethane, 1,2-dichloropropane and 1,2,3-trichloropropane, but displays no detectable activity toward long-chain haloalkanes such as 1-chlorohexadecane and 1-chlorooctadecane
-
-
?
additional information
?
-
the enzyme DadB prefers brominated substrates over than their chlorinated and iodinated counterparts, its activities against brominated C1-C4 substrates are generally 20 times higher than the corresponding chlorinated substrates. In the case of halogenated butane, the activities are 1-bromobutane > 1-iodobutane > 1-chlorobutane. For 1,3-dihalogenated propane, the activities are 1,3-dibromopropane > 1-chloro-3-bromopropane > 1,3-dichloropropane > 1,3-diiodopropane. The activity of enzyme DadB against chlorinated alkenes, such as 2,3-dichloroprop-1-ene, 3-chloro-2-methylprop-1-ene, 1,3-dichloropropene, and 1,2,3-trichloropropene, is higher than the corresponding chlorinated alkanes. Substrate specificity, overview. No activity with 2-iodobutane, chlorocyclohexane, 1-chlorohexadecane, 1-bromohexadecane, 1-chlorooctadecane, trichloromethane, 1-chloro-3-nitrobenzene, 4-bromodiphenyl ether, decabromodiphenyl, and trichloroacetic acid
-
-
?
additional information
?
-
-
the enzyme DadB prefers brominated substrates over than their chlorinated and iodinated counterparts, its activities against brominated C1-C4 substrates are generally 20 times higher than the corresponding chlorinated substrates. In the case of halogenated butane, the activities are 1-bromobutane > 1-iodobutane > 1-chlorobutane. For 1,3-dihalogenated propane, the activities are 1,3-dibromopropane > 1-chloro-3-bromopropane > 1,3-dichloropropane > 1,3-diiodopropane. The activity of enzyme DadB against chlorinated alkenes, such as 2,3-dichloroprop-1-ene, 3-chloro-2-methylprop-1-ene, 1,3-dichloropropene, and 1,2,3-trichloropropene, is higher than the corresponding chlorinated alkanes. Substrate specificity, overview. No activity with 2-iodobutane, chlorocyclohexane, 1-chlorohexadecane, 1-bromohexadecane, 1-chlorooctadecane, trichloromethane, 1-chloro-3-nitrobenzene, 4-bromodiphenyl ether, decabromodiphenyl, and trichloroacetic acid
-
-
?
additional information
?
-
enzyme DadB possesses broad substrate range and has the highest overall activity among the identified haloalkanes dehalogenases. The enzyme prefers brominated substrates, chlorinated alkenes, and the C2-C3 substrates, including the persistent pollutants of 1,2-dichloroethane, 1,2-dichloropropane and 1,2,3-trichloropropane, but displays no detectable activity toward long-chain haloalkanes such as 1-chlorohexadecane and 1-chlorooctadecane
-
-
?
additional information
?
-
the enzyme DadB prefers brominated substrates over than their chlorinated and iodinated counterparts, its activities against brominated C1-C4 substrates are generally 20 times higher than the corresponding chlorinated substrates. In the case of halogenated butane, the activities are 1-bromobutane > 1-iodobutane > 1-chlorobutane. For 1,3-dihalogenated propane, the activities are 1,3-dibromopropane > 1-chloro-3-bromopropane > 1,3-dichloropropane > 1,3-diiodopropane. The activity of enzyme DadB against chlorinated alkenes, such as 2,3-dichloroprop-1-ene, 3-chloro-2-methylprop-1-ene, 1,3-dichloropropene, and 1,2,3-trichloropropene, is higher than the corresponding chlorinated alkanes. Substrate specificity, overview. No activity with 2-iodobutane, chlorocyclohexane, 1-chlorohexadecane, 1-bromohexadecane, 1-chlorooctadecane, trichloromethane, 1-chloro-3-nitrobenzene, 4-bromodiphenyl ether, decabromodiphenyl, and trichloroacetic acid
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
DbeA is less active and has a higher specificity towards brominated and iodinated compounds compared with DbjA
-
-
?
additional information
?
-
-
DbeA is less active and has a higher specificity towards brominated and iodinated compounds compared with DbjA
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
DjA has a high catalytic activity for beta-methylated haloalkanes
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview
-
-
?
additional information
?
-
the pH does not have any effect on enantiodiscriminination of DbjA, but a decrease in temperature results in significantly enhanced enantioselectivity
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
the pH does not have any effect on enantiodiscriminination of DbjA, but a decrease in temperature results in significantly enhanced enantioselectivity
-
-
?
additional information
?
-
no activity with 1-chlorobutane, 1,2-dichloroethane and 1,2-dichloropropane
-
-
-
additional information
?
-
-
no activity with 1-chlorobutane, 1,2-dichloroethane and 1,2-dichloropropane
-
-
-
additional information
?
-
the enzyme shows high activity with both long brominated and chlorinated alkanes. No activity with: 1-chlorobutane, 1,2-dichloroethane, 1,2-dichloropropane
-
-
-
additional information
?
-
-
the enzyme shows high activity with both long brominated and chlorinated alkanes. No activity with: 1-chlorobutane, 1,2-dichloroethane, 1,2-dichloropropane
-
-
-
additional information
?
-
no activity with 1-chlorobutane, 1,2-dichloroethane and 1,2-dichloropropane
-
-
-
additional information
?
-
the enzyme shows high activity with both long brominated and chlorinated alkanes. No activity with: 1-chlorobutane, 1,2-dichloroethane, 1,2-dichloropropane
-
-
-
additional information
?
-
the enzyme prefers brominated substrates over chlorinated and iodinated substrates. Moderate to high enantioselectivity with a preference for the (R) enantiomer is observed for brominated esters with the highest E value of 106 achieved with ethyl-2-bromopropionate. Negligible enantioselectivity is observed with either of the tested brominated n-alkanes
-
-
-
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,2,3-trichloropropane, 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,2,3-trichloropropane, 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
no or poor activity with 1,1,2-trichloroethane and chloroform
-
-
?
additional information
?
-
no or poor activity with 1,1,2-trichloroethane and chloroform
-
-
?
additional information
?
-
no or poor activity with chloroform
-
-
?
additional information
?
-
no or poor activity with chloroform
-
-
?
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates
-
-
-
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates
-
-
-
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates, enzyme form DmrA
-
-
-
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates, enzyme form DmrA
-
-
-
additional information
?
-
enzyme DmrA is active against mono- and dihalogenated alkanes up to six carbons in length and favours brominated species over iodinated or chlorinated ones and linear substrates over cyclic ones
-
-
-
additional information
?
-
enzyme DmrA is active against mono- and dihalogenated alkanes up to six carbons in length and favours brominated species over iodinated or chlorinated ones and linear substrates over cyclic ones
-
-
-
additional information
?
-
no activity with chloroform
-
-
-
additional information
?
-
no activity with chloroform
-
-
-
additional information
?
-
no activity with chloroform and 1,1,2-trichloroethane
-
-
-
additional information
?
-
no activity with chloroform and 1,1,2-trichloroethane
-
-
-
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates, enzyme form DmrA
-
-
-
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates, enzyme form DmrA
-
-
-
additional information
?
-
enzyme DmrA is active against mono- and dihalogenated alkanes up to six carbons in length and favours brominated species over iodinated or chlorinated ones and linear substrates over cyclic ones
-
-
-
additional information
?
-
enzyme DmrA is active against mono- and dihalogenated alkanes up to six carbons in length and favours brominated species over iodinated or chlorinated ones and linear substrates over cyclic ones
-
-
-
additional information
?
-
no activity with chloroform and 1,1,2-trichloroethane
-
-
-
additional information
?
-
no activity with chloroform and 1,1,2-trichloroethane
-
-
-
additional information
?
-
no or poor activity with 1,1,2-trichloroethane and chloroform
-
-
?
additional information
?
-
no or poor activity with 1,1,2-trichloroethane and chloroform
-
-
?
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates
-
-
-
additional information
?
-
active against C2-C6 haloalkanes, with a preference for brominated linear substrates
-
-
-
additional information
?
-
no activity with chloroform
-
-
-
additional information
?
-
no activity with chloroform
-
-
-
additional information
?
-
no or poor activity with chloroform
-
-
?
additional information
?
-
no or poor activity with chloroform
-
-
?
additional information
?
-
DppA shows high preference for 1-bromobutane and does not accept chlorinated alkanes, haloacids, or haloalcohols, substrate specificity, overview
-
-
?
additional information
?
-
no activity with chlorinated compounds
-
-
?
additional information
?
-
-
substrate specificity profiles of DpcA, DpcA prefers brominated or iodinated substrates over chlorinated ones, overview
-
-
?
additional information
?
-
-
substrate specificity profiles of DpcA, DpcA prefers brominated or iodinated substrates over chlorinated ones, overview
-
-
?
additional information
?
-
-
no activity with 1,2-dichloroethane, 1,2-dichloropropane, and 1,2-dichloro-3-propanol
-
-
?
additional information
?
-
-
no substrate: 1-chlorodecane, 2-chlorobutane
-
-
?
additional information
?
-
-
no substrate: 1-chlorodecane, 2-chlorobutane
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview
-
-
?
additional information
?
-
development and evaluation of a high-throughput system to select active haloalkane dehalogenase variants from a large mutant library, enrichment of the active wild-type enzyme in contrast to the inactive variants is about 340fold
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with 1,2,3-tribromopropane, 3-bromo-1-propanol, 1,2-dibromopropane, 1-chlorohexane, 1-chlorobutane, 1,2-dichloroethane and 1,2-dichloropropane
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
gamma-hexachlorocyclohexane is not a substrate for LinB
-
-
?
additional information
?
-
-
various metabolites are formed from minor components of technical hexachlorocyclohexane mixtures, GC-MS analysis, overview
-
-
?
additional information
?
-
-
gamma-hexachlorocyclohexane is not a substrate for LinB
-
-
?
additional information
?
-
-
various metabolites are formed from minor components of technical hexachlorocyclohexane mixtures, GC-MS analysis, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity is influenced by the size and shape of their entrance tunnel, surface residue Leu177 is involved and located at the tunnel opening
-
-
?
additional information
?
-
-
quantitative analysis of substrate specificity
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview
-
-
?
additional information
?
-
-
quantitative analysis of substrate specificity
-
-
?
additional information
?
-
-
substrate specificity is influenced by the size and shape of their entrance tunnel, surface residue Leu177 is involved and located at the tunnel opening
-
-
?
additional information
?
-
-
the enzyme shows a preference for terminally brominated hydrocarbons and enantioselectivity towards beta-brominated alkanes
-
-
?
additional information
?
-
-
substrate specificity profile of DspA, overview. No activity with 1-chlorobutane, 1-chlorohexane, 1,2-dichloroethane, 1,3-dichloropropane, 1,2-dichloropropane, 1,2,3-trichloropropane, bis(2-chlorethyl)ether, chlorocyclohexane, and bromocyclohexane. Medium enantioselectivity is observed with 2-bromobutane and 2-bromopentane, while none or very low enantioselectivity wi observed with methyl 2-bromobutyrate and ethyl 2-bromobutyrate
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity analysis, overview
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane
-
-
?
additional information
?
-
development and evaluation of a high-throughput system to select active haloalkane dehalogenase variants from a large mutant library, enrichment of the active wild-type enzyme in contrast to the inactive variants is about 340fold
-
-
?
additional information
?
-
-
the enzyme catalyses the conversion of prochiral short-chain dihaloalkanes and a meso dihaloalkane, yielding enantioenriched haloalcohols, single enzyme tandem conversion of a prochiral or meso dihaloalkane to chiral haloalcohol and prochiral or meso diol, substrate specificity, overview. Poor activity with 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity analysis, overview
-
-
?
additional information
?
-
-
substrate specificity analysis, overview
-
-
?
additional information
?
-
the bifunctioal enzyme also shows epoxidase activity
-
-
-
additional information
?
-
-
the bifunctioal enzyme also shows epoxidase activity
-
-
-
additional information
?
-
the bifunctioal enzyme also shows epoxidase activity
-
-
-
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0.00066
1,2-dichloroethane
0.0007
-
substrate 1,2-dichloroethane
0.00072
1,2-dichloroethane
0.0016
-
substrate 1,2-dichloropropane
0.004
-
purified recombinant His6-tagged LinB, substrate gamma-hexachlorocyclohexane, pH 8.3, 22°C
0.012
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chlorotetradecane
0.018
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chlorododecane
0.024
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chloro-2-methylpropane
0.06
pH 8.6, 37°C, purified recombinant enzyme, substrate dichloromethane
0.084
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chlorodecane
0.16
-
purified recombinant wild-type enzyme, substrate chlorocyclohexane
0.28
pH 8.6, 37°C, purified recombinant enzyme, substrate (bromomethyl)cyclohexane
0.31
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2-dichloropropane
0.34
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2,3-trichloropropane
0.702
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2-dichloroethane
0.76
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chlorohexane
0.862
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-bromohexane
0.864
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,5-dichloropentane
0.92
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-iodohexane
1.11
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chlorobutane
1.48
pH 8.6, 37°C, purified recombinant enzyme, substrate bromocyclohexane
1.54
-
purified recombinant wild-type enzyme, substrate 1-iodobutane
1.57
-
purified recombinant wild-type enzyme, substrate 1-chlorohexane
1.61
-
purified recombinant wild-type enzyme, substrate bromocyclohexane
1.86
P51698
substrate 1-chlorobutane, 37°C, pH 8.6
1.88
-
purified recombinant wild-type enzyme, substrate 1-chlorobutane
10.3
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,3-dibromopropane
105
-
substrate tetrachloromethane, 35°C, pH 9.0, activity of crude extract
108
-
substrate dichloromethane, 35°C, pH 9.0, activity of crude extract
11.53
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-bromo-2-chloroethane
12.2
-
substrate: 1,2-dibromoethane, enzyme form eHLD-C, pH and temperature not specified in the publication
12.3
-
purified recombinant wild-type enzyme, substrate 1,2-dibromoethane
12.66
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chlorooctane
13.54
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,3-dichloropropene
14.05
pH 8.6, 37°C, purified recombinant enzyme, substrate 2,3-dichloroprop-1-ene
14.16
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2-dibromoethane
14.44
pH 8.6, 37°C, purified recombinant enzyme, substrate 4-bromobutyronitrile
15.13
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2,3-tribromopropane
15.6
P51698
substrate 1,2-dibromoethane, 37°C, pH 8.6
151
-
substrate tetrachloromethane, 35°C, pH 7.5, activity of crude extract
166
-
substrate 1,2-dichloroethane, 35°C, pH 9.0, activity of crude extract
175
-
substrate dichloromethane, 35°C, pH 7.5, activity of crude extract
2.18
-
purified recombinant wild-type enzyme, substrate 1,3-diiodopropane
211
-
substrate 1,2-dichloroethane, 35°C, pH 9.0, activity of crude extract
235
-
substrate trichloroacetic acid, 35°C, pH 9.0, activity of crude extract
24.05
pH 8.6, 37°C, purified recombinant enzyme, substrate 3-chloro-2-methylprop-1-ene
247
-
substrate trichloroacetic acid, 35°C, pH 9.0, activity of crude extract
26.48
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2,3-trichloropropene
270
-
substrate 1,2-dichloroethane, 35°C, pH 7.5, activity of crude extract
294
-
substrate 1,2-dichloroethane, 35°C, pH 7.5, activity of crude extract
3.04
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-iodobutane
3.33
-
purified recombinant wild-type enzyme, substrate 1-bromoobutane
3.54
pH 8.6, 37°C, purified recombinant enzyme, substrate chlorocyclopentane
3.63
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-chloro-2-(2-chloroethoxy)ethane
3.88
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-iodopropane
317
-
substrate monochloroacetic acid, 35°C, pH 9.0, activity of crude extract
329
-
substrate monochloroacetic acid, 35°C, pH 9.0, activity of crude extract
346
-
substrate monochloroacetic acid, 35°C, pH 9.0, activity of crude extract
352
-
substrate monochloroacetic acid, 35°C, pH 9.0, activity of crude extract
4.09
-
substrate 1-chlorobutane
4.51
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-bromobutane
4.86
-
substrate: 1,3-dibromopropane, enzyme form eHLD-B, pH and temperature not specified in the publication
40
-
substrate trichloroacetic acid, 35°C, pH 7.5, activity of crude extract
5.33
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,3-dichloropropane
59
-
substrate trichloroacetic acid, 35°C, pH 7.5, activity of crude extract
66
-
substrate trichloroethane, 35°C, pH 9.0, activity of crude extract
7.48
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2-dibromopropane
8.03
-
purified recombinant wild-type enzyme, substrate 3-chloro-2-methylpropene
8.14
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,2-dibromo-3-chloropropane
8.3
pH 8.6, 37°C, purified recombinant enzyme, substrate 2-bromo-1-chloropropane
88
-
substrate trichloroacetic acid, 35°C, pH 7.5, activity of crude extract
9.92
pH 8.6, 37°C, purified recombinant enzyme, substrate 1-bromo-3-chloropropane
92.3
purified recombinant enzyme, substrate 1,2-dichloroethane, pH 9.0, 37°C
96
-
substrate trichloromethane, 35°C, pH 9.0, activity of crude extract
106
-
substrate trichloroethane, 35°C, pH 7.5, activity of crude extract
106
-
substrate monochloroacetic acid, 35°C, pH 7.5, activity of crude extract
106
-
substrate dichloromethane, 35°C, pH 9.0, activity of crude extract
106
-
substrate trichloromethane, 35°C, pH 9.0, activity of crude extract
117
-
substrate trichloromethane, 35°C, pH 9.0, activity of crude extract
117
-
substrate tetrachloromethane, 35°C, pH 9.0, activity of crude extract
117
-
substrate trichloroethane, 35°C, pH 7.5, activity of crude extract
129
-
substrate trichloroethane, 35°C, pH 7.5, activity of crude extract
129
-
substrate dichloromethane, 35°C, pH 9.0, activity of crude extract
130
-
substrate trichloromethane, 35°C, pH 9.0, activity of crude extract
130
-
substrate trichloroethane, 35°C, pH 7.5, activity of crude extract
130
-
substrate trichloromethane, 35°C, pH 9.0, activity of crude extract
141
-
substrate dichloromethane, 35°C, pH 9.0, activity of crude extract
141
-
substrate trichloroethane, 35°C, pH 7.5, activity of crude extract
141
-
substrate tetrachloromethane, 35°C, pH 7.5, activity of crude extract
153
-
substrate trichloromethane, 35°C, pH 7.5, activity of crude extract
153
-
substrate 1,2-dichloroethane, 35°C, pH 9.0, activity of crude extract
153
-
substrate dichloromethane, 35°C, pH 7.5, activity of crude extract
153
-
substrate dichloromethane, 35°C, pH 7.5, activity of crude extract
153
-
substrate tetrachloromethane, 35°C, pH 7.5, activity of crude extract
164
-
substrate 1,2-dichloroethane, 35°C, pH 9.0, activity of crude extract
164
-
substrate dichloromethane, 35°C, pH 7.5, activity of crude extract
164
-
substrate trichloromethane, 35°C, pH 7.5, activity of crude extract
176
-
substrate tetrachloromethane, 35°C, pH 7.5, activity of crude extract
176
-
substrate trichloromethane, 35°C, pH 7.5, activity of crude extract
176
-
substrate 1,2-dichloroethane, 35°C, pH 9.0, activity of crude extract
176
-
substrate tetrachloromethane, 35°C, pH 7.5, activity of crude extract
188
-
substrate trichloromethane, 35°C, pH 7.5, activity of crude extract
188
-
substrate trichloromethane, 35°C, pH 7.5, activity of crude extract
2.4
pH 8.6, 37°C, purified recombinant enzyme, substrate 1,3-diiodopropane
200
-
substrate dichloromethane, 35°C, pH 7.5, activity of crude extract
200
-
substrate trichloroacetic acid, 35°C, pH 9.0, activity of crude extract
223
-
substrate trichloroacetic acid, 35°C, pH 9.0, activity of crude extract
223
-
substrate 1,2-dichloroethane, 35°C, pH 7.5, activity of crude extract
258
-
substrate 1,2-dichloroethane, 35°C, pH 7.5, activity of crude extract
258
-
substrate trichloroacetic acid, 35°C, pH 9.0, activity of crude extract
282
-
substrate monochloroacetic acid, 35°C, pH 9.0, activity of crude extract
282
-
substrate 1,2-dichloroethane, 35°C, pH 7.5, activity of crude extract
70
-
substrate trichloroacetic acid, 35°C, pH 7.5, activity of crude extract
70
-
substrate trichloroethane, 35°C, pH 9.0, activity of crude extract
70
-
substrate trichloroethane, 35°C, pH 9.0, activity of crude extract
71
-
substrate monochloroacetic acid, 35°C, pH 7.5, activity of crude extract
71
-
substrate trichloroacetic acid, 35°C, pH 7.5, activity of crude extract
72
-
substrate dichloromethane, 35°C, pH 9.0, activity of crude extract
72
-
substrate tetrachloromethane, 35°C, pH 9.0, activity of crude extract
81
-
substrate trichloroethane, 35°C, pH 9.0, activity of crude extract
81
-
substrate tetrachloromethane, 35°C, pH 9.0, activity of crude extract
81
-
substrate monochloroacetic acid, 35°C, pH 7.5, activity of crude extract
82
-
substrate monochloroacetic acid, 35°C, pH 7.5, activity of crude extract
82
-
substrate tetrachloromethane, 35°C, pH 9.0, activity of crude extract
94
-
substrate trichloroethane, 35°C, pH 9.0, activity of crude extract
94
-
substrate monochloroacetic acid, 35°C, pH 7.5, activity of crude extract
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
broad statistical overview over reaction rates of several substrates
additional information
-
broad statistical overview over reaction rates of several substrates
additional information
-
-
additional information
-
broad statistical overview over reaction rates of several substrates
additional information
-
-
additional information
specific constant of LinB, mutant A247H, step HCH to PCHL, 0.0271 mM-1 s-1
additional information
specific constant of LinB, mutant A247H, step PCHL to TCDL, not determined
additional information
specific constant of LinB, mutant I134V, step HCH to PCHL, 0.0969 mM-1 s-1
additional information
specific constant of LinB, mutant I134V, step PCHL to TCDL, 0.0099 mM-1 s-1
additional information
specific constant of LinB, mutant I134V/A247H, step HCH to PCHL, 0.0243 mM-1 s-1
additional information
specific constant of LinB, mutant I134V/A247H, step PCHL to TCDL, 0.0183 mM-1 s-1
additional information
specific constant of LinB, wild-type, step HCH to PCHL, 0.0271 mM-1 s-1
additional information
specific constant of LinB, wild-type, step PCHL to TCDL, 0.0036 mM-1 s-1
additional information
specific constant of LinB, mutant H247A, step HCH to PCHL, 0.210 mM-1 s-1
additional information
specific constant of LinB, mutant H247A, step PCHL to TCDL, 0.240 mM-1 s-1
additional information
specific constant of LinB, mutant V134I, step HCH to PCHL, 0.124 mM-1 s-1
additional information
specific constant of LinB, mutant V134I, step PCHL to TCDL, 0.080 mM-1 s-1
additional information
specific constant of LinB, mutant V134I/H247A, step HCH to PCHL, 0.104 mM-1 s-1
additional information
specific constant of LinB, mutant V134I/H247A, step PCHL to TCDL, 0.027 mM-1 s-1
additional information
specific constant of LinB, wild-type, step HCH to PCHL, 0.205 mM-1 s-1
additional information
specific constant of LinB, wild-type, step PCHL to TCDL, 0.716 mM-1 s-1
additional information
-
comparison of wild-type and His-tagged enzyme concerning reaction rates for several substrates, remaining activity about 80%
additional information
-
data from 2 experimental sets, relative activity of diverse L177 mutants compared to the wild-type enzyme with the different substrates, overview
additional information
profound kinetic calculations
additional information
-
broad statistical overview over reaction rates of several substrates
additional information
calculation of activation energetics for haloalkane hydrolysis
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evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
evolution
-
DmmA belongs to the haloalkane dehalogenase family, subfamily-II, structure comparisons, overview
evolution
-
DpcA is a member of the haloalkane dehalogenase family
evolution
DppA is a member of the haloalkane dehalogenase subfamily HLD-I
evolution
-
the haloalkane dehalogenases form a subclass of enzymes in the alpha/beta-hydrolase fold superfamily
evolution
enzyme DadB likely belongs to the HLD-II subfamily, closely related with LinB and DmbA, while DadA appears to be relatively independent from the HLD-II subfamily. This pentad includes the nucleophile residue D108, the basic residue H271, the acid catalytic residue E132, and the halide-binding residues N37 and W109. DadB possesses a large main tunnel opening, but it prefers small substrates
evolution
haloalkane dehalogenase DatA from Agrobacterium tumefaciens strain C58 belongs to the HLD-II subfamily. Enzyme DatA possesses a unique Asn-Tyr pair instead of the Asn-Trp pair conserved among the subfamily members, which keeps the released halide ion stable
evolution
the enzyme belongs to the alpha/beta hydrolase family with a catalytic triad composed of Asp-His-Asp in its active site
evolution
the enzyme belongs to the alpha/beta hydrolase fold family
evolution
the enzyme belongs to the alpha/beta hydrolase fold family
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
P51698
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
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
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
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
evolution
-
the enzyme belongs to the superfamily of alpha/beta-hydrolases
evolution
-
the enzyme belongs to the superfamily of alpha/beta-hydrolases
evolution
the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs
evolution
the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs. The major structural difference between DmrA (HLD subfamily I) and the well-studied enzymes of HLD subfamily II is the different arrangement of helices in the cap domain
evolution
the enzyme possesses a unique halide-stabilizing tyrosine residue, Y109, in place of the conventional tryptophan. Enzyme DatA is unique in stabilizing its substrate in the active site using only a single hydrogen bond, which is a distinct paradigm in catalysis by this enzyme family
evolution
-
the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
evolution
the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
DpcA is a member of the haloalkane dehalogenase family
-
evolution
-
the enzyme belongs to the superfamily of alpha/beta-hydrolases
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
-
evolution
-
the enzyme belongs to the alpha/beta hydrolase family with a catalytic triad composed of Asp-His-Asp in its active site
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
haloalkane dehalogenase DatA from Agrobacterium tumefaciens strain C58 belongs to the HLD-II subfamily. Enzyme DatA possesses a unique Asn-Tyr pair instead of the Asn-Trp pair conserved among the subfamily members, which keeps the released halide ion stable
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
the enzyme possesses a unique halide-stabilizing tyrosine residue, Y109, in place of the conventional tryptophan. Enzyme DatA is unique in stabilizing its substrate in the active site using only a single hydrogen bond, which is a distinct paradigm in catalysis by this enzyme family
-
evolution
-
the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs. The major structural difference between DmrA (HLD subfamily I) and the well-studied enzymes of HLD subfamily II is the different arrangement of helices in the cap domain
-
evolution
-
the enzyme is a member of the alpha/beta hydrolase superfamily, which also includes epoxide hydrolases and carboxylesterases. Comparison of active site cavities and access tunnels of HLDs of type I and type II HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
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
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
enzyme DadB likely belongs to the HLD-II subfamily, closely related with LinB and DmbA, while DadA appears to be relatively independent from the HLD-II subfamily. This pentad includes the nucleophile residue D108, the basic residue H271, the acid catalytic residue E132, and the halide-binding residues N37 and W109. DadB possesses a large main tunnel opening, but it prefers small substrates
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
-
evolution
-
the enzymes LinBUT and LinBMI, i.e. LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively, catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane, mutational analysis and sequence comparisons, overview
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
evolution
-
comparison and classification of the substrate specificities of nine members of the HLD family, functional classification compared with one derived on the basis of the enzymes' evolutionary relationships, overview
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup III of HLDs
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
-
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
-
evolution
-
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup II of HLDs
-
malfunction
-
DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
malfunction
-
the single mutation in a tunnel to the active site changes the mechanism and kinetics of product release in LinB. Interactions of the bromide ion with the tryptophan increase free energy barrier for its passage, causing the reaction mechanism change
malfunction
-
DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
-
malfunction
-
the single mutation in a tunnel to the active site changes the mechanism and kinetics of product release in LinB. Interactions of the bromide ion with the tryptophan increase free energy barrier for its passage, causing the reaction mechanism change
-
physiological function
haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds
physiological function
haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds
physiological function
haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources
physiological function
the enzyme is involved in 1,2-dichloroethane degradation
physiological function
the enzyme is involved in 1,2-dichloroethane degradation
physiological function
the enzyme is involved in 1-haloalkanes degradation
physiological function
P51698
the enzyme is involved in gamma-HCH degradation
physiological function
xenobiotic stress mitigation
physiological function
-
xenobiotic stress mitigation
-
physiological function
-
haloalkane dehalogenases enable the first step in bacterial growth on haloalkanes as carbon and energy sources
-
physiological function
-
the enzyme is involved in 1-haloalkanes degradation
-
physiological function
-
the enzyme is involved in 1,2-dichloroethane degradation
-
physiological function
-
the enzyme is involved in 1,2-dichloroethane degradation
-
physiological function
-
the enzyme is involved in gamma-HCH degradation
-
additional information
active site residues are Asp123, His278, and Asp249, and Trp124 and Trp163 as halide-stabilizing residues, and a catalytic triad Asp-His-Asp
additional information
DatA possesses a unique pair of halide-stabilizing residues, Asn-Tyr, not reported in other known haloalkane dehalogenases
additional information
-
the active site is formed by a pentad consisting of halide-stabilizing Asn78 and Trp145, nucleophile Asp144, base His315, and acid Glu168. DmmA possesses a larg active site binding pocket allowing to accept a range of linear and cyclic substrates including include chlorinated, brominated, and iodinated alkanes of varying length, structure, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
-
analysis of the composition and diversity of metagenomic sequences encoding alpha/beta-hydrolase fold proteins in four distinct mangrove soils, haloalkane dehalogenases are only found in soil sample from one site, overview
additional information
DadB has an open active cavity with a large access tunnel, which is supposed important for larger molecules as opposed to C2-C3 substrates, homology modeling, residue I247 plays an important role in substrate selection. Homology modeling and structural analysis, overview. Enzyme DadB is composed of a core domain and a cap domain, identical catalytic pentad of HLD-II subfamily
additional information
-
DadB has an open active cavity with a large access tunnel, which is supposed important for larger molecules as opposed to C2-C3 substrates, homology modeling, residue I247 plays an important role in substrate selection. Homology modeling and structural analysis, overview. Enzyme DadB is composed of a core domain and a cap domain, identical catalytic pentad of HLD-II subfamily
additional information
docking models of enzyme DatA complexed with 1,3-dibromopropane and 2-bromohexane, the docking pose shows the highest score for each enantiomer of 2-bromohexane, only the (R)-form of 2-bromohexane can be in a near-attack conformation for the SN2 reaction. Location of the active site, and overall structure of the wild-type DatA, overview
additional information
enzyme ligand docking and molecular dynamics simulations, structure comparisons of wild-type and mutant enzymes, effects of different residues located near the active site on the specificity constants, overview
additional information
-
the active sites of Han enzymes are characterised by a catalytic pentad. This consists of a catalytic triad and a stabilizing pair of residues. The catalytic triad consists of Asp106 (located between beta-strand 5 and alpha-helix 2), His271 (located between beta-strand 8 and 310 helix 9) and Glu130 (located within beta-strand 6). The side chains of Trp107 and Asn36 bind the substrate halogen, while their main chain nitrogen atoms form the oxyanion hole. The HLD active site is built up of an entrance tunnel and a hydrophobic pocket for substrate binding. The residues lining the substrate pocket mainly belong to the cap domain and define substrate specificity. Minor differences in the substrate pocket can dramatically affect the substrate specificity of very similar HLDs
additional information
the enzyme has a core domain bearing the catalytic triad of Asp-His-Asp/Glu and a variable, mostly helical cap domain, which provides essential residues to stabilize the transition state, bind substrates and products and determine the selectivity. The essential residues D106 (nucleophile) and H272 (base) are involved in the catalytic mechanism of DhaA
additional information
the enzyme has a core domain bearing the catalytic triad of Asp-His-Asp/Glu and a variable, mostly helical cap domain, which provides essential residues to stabilize the transition state, bind substrates and products and determine the selectivity. The essential residues D124 (nucleophile) and H289 (base) are involved in the catalytic mechanism of DhlA
additional information
-
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
additional information
P51698
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
additional information
three-dimensional enzyme structure analysis modeling
additional information
-
three-dimensional enzyme structure analysis modeling
additional information
-
three-dimensional enzyme structure analysis modeling
-
additional information
-
docking models of enzyme DatA complexed with 1,3-dibromopropane and 2-bromohexane, the docking pose shows the highest score for each enantiomer of 2-bromohexane, only the (R)-form of 2-bromohexane can be in a near-attack conformation for the SN2 reaction. Location of the active site, and overall structure of the wild-type DatA, overview
-
additional information
-
DatA possesses a unique pair of halide-stabilizing residues, Asn-Tyr, not reported in other known haloalkane dehalogenases
-
additional information
-
DadB has an open active cavity with a large access tunnel, which is supposed important for larger molecules as opposed to C2-C3 substrates, homology modeling, residue I247 plays an important role in substrate selection. Homology modeling and structural analysis, overview. Enzyme DadB is composed of a core domain and a cap domain, identical catalytic pentad of HLD-II subfamily
-
additional information
-
enzyme ligand docking and molecular dynamics simulations, structure comparisons of wild-type and mutant enzymes, effects of different residues located near the active site on the specificity constants, overview
-
additional information
-
the enzyme shows higher activity toward beta-HCH than LinBUT from Sphingobium japonicum strain UT26
-
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Keuning, S.; Janssen, D.B.; Witholt, B.
Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
J. Bacteriol.
163
635-639
1985
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Yokota, T.; Omori, T.; Kodama, T.
Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3
J. Bacteriol.
169
4049-4054
1987
Corynebacterium sp., Corynebacterium sp. m15-3
brenda
Scholtz, R.; Leisinger, T.; Suter, F.; Cook, A.M.
Characterization of 1-chlorohexane halidohydrolase, a dehalogenase of wide substrate range from an Arthrobacter sp
J. Bacteriol.
169
5016-5021
1987
Arthrobacter sp., Arthrobacter sp. HA1
brenda
Franken, S.M.; Rozeboom, H.J.; Kalk, K.H.; Dijkstra, B.W.
Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes
EMBO J.
10
1297-1302
1991
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Verschueren, K.H.G.; Franken, S.M.; Rozeboom, H.J.; Kalk, K.H.; Dijkstra, B.W.
Non-covalent binding of the heavy atom compound [Au(CN)2]- at the halide binding site of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
FEBS Lett.
323
267-270
1993
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Verschueren, K.H.G.; Franken, S.M.; Rozeboom, H.J.; Kalk, K.H.; Dijkstra, B.W.
Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism
J. Mol. Biol.
232
856-872
1993
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Verschueren, K.H.G.; Seljee, F.; Rozeboom, H.J.; Kalk, K.H.; Dijkstra, B.W.
Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
Nature
363
693-698
1993
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Prince, R.C.
Haloalkane dehalogenase caught in the act
Trends Biochem. Sci.
19
3-4
1994
Xanthobacter autotrophicus, Rhodococcus sp., Xanthobacter autotrophicus GJ10
brenda
Kennes, C.; Pries, F.; Krooshof, G.H.; Bokma, E.; Kingma, J.; Janssen, D.B.
Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity
Eur. J. Biochem.
228
403-407
1995
Escherichia coli
brenda
Rozeboom, H.J.; Kingma, J.; Janssen, D.B.; Dijkstra, B.W.
Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
J. Mol. Biol.
200
611-612
1988
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Sallis, P.J.; Armfield, S.J.; Bull, A.T.; Hardman, D.J.
Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2
J. Gen. Microbiol.
136
115-120
1990
Rhodococcus erythropolis, Rhodococcus erythropolis Y2
brenda
Schanstra, J.P.; Ridder, I.S.; Heimeriks, G.J.; Rink, R.; Poelarends, G.J.; Kalk, K.H.; Dijkstra, B.W.; Janssen, D.B.
Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate range
Biochemistry
35
13185-13195
1996
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
-
brenda
Damborsky, J.; Nyandoroh, M.G.; Nemec, M.; Holoubek, I.; Bull, A.T.; Hardman, D.J.
Some biochemical properties and the classification of a range of bacterial haloalkane dehalogenases
Biotechnol. Appl. Biochem.
26
19-25
1997
Arthrobacter sp., Xanthobacter autotrophicus, Corynebacterium sp., Pseudomonas sp., Rhodococcus erythropolis, Rhodococcus erythropolis Y2, Arthrobacter sp. HA1, Rhodococcus erythropolis CP9, Pseudomonas sp. E4M
brenda
Nagata, Y.; Hynkova, K.; Damborsky, J.; Takagi, M.
Construction and characterization of histidine-tagged haloalkane dehalogenase (LinB) of a new substrate class from a gamma-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26
Protein Expr. Purif.
17
299-304
1999
Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
brenda
Nagata, Y.; Miyauchi, K.; Damborsky, J.; Manova, K.; Ansorgova, A.; Takagi, M.
Purification and characterization of a haloalkane dehalogenase of a new substrate class from a gamma-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26
Appl. Environ. Microbiol.
63
3707-3710
1997
Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
brenda
Pries, F.; Kingma, J.; Krooshof, G.H.; Jeronimus-Stratingh, C.M.; Bruins, A.; Janssen, D.B.
Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase
J. Biol. Chem.
270
10405-10411
1995
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Krooshof, G.H.; Ridder, I.S.; Tepper, A.W.J.; Vos, G.J.; Rozeboom, H.J.; Kalk, K.H.; Dijkstra, B.W.; Janssen, D.B.
Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site
Biochemistry
37
15013-15023
1998
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643)
brenda
Newman, J.; Peat, T.S.; Richard, R.; Kan, L.; Swanson, P.E.; Affholter, J.A.; Holmes, I.H.; Schindler, J.F.; Unkefer, C.J.; Terwillinger, T.C.
Haloalkane dehalogenases: structure of a Rhodoccocus enzyme
Biochemistry
38
16105-16114
1999
Rhodococcus erythropolis
brenda
Schindler, J.F.; Naranjo, P.A.; Honaberger, D.A.; Chang, C.H.; Brainard, J.R.; Vanderberg, L.A.; Unkefer, C.J.
Haloalkane dehalogenases: steady-state kinetics and halide inhibition
Biochemistry
38
5772-5778
1999
Xanthobacter autotrophicus, Rhodococcus erythropolis, Xanthobacter autotrophicus GJ10
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Pikkemaat, M.G.; Ridder, I.S.; Rozeboom, H.J.; Klak, K.H.; Dijkstra, B.W.; Janssen, D.B.
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
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Biochemistry
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Sphingomonas paucimobilis, Rhodococcus erythropolis, Xanthobacter autotrophicus (P22643), Sphingomonas paucimobilis UT26, Xanthobacter autotrophicus GJ10 (P22643)
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Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition
Biochemistry
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
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Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a Rhodococcus haloalkane dehalogenase
Biochemistry
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Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13064
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Crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A resolution: dynamics of catalytic residues
Biochemistry
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
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Xanthobacter autotrophicus (P22643)
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
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Nagata, Y.; Prokop, Z.; Sato, Y.; Jerabek, P.; Kumar, A.; Ohtsubo, Y.; Tsuda, M.; Damborsky, J.
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
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Sato, Y.; Monincova, M.; Chaloupkova, R.; Prokop, Z.; Ohtsubo, Y.; Minamisawa, K.; Tsuda, M.; Damborsky, J.; Nagata, Y.
Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities
Appl. Environ. Microbiol.
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Bradyrhizobium japonicum, Mesorhizobium loti, Bradyrhizobium japonicum USDA 110, Mesorhizobium loti MAFF303099
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Jesenska, A.; Pavlova, M.; Strouhal, M.; Chaloupkova, R.; Tesinska, I.; Monincova, M.; Prokop, Z.; Bartos, M.; Pavlik, I.; Rychlik, I.; Moebius, P.; Nagata, Y.; Damborsky, J.
Cloning, biochemical properties, and distribution of mycobacterial haloalkane dehalogenases
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Mycobacterium tuberculosis variant bovis (Q9XB14), Mycobacterium tuberculosis variant bovis 5033/66 (Q9XB14)
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Sharma, P.; Raina, V.; Kumari, R.; Malhotra, S.; Dogra, C.; Kumari, H.; Kohler, H.P.; Buser, H.R.; Holliger, C.; Lal, R.
Haloalkane dehalogenase LinB is responsible for beta- and delta-hexachlorocyclohexane transformation in Sphingobium indicum B90A
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Sphingobium indicum, Sphingobium indicum (A8CFB7), Sphingobium indicum B90A, Sphingobium indicum UT26, Sphingobium indicum Sp+
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Kmunicek, J.; Hynkova, K.; Jedlicka, T.; Nagata, Y.; Negri, A.; Gago, F.; Wade, R.C.; Damborsky, J.
Quantitative analysis of substrate specificity of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26
Biochemistry
44
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26
brenda
Torz, M.; Wietzes, P.; Beschkov, V.; Janssen, D.B.
Metabolism of mono- and dihalogenated C1 and C2 compounds by Xanthobacter autotrophicus growing on 1,2-dichloroethane
Biodegradation
18
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2006
Xanthobacter autotrophicus
brenda
Erable, B.; Goubet, I.; Lamare, S.; Legoy, M.D.; Maugard, T.
Haloalkane hydrolysis by Rhodococcus erythropolis cells: comparison of conventional aqueous phase dehalogenation and nonconventional gas phase dehalogenation
Biotechnol. Bioeng.
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2004
Rhodococcus erythropolis, Rhodococcus erythropolis NCIMB 13064
brenda
Erable, B.; Goubet, I.; Lamare, S.; Seltana, A.; Legoy, M.D.; Maugard, T.
Nonconventional hydrolytic dehalogenation of 1-chlorobutane by dehydrated bacteria in a continuous solid-gas biofilter
Biotechnol. Bioeng.
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2005
Xanthobacter autotrophicus, Rhodococcus erythropolis, Rhodococcus erythropolis NCIMB 13064
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Olaniran, A.O.; Pillay, D.; Pillay, B.
Haloalkane and haloacid dehalogenase from aerobic bacterial isolates indigenous to contaminated sites in Africa demonstrate diverse substrate specificities
Chemosphere
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Bacillus sp. (in: Bacteria), Burkholderia sp., Corynebacterium sp., Micrococcus sp., Pseudomonas sp.
brenda
Soriano, A.; Silla, E.; Tunon, I.; Ruiz-Lopez, M.F.
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Xanthobacter autotrophicus (P22643)
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Banas, P.; Otyepka, M.; Jerabek, P.; Petrek, M.; Damborsky, J.
Mechanism of enhanced conversion of 1,2,3-trichloropropane by mutant haloalkane dehalogenase revealed by molecular modeling
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Rhodococcus sp., Rhodococcus sp. (P0A3G3)
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Pavlova, M.; Klva?a, M.; Jesenska, A.; Prokop, Z.; Kone?na, H.; Sato, T.; Tsuda, M.; Nagata, Y.; Damborsky, J.
The identification of catalytic pentad in the haloalkane dehalogenase DhmA from Mycobacterium avium N85: Reaction mechanism and molecular evolution
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Mycobacterium avium, Mycobacterium avium (Q73Y99), Mycobacterium avium N85
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Erable, B.; Maugard, T.; Goubet, I.; Lamare, S.; Legoy, M.D.
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Process Biochem.
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Rhodococcus erythropolis, Rhodococcus erythropolis NCIMB 13064
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Nakamura, T.; Zamocky, M.; Zdrahal, Z.; Chaloupkova, R.; Monincova, M.; Prokop, Z.; Nagata, Y.; Damborsky, J.
Expression of glycosylated haloalkane dehalogenase LinB in Pichia pastoris
Protein Expr. Purif.
46
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2006
Sphingomonas paucimobilis (P51698), Sphingomonas paucimobilis UT26 (P51698), Sphingomonas paucimobilis UT26
brenda
Sato, Y.; Natsume, R.; Tsuda, M.; Damborsky, J.; Nagata, Y.; Senda, T.
Crystallization and preliminary crystallographic analysis of a haloalkane dehalogenase, DbjA, from Bradyrhizobium japonicum USDA110
Acta Crystallogr. Sect. F
63
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2007
Bradyrhizobium japonicum
brenda
Monincova, M.; Prokop, Z.; Vevodova, J.; Nagata, Y.; Damborsky, J.
Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane revealed by X-Ray crystallography and microcalorimetry
Appl. Environ. Microbiol.
73
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2007
Sphingobium indicum (A8CFB7)
brenda
Ito, M.; Prokop, Z.; Klvana, M.; Otsubo, Y.; Tsuda, M.; Damborsky, J.; Nagata, Y.
Degradation of beta-hexachlorocyclohexane by haloalkane dehalogenase LinB from gamma-hexachlorocyclohexane-utilizing bacterium Sphingobium sp. MI1205
Arch. Microbiol.
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Sphingobium sp. (A4PEU6), Sphingobium indicum (A8CFB7), Sphingobium sp. MI1205 (A4PEU6), Sphingobium indicum UT26 (A8CFB7)
brenda
Silberstein, M.; Damborsky, J.; Vajda, S.
Exploring the binding sites of the haloalkane dehalogenase DhlA from Xanthobacter autotrophicus GJ10
Biochemistry
46
9239-9249
2007
Rhodococcus sp. (P0A3G3), Xanthobacter autotrophicus (P22643), Sphingomonas paucimobilis (P51698)
brenda
Mazumdar, P.A.; Hulecki, J.C.; Cherney, M.M.; Garen, C.R.; James, M.N.
X-ray crystal structure of Mycobacterium tuberculosis haloalkane dehalogenase Rv2579
Biochim. Biophys. Acta
1784
351-362
2008
Mycobacterium tuberculosis (P9WMR9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMR9), Mycobacterium tuberculosis H37Rv
brenda
Negri, A.; Marco, E.; Damborsky, J.; Gago, F.
Stepwise dissection and visualization of the catalytic mechanism of haloalkane dehalogenase LinB using molecular dynamics simulations and computer graphics
J. Mol. Graph. Model.
26
643-651
2007
Sphingobium indicum (A8CFB7)
brenda
Chovancova, E.; Kosinski, J.; Bujnicki, J.M.; Damborsky, J.
Phylogenetic analysis of haloalkane dehalogenases
Proteins
67
305-316
2007
Mycobacterium tuberculosis, Mycobacterium avium, Mycolicibacterium smegmatis, Sphingobium indicum (A8CFB7), Rhodococcus sp. (P0A3G3), Xanthobacter autotrophicus (P22643), Bradyrhizobium japonicum (P59337), Rhodopirellula baltica (Q7UF99), Agrobacterium tumefaciens (Q8U671), Mesorhizobium loti (Q98C03)
brenda
Otyepka, M.; Banas, P.; Magistrato, A.; Carloni, P.; Damborsky, J.
Second step of hydrolytic dehalogenation in haloalkane dehalogenase investigated by QM/MM methods
Proteins
70
707-717
2008
Sphingomonas paucimobilis (P51698)
brenda
Stsiapanava, A.; Koudelakova, T.; Lapkouski, M.; Pavlova, M.; Damborsky, J.; Smatanova, I.K.
Crystals of DhaA mutants from Rhodococcus rhodochrous NCIMB 13064 diffracted to ultrahigh resolution: crystallization and preliminary diffraction analysis
Acta Crystallogr. Sect. F
64
137-140
2008
Rhodococcus rhodochrous (P0A3G2), Rhodococcus rhodochrous NCIMB 13064 (P0A3G2), Rhodococcus rhodochrous NCIMB 13064
brenda
Prudnikova, T.; Mozga, T.; Rezacova, P.; Chaloupkova, R.; Sato, Y.; Nagata, Y.; Brynda, J.; Kuty, M.; Damborsky, J.; Smatanova, I.K.
Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94
Acta Crystallogr. Sect. F
65
353-356
2009
Bradyrhizobium elkanii, Bradyrhizobium elkanii USDA94
brenda
Raina, V.; Rentsch, D.; Geiger, T.; Sharma, P.; Buser, H.R.; Holliger, C.; Lal, R.; Kohler, H.P.
New metabolites in the degradation of alpha- and gamma-hexachlorocyclohexane (HCH): pentachlorocyclohexenes are hydroxylated to cyclohexenols and cyclohexenediols by the haloalkane dehalogenase LinB from Sphingobium indicum B90A
J. Agric. Food Chem.
56
6594-6603
2008
Sphingobium indicum, Sphingobium indicum B90A
brenda
Jesenska, A.; Sykora, J.; Olzynska, A.; Brezovsky, J.; Zdrahal, Z.; Damborsky, J.; Hof, M.
Nanosecond time-dependent Stokes shift at the tunnel mouth of haloalkane dehalogenases
J. Am. Chem. Soc.
131
494-501
2009
Rhodococcus rhodochrous, Bradyrhizobium japonicum (P59337), Bradyrhizobium japonicum USDA 110 (P59337), Rhodococcus rhodochrous NCIMB13064
brenda
Murugan, N.A.; Agren, H.
1,2-dichloroethane in haloalkane dehalogenase protein and in water solvent: a case study of confinement effect on structural and dynamical properties
J. Phys. Chem. B
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3257-3263
2009
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643)
brenda
Mena-Benitez, G.L.; Gandia-Herrero, F.; Graham, S.; Larson, T.R.; McQueen-Mason, S.J.; French, C.E.; Rylott, E.L.; Bruce, N.C.
Engineering a catabolic pathway in plants for the degradation of 1,2-dichloroethane
Plant Physiol.
147
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2008
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
brenda
Hasan, K.; Fortova, A.; Koudelakova, T.; Chaloupkova, R.; Ishitsuka, M.; Nagata, Y.; Damborsky, J.; Prokop, Z.
Biochemical characteristics of the novel haloalkane dehalogenase DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58
Appl. Environ. Microbiol.
77
1881-1884
2011
Agrobacterium tumefaciens (E2RV69), Agrobacterium tumefaciens C58 / ATCC 33970 (E2RV69)
brenda
Drienovska, I.; Chovancova, E.; Koudelakova, T.; Damborsky, J.; Chaloupkova, R.
Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium
Appl. Environ. Microbiol.
78
4995-4998
2012
Psychrobacter cryohalolentis, Psychrobacter cryohalolentis K5
brenda
Hesseler, M.; Bogdanovic, X.; Hidalgo, A.; Berenguer, J.; Palm, G.J.; Hinrichs, W.; Bornscheuer, U.T.
Cloning, functional expression, biochemical characterization, and structural analysis of a haloalkane dehalogenase from Plesiocystis pacifica SIR-1
Appl. Microbiol. Biotechnol.
91
1049-1060
2011
Plesiocystis pacifica (A6G7B1)
brenda
Koudelakova, T.; Chovancova, E.; Brezovsky, J.; Monincova, M.; Fortova, A.; Jarkovsky, J.; Damborsky, J.
Substrate specificity of haloalkane dehalogenases
Biochem. J.
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Agrobacterium tumefaciens, Bradyrhizobium japonicum, Xanthobacter autotrophicus, Mycobacterium tuberculosis variant bovis, Rhodococcus rhodochrous, Sphingobium indicum, Rhodopirellula baltica, Bradyrhizobium elkanii, Bradyrhizobium japonicum USDA 110, Agrobacterium tumefaciens C58 / ATCC 33970, Rhodococcus rhodochrous NCIMB 13064, Bradyrhizobium elkanii USDA94, Rhodopirellula baltica SH1, Xanthobacter autotrophicus GJ10, Sphingobium indicum UT26, Mycobacterium tuberculosis variant bovis 5033/66
brenda
van Leeuwen, J.G.; Wijma, H.J.; Floor, R.J.; van der Laan, J.M.; Janssen, D.B.
Directed evolution strategies for enantiocomplementary haloalkane dehalogenases: from chemical waste to enantiopure building blocks
ChemBioChem
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137-148
2012
Rhodococcus rhodochrous
brenda
Bala, K.; Geueke, B.; Miska, M.E.; Rentsch, D.; Poiger, T.; Dadhwal, M.; Lal, R.; Holliger, C.; Kohler, H.P.
Enzymatic conversion of epsilon-hexachlorocyclohexane and a heptachlorocyclohexane isomer, two neglected components of technical hexachlorocyclohexane
Environ. Sci. Technol.
46
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2012
Sphingobium indicum, Sphingobium indicum B90A
brenda
Chaloupkova, R.; Prokop, Z.; Sato, Y.; Nagata, Y.; Damborsky, J.
Stereoselectivity and conformational stability of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110: the effect of pH and temperature
FEBS J.
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Bradyrhizobium japonicum (P59337), Bradyrhizobium japonicum USDA 110 (P59337)
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Biedermannova, L.; Prokop, Z.; Gora, A.; Chovancova, E.; Kovacs, M.; Damborsky, J.; Wade, R.C.
A single mutation in a tunnel to the active site changes the mechanism and kinetics of product release in haloalkane dehalogenase LinB
J. Biol. Chem.
287
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2012
Sphingobium indicum, Sphingobium indicum UT26
brenda
Gehret, J.J.; Gu, L.; Geders, T.W.; Brown, W.C.; Gerwick, L.; Gerwick, W.H.; Sherman, D.H.; Smith, J.L.
Structure and activity of DmmA, a marine haloalkane dehalogenase
Protein Sci.
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2012
uncultured marine bacterium, no activity in Moorea producta
brenda
Westerbeek, A.; van Leeuwen, J.; Szymanski, W.; Feringa, B.; Janssen, D.
Haloalkane dehalogenase catalysed desymmetrisation and tandem kinetic resolution for the preparation of chiral haloalcohols
Tetrahedron
68
7645-7650
2012
Bradyrhizobium japonicum, Xanthobacter autotrophicus, Sphingomonas paucimobilis, Mesorhizobium loti, Rhodococcus rhodochrous, Bradyrhizobium japonicum USDA 110, Sphingomonas paucimobilis UT26, Mesorhizobium loti MAFF303099, Rhodococcus rhodochrous NCIMB13064, Xanthobacter autotrophicus GJ10
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brenda
Tratsiak, K.; Degtjarik, O.; Drienovska, I.; Chrast, L.; Rezacova, P.; Kuty, M.; Chaloupkova, R.; Damborsky, J.; Kuta Smatanova, I.
Crystallographic analysis of new psychrophilic haloalkane dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17
Acta Crystallogr. Sect. F
69
683-688
2013
Marinobacter sp., Psychrobacter cryohalolentis, Psychrobacter cryohalolentis K5
brenda
Guan, L.; Yabuki, H.; Okai, M.; Ohtsuka, J.; Tanokura, M.
Crystal structure of the novel haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 reveals a special halide-stabilizing pair and enantioselectivity mechanism
Appl. Microbiol. Biotechnol.
98
8573-8582
2014
Agrobacterium tumefaciens (E2RV69), Agrobacterium tumefaciens C58 / ATCC 33970 (E2RV69)
brenda
Fibinger, M.P.; Davids, T.; Boettcher, D.; Bornscheuer, U.T.
A selection assay for haloalkane dehalogenase activity based on toxic substrates
Appl. Microbiol. Biotechnol.
99
8955-8962
2015
Rhodococcus rhodochrous (P0A3G2), Xanthobacter autotrophicus (P22643)
brenda
Nagata, Y.; Ohtsubo, Y.; Tsuda, M.
Properties and biotechnological applications of natural and engineered haloalkane dehalogenases
Appl. Microbiol. Biotechnol.
99
9865-9881
2015
Arthrobacter sp., Corynebacterium sp., Rhodococcus sp., Sphingomonas sp., Strongylocentrotus purpuratus, Sphingobium indicum, Sphingobium indicum (P51698), Alcanivorax dieselolei, Rhodobacteraceae bacterium UDC319 (A0A023I2Y1), Marinobacter sp. (A3JB27), Sphingobium sp. (A4PEU6), Mycobacterium tuberculosis variant bovis (A4Q9R7), Mycobacterium tuberculosis variant bovis (Q6EUU8), Mycobacterium tuberculosis variant bovis (Q9XB14), Plesiocystis pacifica (A6G7B1), Bradyrhizobium elkanii (E2RV62), Agrobacterium tumefaciens (E2RV69), Rhodopirellula baltica (G3XCP3), Rhodococcus rhodochrous (P0A3G2), Xanthobacter autotrophicus (P22643), Bradyrhizobium japonicum (P59337), Mycobacterium tuberculosis (P9WMR9), Psychrobacter cryohalolentis (Q1QBB9), Mycobacterium avium (Q93K00), Mesorhizobium loti (Q98C03), Mycobacterium sp. (Q9ZER0), Bradyrhizobium japonicum USDA 110 (P59337), Mycobacterium sp. GP1 (Q9ZER0), Psychrobacter cryohalolentis K5 (Q1QBB9), Mycobacterium avium N85 (Q93K00), Mesorhizobium loti MAFF303099 (Q98C03), Agrobacterium tumefaciens C58 / ATCC 33970 (E2RV69), Rhodococcus rhodochrous NCIMB 13064 (P0A3G2), Mycobacterium tuberculosis H37Rv (P9WMR9), Bradyrhizobium elkanii USDA94 (E2RV62), Rhodopirellula baltica SH1 (G3XCP3), Alcanivorax dieselolei B-5, Sphingobium sp. MI1205 (A4PEU6), Sphingobium indicum B90A, Xanthobacter autotrophicus GJ10 (P22643), Sphingobium indicum UT26 (P51698), Mycobacterium tuberculosis variant bovis 5033/66 (A4Q9R7), Mycobacterium tuberculosis variant bovis 5033/66 (Q6EUU8), Mycobacterium tuberculosis variant bovis 5033/66 (Q9XB14), Sphingomonas sp. BHC-A
brenda
Fortova, A.; Sebestova, E.; Stepankova, V.; Koudelakova, T.; Palkova, L.; Damborsky, J.; Chaloupkova, R.
DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin
Biochimie
95
2091-2096
2013
Strongylocentrotus purpuratus
brenda
Koudelakova, T.; Bidmanova, S.; Dvorak, P.; Pavelka, A.; Chaloupkova, R.; Prokop, Z.; Damborsky, J.
Haloalkane dehalogenases: biotechnological applications
Biotechnol. J.
8
32-45
2013
Bradyrhizobium japonicum, Sphingomonas paucimobilis, Rhodococcus rhodochrous, Bradyrhizobium japonicum USDA 110
brenda
Hasan, K.; Gora, A.; Brezovsky, J.; Chaloupkova, R.; Moskalikova, H.; Fortova, A.; Nagata, Y.; Damborsky, J.; Prokop, Z.
The effect of a unique halide-stabilizing residue on the catalytic properties of haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58
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Agrobacterium tumefaciens (E2RV69), Agrobacterium tumefaciens C58 / ATCC 33970 (E2RV69)
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Novak, H.R.; Sayer, C.; Isupov, M.N.; Gotz, D.; Spragg, A.M.; Littlechild, J.A.
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Rhodobacteraceae
brenda
Okai, M.; Ohtsuka, J.; Imai, L.F.; Mase, T.; Moriuchi, R.; Tsuda, M.; Nagata, K.; Nagata, Y.; Tanokura, M.
Crystal structure and site-directed mutagenesis analyses of haloalkane dehalogenase LinB from Sphingobium sp. strain MI1205
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Sphingobium indicum, Sphingobium sp. (A4PEU6), Sphingobium sp. MI1205 (A4PEU6), Sphingobium indicum UT26
brenda
Jimenez, D.; Dini-Andreote, F.; Ottoni, J.; de Oliveira, V.; van Elsas, J.; Andreote, F.
Compositional profile of alpha/beta-hydrolase fold proteins in mangrove soil metagenomes: Prevalence of epoxide hydrolases and haloalkane dehalogenases in oil-contaminated sites
Microb. Biotechnol.
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Aeromicrobium marinum, Alcanivorax borkumensis, Anaeromyxobacter sp. K, Chloroflexus sp., Moritella sp., Mycobacterium marinum, Mycolicibacterium vanbaalenii, Oceanicaulis alexandrii, Photobacterium profundum, Salinispora arenicola
brenda
Fung, H.; Gadd, M.; Drury, T.; Cheung, S.; Guss, J.; Coleman, N.; Matthews, J.
Biochemical and biophysical characterisation of haloalkane dehalogenases DmrA and DmrB in Mycobacterium strain JS60 and their role in growth on haloalkanes
Mol. Microbiol.
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439-453
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Mycolicibacterium rhodesiae (G4I2J6), Mycolicibacterium rhodesiae (G4I5P8), Mycolicibacterium rhodesiae JS60 (G4I2J6), Mycolicibacterium rhodesiae JS60 (G4I5P8)
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Li, A.; Shao, Z.
Biochemical characterization of a haloalkane dehalogenase DadB from Alcanivorax dieselolei B-5
PLoS ONE
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Alcanivorax dieselolei (K0CAI2), Alcanivorax dieselolei, Alcanivorax dieselolei B-5 (K0CAI2)
brenda
Kumar, A.; Pillay, B.; Olaniran, A.O.
Cloning, expression, purification and three-dimensional structure prediction of haloalkane dehalogenase from a recently isolated Ancylobacter aquaticus strain UV5
Protein Expr. Purif.
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2014
Ancylobacter aquaticus (B8YPW8), Ancylobacter aquaticus, Ancylobacter aquaticus UV5 (B8YPW8), Ancylobacter aquaticus UV5
brenda
Ang, T.F.; Salleh, A.B.; Normi, Y.M.; Leow, T.C.
In silico design of potentially functional artificial metallo-haloalkane dehalogenase containing catalytic zinc
3 Biotech
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314
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Rhodococcus rhodochrous (P0A3G2)
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Tratsiak, K.; Prudnikova, T.; Drienovska, I.; Damborsky, J.; Brynda, J.; Pachl, P.; Kuty, M.; Chaloupkova, R.; Rezacova, P.; Kuta Smatanova, I.
Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
Acta Crystallogr. Sect. F
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324-331
2019
Psychrobacter cryohalolentis (Q1QBB9), Psychrobacter cryohalolentis K5 (Q1QBB9), Psychrobacter cryohalolentis K5
brenda
Buryska, T.; Daniel, L.; Kunka, A.; Brezovsky, J.; Damborsky, J.; Prokop, Z.
Discovery of novel haloalkane dehalogenase inhibitors
Appl. Environ. Microbiol.
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Mycobacterium tuberculosis (P9WMR9), Mycobacterium tuberculosis H37Rv (P9WMR9), Mycobacterium tuberculosis H37Rv
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Buryska, T.; Babkova, P.; Vavra, O.; Damborsky, J.; Prokop, Z.
A haloalkane dehalogenase from a marine microbial consortium possessing exceptionally broad substrate specificity
Appl. Environ. Microbiol.
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Lyngbya majuscula (Q6DND9)
brenda
Kotik, M.; Vanacek, P.; Kunka, A.; Prokop, Z.; Damborsky, J.
Metagenome-derived haloalkane dehalogenases with novel catalytic properties
Appl. Microbiol. Biotechnol.
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6385-6397
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uncultured bacterium
brenda
Tang, X.; Zhang, R.; Li, Y.; Zhang, Q.; Wang, W.
Enantioselectivity of haloalkane dehalogenase LinB on the degradation of 1,2-dichloropropane A QM/MM study
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Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26S
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Gross, J.; Prokop, Z.; Janssen, D.; Faber, K.; Hall, M.
Regio- and enantioselective sequential dehalogenation of rac-1,3-dibromobutane by haloalkane dehalogenase LinB
ChemBioChem
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1437-1441
2016
Sphingobium indicum (D4Z2G1), Sphingobium indicum UT26 (D4Z2G1)
brenda
Wang, F.; Song, T.; Jiang, H.; Pei, C.; Huang, Q.; Xi, H.
Bacillus subtilis spore surface display of haloalkane dehalogenase DhaA
Curr. Microbiol.
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Rhodococcus rhodochrous (P0A3G2), Rhodococcus rhodochrous NCIMB 13064 (P0A3G2), Rhodococcus rhodochrous NCIMB 13064
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Zheng, H.; Yu, W.L.; Guo, X.; Zhao, Y.Z.; Cui, Y.; Hu, T.; Zhong, J.Y.
An effective immobilized haloalkane dehalogenase DhaA from Rhodococcus rhodochrous by adsorption, crosslink and PEGylation on meso-cellular foam
Int. J. Biol. Macromol.
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1016-1023
2019
Rhodococcus rhodochrous (P0A3G2), Rhodococcus rhodochrous
brenda
Kokkonen, P.; Bednar, D.; Dockalova, V.; Prokop, Z.; Damborsky, J.
Conformational changes allow processing of bulky substrates by a haloalkane dehalogenase with a small and buried active site
J. Biol. Chem.
293
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Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
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Zhao, Y.Z.; Yu, W.L.; Zheng, H.; Guo, X.; Guo, N.; Hu, T.; Zhong, J.Y.
PEGylation with the thiosuccinimido butylamine linker significantly increases the stability of haloalkane dehalogenase DhaA
J. Biotechnol.
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2017
Rhodococcus rhodochrous (P0A3G2)
brenda
Marques, S.M.; Dunajova, Z.; Prokop, Z.; Chaloupkova, R.; Brezovsky, J.; Damborsky, J.
Catalytic cycle of haloalkane dehalogenases toward unnatural substrates explored by computational modeling
J. Chem. Inf. Model.
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2017
Rhodococcus rhodochrous (P0A3G2)
brenda
Daud, N.H.; Leow, T.C.; Oslan, S.N.; Salleh, A.B.
A Novel mini protein design of haloalkane dehalogenase
Mol. Biotechnol.
61
477-488
2019
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643)
brenda
Fung, H.; Gadd, M.; Drury, T.; Cheung, S.; Guss, J.; Coleman, N.; Matthews, J.
Biochemical and biophysical characterisation of haloalkane dehalogenases DmrA and DmrB in Mycobacterium strain JS60 and their role in growth on haloalkanes
Mol. Microbiol.
97
439-453
2015
Mycolicibacterium rhodesiae (G4I2J6), Mycolicibacterium rhodesiae (G4I5P8), Mycolicibacterium rhodesiae JS60 (G4I2J6), Mycolicibacterium rhodesiae JS60 (G4I5P8)
brenda
Carlucci, L.; Zhou, E.; Malashkevich, V.N.; Almo, S.C.; Mundorff, E.C.
Biochemical characterization of two haloalkane dehalogenases DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea
Protein Sci.
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877-886
2016
Caulobacter vibrioides (Q9A919), Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089 (Q9A919), Saccharomonospora azurea
brenda
Bendigiri, C.; Zinjarde, S.; RaviKumar, A.
Ylehd, an epoxide hydrolase with promiscuous haloalkane dehalogenase activity from tropical marine yeast Yarrowia lipolytica is induced upon xenobiotic stress
Sci. Rep.
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11887
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Yarrowia lipolytica (Q6C598), Yarrowia lipolytica, Yarrowia lipolytica CLIB 122 (Q6C598)
brenda