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3.8.1.5: haloalkane dehalogenase

This is an abbreviated version!
For detailed information about haloalkane dehalogenase, go to the full flat file.

Word Map on EC 3.8.1.5

Reaction

1-Haloalkane
+
H2O
=
a primary alcohol
+
halide

Synonyms

1,3,4,6,-tetrachloro-1,4-cyclohexadiene halidohydrolase, 1-chlorohexane halidohydrolase, 1-haloalkane dehalogenase, DadB, DatA, DbeA, DbjA, DccA, DhaA, DhaA31, DhaB, DhaC, DhAf, DhlA, DhmA, DmaA, dmbA, DmbB, DmbC, dmlA, DmmA, DmrA, DmrB, DmsA, DmtA, DmxA, DpcA, DppA, DrbA, DsaA, DspA, EC 3.8.1.1, eHLD-B, eHLD-C, haloalkane dehalogenase, haloalkane dehalogenase LinB, HanR, HLD, HLD-I, LinB, LinBMI, LinBUT, metallo-haloalkane dehalogenase, protein XP_504164, Rv2579, Ylehd

ECTree

     3 Hydrolases
         3.8 Acting on halide bonds
             3.8.1 In carbon-halide compounds
                3.8.1.5 haloalkane dehalogenase

Engineering

Engineering on EC 3.8.1.5 - haloalkane dehalogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y109W
D103A
-
no activity with substrates 1,3-dibromopropane or 1-chlorobutane
E127A
-
no activity with substrates 1,3-dibromopropane or 1-chlorobutane, purification of enzyme not possible because of very small amount of soluble enzyme protein
H139A
site-directed mutagenesis
H280A
-
no activity with substrates 1,3-dibromopropane or 1-chlorobutane
D103A
-
no activity with substrates 1,3-dibromopropane or 1-chlorobutane
-
E127A
-
no activity with substrates 1,3-dibromopropane or 1-chlorobutane, purification of enzyme not possible because of very small amount of soluble enzyme protein
-
H139A
-
site-directed mutagenesis
-
H280A
-
no activity with substrates 1,3-dibromopropane or 1-chlorobutane
-
W125F
-
modified substrate binding properties
W125Q
-
modified substrate binding properties
W125R
-
modified substrate binding properties
W175Q
-
modified substrate binding properties
D123A
D250A
H279A
W124L
W164L
D123A
-
no enzymic activity
-
D250A
-
no enzymic activity
-
H279A
-
no enzymic activity
-
W124L
-
no enzymic activity
-
W164L
-
no enzymic activity
-
C176Y/Y273F
W118F
-
mutant with increased KM and decreased kcat for primary, secondary and cyclic alkylhalide substrates
D106A
site-directed mutagenesis, inactive mutant
D106A/H272A
site-directed mutagenesis, inactive mutant
F168W/A172L/Y176G
-
site-directed mutagenesis, the mutant shows increased enantioselectivity with substrate TCP compared to the wild-type enzyme, 1,2,3-trichloropropane is docked in the active site in a configuration that leads to (R)-2,3-dichloropropan-1-ol formation
H271A
site-directed mutagenesis, inactive mutant
I135F/C176Y/V245F/L246I/Y273F
C176Y
A247H
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
I134A
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
I134V/A247H
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
L177W
-
naturally occuring mutation, 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
A247H
-
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
-
I134A
-
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
-
I134V/A247H
-
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
-
L177W
-
naturally occuring mutation, 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
-
H247A
I253M
site-directed mutagenesis
L138I
site-directed mutagenesis
T135A
site-directed mutagenesis
T81A
site-directed mutagenesis
V112A
site-directed mutagenesis
V134I
V134I/H247A
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
H247A
-
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
-
T135A
-
site-directed mutagenesis
-
T81A
-
site-directed mutagenesis
-
V112A
-
site-directed mutagenesis
-
V134I
V134I/H247A
-
mutant, constructed for quantitative evaluation of the differences between LinB of Sphingobium japonicum and LinB of Sphingobium sp.
-
F151L
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
F151W
F151Y
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
F169L
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
L177A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
L177C
-
site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane, bromocyclohexane and 1-bromobutane
L177D
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
L177E
-
site-directed mutagenesis, mutant cannot be expressed in Escherichia coli due to incorrect protein folding
L177F
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
L177H
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
L177I
-
site-directed mutagenesis, inactive mutant, incorrect protein folding
L177M
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
L177N
-
site-directed mutagenesis, mutant cannot be expressed in Escherichia coli due to incorrect protein folding
L177P
-
site-directed mutagenesis, inactive mutant, incorrect protein folding
L177Q
-
site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane and 1-bromobutane
L177R
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
L177S
-
site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane and 1-bromobutane
L177T
-
site-directed mutagenesis, altered substrate specificity, especially high activity with 1-iodobutane and 1-bromobutane
L177V
-
site-directed mutagenesis, altered substrate specificity, especially high activity with 1-bromobutane
L177W
-
site-directed mutagenesis, altered substrate specificity, specifically highly active with 1-chlorobutane
L177Y
-
site-directed mutagenesis, altered substrate specificity, especially low activity with 1,2-dibromoethane
N38D
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
N38E
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
N38F
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
N38Q
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
W109L
F151W
L177A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
-
L177E
-
site-directed mutagenesis, mutant cannot be expressed in Escherichia coli due to incorrect protein folding
-
L177I
-
site-directed mutagenesis, inactive mutant, incorrect protein folding
-
L177N
-
site-directed mutagenesis, mutant cannot be expressed in Escherichia coli due to incorrect protein folding
-
L177P
-
site-directed mutagenesis, inactive mutant, incorrect protein folding
-
N38D
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
-
N38E
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
-
N38F
-
site-directed mutagenesis, altered catalytic properties compared to the wild-type enzyme
-
W109L
D124A
site-directed mutagenesis, inactive mutant
D124A/H289A
site-directed mutagenesis, inactive mutant
F172W
F172Y
-
mutant with 5fold higher KM for 1-chlorohexane
F294A
mutant with modified kinetic mechanism for halide binding
H289A
site-directed mutagenesis, inactive mutant
H289Q
-
GJ10, mutant with 660fold reduced activity with substrate 1,2-dibromoethane
T197A
mutant with modified kinetic mechanism for halide binding
W175F
-
mutant with no inhibition through halide product
W175Y
F172W
F172Y
-
mutant with 5fold higher KM for 1-chlorohexane
-
H289Q
-
GJ10, mutant with 660fold reduced activity with substrate 1,2-dibromoethane
-
W175F
-
mutant with no inhibition through halide product
-
W175Y
additional information