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Information on EC 3.8.1.5 - haloalkane dehalogenase and Organism(s) Xanthobacter autotrophicus and UniProt Accession P22643
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3.8.1.5 haloalkane dehalogenaseIUBMB Comments
Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.
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Word Map
- 3.8.1.5
- xanthobacter
- autotrophicus
-
dehalogenation
- 1,2-dichloroethane
- halide
-
carbon-halogen
- 1,2-dibromoethane
- sphingomonas
- paucimobilis
- 1,2,3-trichloropropane
- synthesis
- hexachlorocyclohexane
- rhodochrous
- sphingobium
- environmental protection
-
alkyl-enzyme
-
haloacid
- 1-chlorobutane
- 2-chloroethanol
-
ncimb
-
chloroalkane
- dehydrochlorinase
- epichlorohydrine
- gamma-hexachlorocyclohexane
-
halotag
- biotechnology
-
alpha/beta-hydrolase
- haloalcohols
- agriculture
-
halide-binding
- degradation
- industry
The taxonomic range for the selected organisms is: Xanthobacter autotrophicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
haloalkane dehalogenase, haloalkane dehalogenase linb, dhaa31, hld-i, rv2579, ehld-c, linbut, ylehd, 1-chlorohexane halidohydrolase, ehld-b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DhlA
1-chlorohexane halidohydrolase
-
-
-
-
1-haloalkane dehalogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-haloalkane + H2O = a primary alcohol + halide
GJ10, three-step reaction mechanism with covalent alkyl-enzyme ester intermediate
1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction
1-haloalkane + H2O = a primary alcohol + halide
GJ10, detailed reaction mechanism and energetics calculated from computational model
1-haloalkane + H2O = a primary alcohol + halide
3 features are important for catalytic performance: i. a catalytic triad, ii. anoxyanion hole, and iii. the halide-stabilizing residues, which are not conserved among different haloalkane dehalogenases, active site structure, Glu56 is involved, SN2 reaction mechanism, modeling, overview
1-haloalkane + H2O = a primary alcohol + halide
hydrogen bond interactions between substrate and the environment are significantly different in aqueous solution and in the enzyme. Structure of the enzyme active site provides a more adequate interaction pattern for the reaction process
1-haloalkane + H2O = a primary alcohol + halide
GJ10, four-step reaction mechanism with covalent ester intermediate
-
1-haloalkane + H2O = a primary alcohol + halide
distinction of 3 different substrate classes for haloalkane dehalogenases after profound statistical reaction rate analysis
-
1-haloalkane + H2O = a primary alcohol + halide
alpha/beta hydrolase with catalytic triad, i.e. nucleophile (Asp124)-histidine (H289)-acid (Asp260), during catalytic reaction
-
1-haloalkane + H2O = a primary alcohol + halide
two-step mechanism involving an ester intermediate covalently bound at Asp124, His 289 is important for hydrolysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-halide
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
1-haloalkane halidohydrolase
Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.
CAS REGISTRY NUMBER
COMMENTARY
95990-29-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dibromoethane + H2O
2-bromoethanol + bromide
-
-
-
?
1,2-dibromopropane + H2O
2-bromopropan-1-ol + bromide
-
-
-
?
1,2-dichloroethane + H2O
2-chloro-1-ethanol + chloride
-
-
-
?
1,2-dichloropropane + H2O
2-chloropropan-1-ol + chloride
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-I, substrates small, terminally halogenated
-
-
?
2-bromoacetamide + H2O
acetamide + bromide
poor substrate
-
-
?
2-chloroacetamide + H2O
acetamide + chloride
poor substrate
-
-
?
2-chloroethanol + H2O
ethanol + chloride
very poor substrate
-
-
?
dichloromethane + H2O
chloromethanol + chloride
poor substrate
-
-
?
1-bromo-2-chloroethane + H2O
?
-
76% of the activity with 1,2-dichloroethane
-
-
?
1-bromopropane + H2O
propanol + bromide
-
29% of the activity with 1,2-dichloroethane
-
-
?
1-chloro-2-fluoroethane + H2O
?
-
no release of fluoride, 25% of the activity with 1,2-dichloroethane
-
-
?
1-chloropropane + H2O
propanol + chloride
-
51% of the activity with 1,2-dichloroethane
-
-
?
1-iodopropane + H2O
propanol + iodide
-
14% of the activity with 1,2-dichloroethane
-
-
?
3-chloropropene + H2O
propenol + chloride
-
45% of the activity with 1,2-dichloroethane
-
-
?
bromochloromethane + H2O
?
-
99% of the activity with 1,2-dichloroethane
-
-
?
bromoethane + H2O
ethanol + bromide
-
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
-
-
?
dibromomethane + H2O
bromomethanol + bromide
-
71% of the activity with 1,2-dichloroethane
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
broad substrate range
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
analysis of dynamic and electrostatic effects
-
-
?
haloalkane + H2O
alcohol + halide
comparison of substrate specificities and classification
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
broad substrate range
-
-
?
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-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
highest activity
-
-
?
1,3-dichloropropane + H2O
?
-
80% of the activity with 1,2-dichloroethane
-
-
?
1-chlorobutane + H2O
butanol + chloride
-
31% of the activity with 1,2-dichloroethane
-
-
?
haloalkane + H2O
alcohol + halide
-
-
-
-
?
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
-
-
?
additional information
?
-
substrate specificity analysis, 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. Poor activity with 1,3-dibromo-2-methylpropane, 1,3-dibromo-2-phenylpropane, and meso-2,3-dibromobutane
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
?
1-haloalkane + H2O
a primary alcohol + halide
subfamily HLD-I, substrates small, terminally halogenated
-
-
?
1,2-dichloroethane + H2O
2-chloroethanol + chloride
-
-
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
-
broad substrate range
-
-
?
n-haloalkanes + H2O
primary alcohols + halide
broad substrate range
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by some substrate analogs, such as 1,1-dichloroethane
-
halide
-
product shows uncompetitive, pH-dependent inhibition pattern, maximal inhibition at optimal pH
halide
-
GJ10 mutant H289Q blocked by bromide in intermediate state
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
59
1,2-Dibromoethane
GJ10mutant W175Y, calculated from rate constants
60
1,2-Dibromoethane
GJ10 mutant W175Y, steady state experiments
4.3
1,2-Dibromoethane
-
GJ10, calculated from rate constants for four-steps reaction mechanism
29
1,2-Dibromoethane
-
GJ10, F172W mutant, calculated from rate constants for four-steps reaction mechanism
0.001
1,2-Dichloroethane
-
GJ10, calculated from rate constants for four-steps reaction mechanism
0.008
1,2-Dichloroethane
-
GJ10, F172W mutant, calculated from rate constants for four-steps reaction mechanism
additional information
additional information
kinetics and binding energy analysis, wild-type and mutant F172W
-
additional information
additional information
-
substrate specificity and kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
rate limiting reaction step is the release of halide
-
additional information
additional information
-
GJ10, rate limiting step is hydrolysis of alkyl-enzyme intermediate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
calculation of activation energetics for haloalkane hydrolysis
additional information
-
broad statistical overview over reaction rates of several substrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
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
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
evolution
the enzyme belongs to the alpha/beta hydrolase fold family
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily, subgroup I of HLDs
physiological function
haloalkane dehalogenases can degrade toxic pollutants by cleaving the carbon-halogen bond of halogenated aliphatic compounds
physiological function
the enzyme is involved in 1,2-dichloroethane degradation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme-ligand-structure of wild-type and mutant enzymes, overview
additional information
primary halide-stabilizing residues are Trp125 and Trp175, secondary halide-stabilizing residues are Phe172, Pro223, and Val226
additional information
structure modeling of the enzyme-substrate-complex on the basis of X-ray diffraction data at 2.4 A resolution, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of crystal structures of haloalkane dehalogenases by homology models
enzyme-substrate-complex: molecular dynamics simulation and structure modeling on the basis of X-ray diffraction data at 2.4 A resolution, overview
GJ10, X-ray structure at pH 6.2 and pH 5.0 at room temperature of wild-type and mutant W175Y
X-ray structure with bound bromide of wild-type and mutant enzymes
X-ray structures at pH 6.2 and pH 8.2 and implications for the reaction mechanism
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F172W
F294A
mutant with modified kinetic mechanism for halide binding
T197A
mutant with modified kinetic mechanism for halide binding
F172W
-
mutant with 10fold higher KM for 1-chlorohexane and 2fold higher KM for 1,2-dibromoethane, increased bromide release but velocity of hydrolysis of alkyl-enzyme bond remains unchanged
H289Q
-
GJ10, mutant with 660fold reduced activity with substrate 1,2-dibromoethane
additional information
F172W
steady state kinetics of the mutant compared to the wild-type enzyme
F172W
the conformational change of the mutant enzyme is faster than that of the wild-type enzyme. The open conformation is more common than the closed one. The closed conformation also displays a larger distance between the two helices than what is observed in the wild-type simulations
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. Three saturation libraries, with a size of more than 106 cells, based on inactive variants of the haloalkane dehalogenases DhlA are successfully screened to retrieve active enzymes
additional information
engineered enzyme variants are constructed for in vivo evolution for activity toward 1-chlorohexane, more activity toward 1,6-dichlorohexane than DhlA wild-type, and increased activity toward 1,2-dibromoethane/1-bromobutane the wild-type
additional information
-
GJ10, several mutants of F172, tested for substrate binding
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
83.73
mini protein, designed via computer modeling and analysis that mimicks the main function of haloalkane dehalogenase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-sulfate buffer, pH 7.5, 1 mM EDTA, 1 mM beta-mercaptoethanol, less than 20% loss of activity after several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
five mini proteins are designed via computer modeling and analysis that mimick the main function of haloalkane dehalogenase. A mini protein with 86 amino acids is chosen for His-tag purification
recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dhlA, expression of a saturation mutagenesis library in Escherichia coli strain BL21(DE3)
multiple alignment of protein sequences of cloned haloalkane dehalogenases
recombinant expression as N-terminally His-tagged enzyme in Escherichia coli TOP10
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biocatalyzation and bioremediation of haloalkanes
environmental protection
because the halogenated substrates are often environmentally toxic industrial byproducts, the enzyme has been suggested to be an useful catalyst for biodegradation and bioremediation
industry
a stable mini protein is successfully designed and may be used as bioreceptors in the haloalkane sensor that is suitable for industrial application
biotechnology
-
hydrolytic dehalogenation of 1-chlorobutane in a non-conventional gas phase system under a controlled water thermodynamic activity and in aqueous phase. Maximal transformation capacity of 1.4 g of 1-chlorobutane per day with 1 g of Xanthobacter autotrophicus lyophilized cells. Comparison of Rhodococcus erythropolis and Xanthobacter autotrophicus
synthesis
-
haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
Prince, R.C.
Haloalkane dehalogenase caught in the act
Trends Biochem. Sci.
19
3-4
1994
Xanthobacter autotrophicus, Rhodococcus sp., Xanthobacter autotrophicus GJ10
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
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
-
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
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
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)
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
Pikkemaat, M.G.; Ridder, I.S.; Rozeboom, H.J.; Klak, K.H.; Dijkstra, B.W.; Janssen, D.B.
Crystallographic and kinetic evidence o a collison complex formed during halide import in haloalkane dehalogenase
Biochemistry
38
12052-12061
1999
Xanthobacter autotrophicus (P22643)
Damborsky, J.; Koca, J.
Analysis of the reaction mechnism and substrate specificity of haloalkane dehalogenases by sequential and structural comparisons
Protein Eng.
12
989-998
1999
Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13064, Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26, Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
Lau, E.Y.; Kahn, K.; Bash, P.A.; Bruice, T.C.
The importance of reactant positioning in enzyme catalysis: a hybrid quantum mechanics /molecular mechanics study of a haloalkane dehalogenase
Proc. Natl. Acad. Sci. USA
97
9937-9942
2000
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
Kmunicek, J.; Luengo, S.; Gago, F.; Ortiz, A.R.; Wade, R.C.; Damborsky, J.
Comparative binding energy analysis of the substrate specificity of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
Biochemistry
40
8905-8917
2001
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
Bohac, M.; Nagata, Y.; Prokop, M.; Monincova, M.; Tsuda, M.; Koca, J.; Damborsky, J.
Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis
Biochemistry
41
14272-14280
2002
Rhodococcus erythropolis, Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26, Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643)
Nam, K.; Prat-Resina, X.; Garcia-Viloca, M.; Devi-Kesavan, L.S.; Gao, J.
Dynamics of an enzymatic substitution reaction in haloalkane dehalogenase
J. Am. Chem. Soc.
126
1369-1376
2004
Xanthobacter autotrophicus (P22643)
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
145-157
2006
Xanthobacter autotrophicus
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.
91
304-313
2005
Xanthobacter autotrophicus, Rhodococcus erythropolis, Rhodococcus erythropolis NCIMB 13064
Soriano, A.; Silla, E.; Tunon, I.; Ruiz-Lopez, M.F.
Dynamic and electrostatic effects in enzymatic processes. An analysis of the nucleophilic substitution reaction in haloalkane dehalogenase
J. Am. Chem. Soc.
127
1946-1957
2005
Xanthobacter autotrophicus (P22643)
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)
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)
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
113
3257-3263
2009
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643)
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
1192-1198
2008
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
Koudelakova, T.; Chovancova, E.; Brezovsky, J.; Monincova, M.; Fortova, A.; Jarkovsky, J.; Damborsky, J.
Substrate specificity of haloalkane dehalogenases
Biochem. J.
435
345-354
2011
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970, Bradyrhizobium elkanii, Bradyrhizobium elkanii USDA94, Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110, Mycobacterium tuberculosis variant bovis, Mycobacterium tuberculosis variant bovis 5033/66, Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13064, Rhodopirellula baltica, Rhodopirellula baltica SH1, Sphingobium indicum, Sphingobium indicum UT26, Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
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, Bradyrhizobium japonicum USDA 110, Mesorhizobium loti, Mesorhizobium loti MAFF303099, Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB13064, Sphingomonas paucimobilis, Sphingomonas paucimobilis UT26, Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
-
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)
Nagata, Y.; Ohtsubo, Y.; Tsuda, M.
Properties and biotechnological applications of natural and engineered haloalkane dehalogenases
Appl. Microbiol. Biotechnol.
99
9865-9881
2015
Agrobacterium tumefaciens (E2RV69), Agrobacterium tumefaciens C58 / ATCC 33970 (E2RV69), Alcanivorax dieselolei, Alcanivorax dieselolei B-5, Arthrobacter sp., Bradyrhizobium elkanii (E2RV62), Bradyrhizobium elkanii USDA94 (E2RV62), Bradyrhizobium japonicum (P59337), Bradyrhizobium japonicum USDA 110 (P59337), Corynebacterium sp., Marinobacter sp. (A3JB27), Mesorhizobium loti (Q98C03), Mesorhizobium loti MAFF303099 (Q98C03), Mycobacterium avium (Q93K00), Mycobacterium avium N85 (Q93K00), Mycobacterium sp. (Q9ZER0), Mycobacterium sp. GP1 (Q9ZER0), Mycobacterium tuberculosis (P9WMR9), Mycobacterium tuberculosis H37Rv (P9WMR9), Mycobacterium tuberculosis variant bovis (A4Q9R7), Mycobacterium tuberculosis variant bovis (Q6EUU8), Mycobacterium tuberculosis variant bovis (Q9XB14), Mycobacterium tuberculosis variant bovis 5033/66 (A4Q9R7), Mycobacterium tuberculosis variant bovis 5033/66 (Q6EUU8), Mycobacterium tuberculosis variant bovis 5033/66 (Q9XB14), Plesiocystis pacifica (A6G7B1), Psychrobacter cryohalolentis (Q1QBB9), Psychrobacter cryohalolentis K5 (Q1QBB9), Rhodobacteraceae bacterium UDC319 (A0A023I2Y1), Rhodococcus rhodochrous (P0A3G2), Rhodococcus rhodochrous NCIMB 13064 (P0A3G2), Rhodococcus sp., Rhodopirellula baltica (G3XCP3), Rhodopirellula baltica SH1 (G3XCP3), Sphingobium indicum, Sphingobium indicum (P51698), Sphingobium indicum B90A, Sphingobium indicum UT26 (P51698), Sphingobium sp. (A4PEU6), Sphingobium sp. MI1205 (A4PEU6), Sphingomonas sp., Sphingomonas sp. BHC-A, Strongylocentrotus purpuratus, Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643)
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
11505-11512
2018
Xanthobacter autotrophicus (P22643), Xanthobacter autotrophicus GJ10 (P22643), Xanthobacter autotrophicus GJ10
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