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Information on EC 3.8.1.5 - haloalkane dehalogenase and Organism(s) Rhodococcus rhodochrous and UniProt Accession P0A3G2
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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: Rhodococcus rhodochrous
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, ylehd, 1-chlorohexane halidohydrolase, linbut, ehld-b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-chlorohexane halidohydrolase
-
-
-
-
1-haloalkane dehalogenase
-
-
-
-
DhaA
HLD
DhaA
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-haloalkane + H2O = a primary alcohol + halide
acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds
-
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
-
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
1,2,3-tribromopropane + H2O
2,3-dibromo-1-propanol + bromide
-
-
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichloro-1-propanol + chloride
-
low activity
-
-
?
1,2,3-trichloropropane + H2O
2,3-dichlorpropane-1-ol + chloride
-
-
-
ir
1,3-dibromopropane + H2O
3-bromo-1-propanol + bromide
-
best substrate, the release of product 3-bromo-1-propanol is the rate limiting step
-
-
?
haloalkane + H2O
alcohol + halide
-
comparison of substrate specificities and classification
-
-
?
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-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
?
-
substrate of DhaA31, a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
-
-
?
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
-
-
?
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
1,2,3-trichloropropane + H2O
(RS)-2,3-dichloropropan-1-ol + chloride
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.9
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker
6.9
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker
additional information
additional information
-
steady-state and pre-steady-state kintic analysis, kinetic mechanism of dehalogenation
-
additional information
additional information
-
steady-state kinetics with substrate1,2,3-trichloropropane, wild-type and mutant enzymes, overview
-
additional information
additional information
-
substrate specificity and kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
rates of reaction steps
-
0.05
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker
0.08
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker
0.016
bis(2-chloroethyl) ether
37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
DhaA31 is a mutant of DhaA with enhanced catalytic activity for 1,2,3-trichloropropane
physiological function
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
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 haloalkane dehalogenases form a subclass of enzymes in the alpha/beta-hydrolase fold superfamily
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, subgroup II 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-haloalkanes 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
-
the enzyme is composed of a main domain and a cap domain, with a catalytic pentad located between these domains
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of crystal structures of haloalkane dehalogenases by homology models
-
mutant enzymes C176Y, I135F, and I135F/C176Y are crystallized by sitting drop vapour diffusion method, using either 80 mM bicine pH 9.0, 8% (v/v) PEG 8000, and 80 mM MgCl2 or 25% (v/v) PEG 4000, 8% 2-propanol, and 100 mM sodium acetate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
I135F/C176Y/V245F/L246I/Y273F
additional information
I135F/C176Y/V245F/L246I/Y273F
-
structural modeling of the mutant compared to the wild-type DhaA31 using the wild-type crystal structure
I135F/C176Y/V245F/L246I/Y273F
four out of five mutations are located in the tunnels and introduce bulkier residues, which narrowed the p1 and p2 tunnels leading to its active site. The mutant enzyme has higher activity toward 1,2,3-trichloropropane than the wild-type, with enhancements of 32fold on the catalytic constant kcat and 26fold on the catalytic efficiency (kcat/Km). The carbon-halogen bond is the rate-limiting step in the wild-type. This step is enhanced in DhaA31 due to a significantly higher number of reactive configurations of the substrate and a decrease of the energy barrier to the SN2 reaction. C176Y and V245F are identified as the key mutations responsible for most of those improvements. The release of the alcohol product is the rate-limiting step in the mutant enzyme primarily due to the C176Y mutation. Mutational dissection of the mutant and kinetic analysis of the intermediate mutants confirm the theoretical observations
additional information
-
library screening for mutants with altered enantioselectivity with substrate 1,2,3-trichloropropane compared to DhaA31 wild-type, 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. Three saturation libraries, with a size of more than 106 cells, based on inactive variants of the haloalkane dehalogenases DhaA are successfully screened to retrieve active enzymes
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
multi-PEGylated enzyme with the thiosuccinimido butylamine linker and mono-PEGylated enzyme with the thiosuccinimido butylamine linker show the remaining activities comparable to wild-type enzyme
757271
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
immobilized enzyme shows 51.8% at room temperature for 30 days
additional information
PEGylation with the thiosuccinimido butylamine linker significantly increases the thermal stability of the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme PEGylated with the thiosuccinimido butylamine linker shows the maximum resistance to high ionic strength (1 M NaCl)
immobilized enzyme exhibits a high stability in the extreme environmental conditions. The enzyme (DhaA) suffers from poor environmental stability and difficult recovery, which significantly increase the cost of DhaA. An effective enzyme immobilization strategy is developed to overcome the disadvantages of DhaA. DhaA is physically absorbed with amine-functionalized meso-cellular foam. The MCF-absorbed enzyme is intermolecularly crosslinked with 8-arm PEG N-hydroxysuccinimide ester and then PEGylated by maleimide-thiol chemistry
PEGylation with the thiosuccinimido butylamine linker significantly increases the stability of the enzyme
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethyl sulfoxide
immobilized enzyme shows 99.8% remaining activity in 40% (v/v) dimethylsulfoxide for 5 h
DMSO
urea
immobilized enzyme shows 87.3% remaining activity in 3 M urea solution for 1 h
additional information
-
analysis of organic solvent stability of the enzyme, effects of co-solvents in enzyme assays, overview. Ethyene glycol and 1,4-dioxane have a positive effect on enantioselectivity of the enzyme
DMSO
the remaining activity of wild-type enzyme (DhaA) is 15.4% in 40% (v/v) DMSO solution at 37 °C. The remaining activity of the enzyme mono-PEGylated with the thiosuccinimido butylamine linker is 37.4% and the remaining activity of the enzyme multi-PEGylated enzyme with the thiosuccinimido butylamine linker is 48.5%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Ni-chelating affinity resin chromatography and Superdex 75 gel filtration
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography
-
recombinant N-terminally His-tagged enzyme from Escherichia coli TOP10 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dhaA, 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
biotechnology
-
enzyme, covalently immobilized on a polyethylenimine impregnated gamma-alumina support with an optimal loading of 70-75 mg/g and a maximal loading of 156 mg/g, retains more than 40% of its maximal activity, unaltered pH dependency compared to the native enzyme, thermostability and resistance towards inactivation by organic solvents of the immobilized enzyme are improved by an order of magnitude
environmental protection
synthesis
environmental protection
-
DhaA is capable of degrading 1,2,3-trichloropropane, TCP, an industrial waste product that is toxic, extremely recalcitrant to biodegradation, and expensive to dispose of by physical or chemical methods
environmental protection
DhaA displayed on the surface of Bacillus subtilis spores retains enzymatic activity, which suggests that it can be used effectively in applications including bioremediation of contaminated environments
synthesis
-
DhaA produces reaction products (R)- and (S)-2,3-dichloropropan-1-ol, which can be converted to (S)- and (R)-epihydrins, valuable fine chemicals that find application in synthetic routes to several pharmaceutical and healthcare products
synthesis
-
haloalkane dehalogenases can be used for the production of highly enantioenriched haloalcohols
synthesis
-
the enzyme might be useful for biocatalytic syntheses in industrial processes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Bosma, T.; Pikkemaat, M.G.; Kingma, J.; Dijk, J.; Janssen, D.B.
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a Rhodococcus haloalkane dehalogenase
Biochemistry
42
8047-8053
2003
Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13064
Dravis, B.C.; Swanson, P.E.; Russell, A.J.
Haloalkane hydrolysis with an immobilized haloalkane dehalogenase
Biotechnol. Bioeng.
75
416-423
2001
Rhodococcus rhodochrous
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
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
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
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
13
137-148
2012
Rhodococcus rhodochrous
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)
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, Bradyrhizobium japonicum USDA 110, Rhodococcus rhodochrous, Sphingomonas paucimobilis
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
8
314
2018
Rhodococcus rhodochrous (P0A3G2)
Wang, F.; Song, T.; Jiang, H.; Pei, C.; Huang, Q.; Xi, H.
Bacillus subtilis spore surface display of haloalkane dehalogenase DhaA
Curr. Microbiol.
76
1161-1167
2019
Rhodococcus rhodochrous (P0A3G2), Rhodococcus rhodochrous NCIMB 13064 (P0A3G2), Rhodococcus rhodochrous NCIMB 13064
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.
125
1016-1023
2019
Rhodococcus rhodochrous (P0A3G2), Rhodococcus rhodochrous
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.
254
25-33
2017
Rhodococcus rhodochrous (P0A3G2)
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