Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2, see also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)
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(R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
proposed reaction mechanism, conserved residue Arg134 plays a key role in the dehalogenation process. Residues Arg107, Arg134 and Tyr135 interact with the substrates and are the catalytic residues of DehD that are involved in the dehalogenation of D-2-chloropropionate and D-2-bromopropionate, while Glu20 activates the water molecule that attacks the carbon halogen bond on the alpha-carbon, thereby releasing chloride ion
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-haloacid halidohydrolase
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
the D-2-haloacid dehalogenase of D-specific dehalogenase (DehD) from Rhizobium sp. RC1 catalyses the hydrolytic dehalogenation of D-haloalkanoic acids, inverting the substrate-product configuration and thereby forming the corresponding L-hydroxyalkanoic acids. Molecular docking of substrates into the active site of the DehD mutants R134A and Y135A, which produce altered catalytic functions. The mutants interact strongly with substrates that wild-type DehD does not interact with or degrade. The interaction is particularly enhanced with 3-chloropropionate, in addition to monobromoacetate, monochloroacetate and D,L-2,3-dichloropropionate. The mutants exhibit a strong interaction with 3-chloropropionate at Arg134
the D-2-haloacid dehalogenase of D-specific dehalogenase (DehD) from Rhizobium sp. RC1 catalyses the hydrolytic dehalogenation of D-haloalkanoic acids, inverting the substrate-product configuration and thereby forming the corresponding L-hydroxyalkanoic acids. Molecular docking of substrates into the active site of the DehD mutants R134A and Y135A, which produce altered catalytic functions. The mutants interact strongly with substrates that wild-type DehD does not interact with or degrade. The interaction is particularly enhanced with 3-chloropropionate, in addition to monobromoacetate, monochloroacetate and D,L-2,3-dichloropropionate. The mutants exhibit a strong interaction with 3-chloropropionate at Arg134
molecular docking of D-2-chloropropionate, D-2-bromopropionate, monochloroacetate, monobromoacetate, 2,2-dichloropropionate, DL-2,3-dichloropropionate, and 3-chloropropionate into the DehD active site, residues Arg107, Arg134 and Tyr135 interact with D-2-chloropropionate, and Glu20 activates the water molecule for hydrolytic dehalogenation
molecular docking of D-2-chloropropionate, D-2-bromopropionate, monochloroacetate, monobromoacetate, 2,2-dichloropropionate, DL-2,3-dichloropropionate, and 3-chloropropionate into the DehD active site, residues Arg107, Arg134 and Tyr135 interact with D-2-chloropropionate, and Glu20 activates the water molecule for hydrolytic dehalogenation
the D-2-haloacid dehalogenase of D-specific dehalogenase (DehD) from Rhizobium sp. RC1 catalyses the hydrolytic dehalogenation of D-haloalkanoic acids, inverting the substrate-product configuration and thereby forming the corresponding L-hydroxyalkanoic acids. Molecular docking of substrates into the active site of the DehD mutants R134A and Y135A, which produce altered catalytic functions. The mutants interact strongly with substrates that wild-type DehD does not interact with or degrade. The interaction is particularly enhanced with 3-chloropropionate, in addition to monobromoacetate, monochloroacetate and D,L-2,3-dichloropropionate. The mutants exhibit a strong interaction with 3-chloropropionate at Arg134
the D-2-haloacid dehalogenase of D-specific dehalogenase (DehD) from Rhizobium sp. RC1 catalyses the hydrolytic dehalogenation of D-haloalkanoic acids, inverting the substrate-product configuration and thereby forming the corresponding L-hydroxyalkanoic acids. Molecular docking of substrates into the active site of the DehD mutants R134A and Y135A, which produce altered catalytic functions. The mutants interact strongly with substrates that wild-type DehD does not interact with or degrade. The interaction is particularly enhanced with 3-chloropropionate, in addition to monobromoacetate, monochloroacetate and D,L-2,3-dichloropropionate. The mutants exhibit a strong interaction with 3-chloropropionate at Arg134
the growth of DEH 138 strain culture is not affected by salinity of 0-15%. Growth on 1,2-dichloroethane, 3-chloro-1,2-propanediol, 2,2-dichloropropionic acid, and 2,4,6-trichlorophenol medium
three-dimensional enzyme structure modeling and analysis, molecular dynamics simulations, comparison with Pseudomonas putida enzyme structures from strain AJ1 and PP3, overview. Residues Arg107, Arg134 and Tyr135 interact with D-2-chloropropionate, and Glu20 activated the water molecule for hydrolytic dehalogenation
three-dimensional enzyme structure modeling and analysis, molecular dynamics simulations, comparison with Pseudomonas putida enzyme structures from strain AJ1 and PP3, overview. Residues Arg107, Arg134 and Tyr135 interact with D-2-chloropropionate, and Glu20 activated the water molecule for hydrolytic dehalogenation
three-dimensional enzyme structure modeling and analysis. The secondary structure is predominantly alpha-helical. The N-terminus consists of 24 residues, primarily in the loop region, whereas the C-terminus had only one residue in the loop region. The D-2-specific dehalogenase (DehD) is predominantly made of alpha-helices and coil-coils with highly curved bends and is without strands, secondary structural elements, overview
three-dimensional enzyme structure modeling and analysis. The secondary structure is predominantly alpha-helical. The N-terminus consists of 24 residues, primarily in the loop region, whereas the C-terminus had only one residue in the loop region. The D-2-specific dehalogenase (DehD) is predominantly made of alpha-helices and coil-coils with highly curved bends and is without strands, secondary structural elements, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained by hanging-drop vapour diffusion method. The enzyme is crystallized in the presence of the substrate D-2-chloropropionate at pH 5.5-6.4 and 4°C. 2.64 A resolution
crystals are obtained by the hanging-drop vapor-diffusion method. Crystals of the D205N mutant with D-2-chloropropionate are prepared by co-crystallization using the sitting drop method
activity with D-2-chloropropionate is 10.1% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 13fold higher compared to mutant enzyme
activity with D-2-chloropropionate is 36.6% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 4fold higher compared to mutant enzyme
site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates
site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates
the mutation enlarges the size of the channel and allows the enzyme to accommodate L-enantiomers (L-2-bromopropionate). The wing flip of I288 induces hydrophobic interactions with the L-enantiomer and directly affects the catalytic efficiency
activity with D-2-chloropropionate is 1.2% compared to activity of the wild-type enzyme. The kcat value of wild-type enzyme is 355fold higher compared to mutant enzyme
D-specific dehalogenase DehD from Rhizobium sp. strain RC1 can be exploited as a potential target enzyme for industrial, pharmaceutical and other biotechnological applications
D-specific dehalogenase DehD from Rhizobium sp. strain RC1 can be exploited as a potential target enzyme for industrial, pharmaceutical and other biotechnological applications
Biochemical and molecular characterisation of the 2,3-dichloro-1-propanol dehalogenase and stereospecific haloalkanoic dehalogenases from a versatile Agrobacterium sp