Any feedback?
Information on EC 3.8.1.9 - (R)-2-haloacid dehalogenase and Organism(s) Rhizobium sp. and UniProt Accession Q8KLS9
for references in articles please use BRENDA:EC3.8.1.9Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.8.1.9 (R)-2-haloacid dehalogenaseIUBMB Comments
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)]
Specify your search results
Word Map
- 3.8.1.9
-
dehalogenation
- putida
- dexamethasone
-
rhizobium
-
2-haloalkanoic
-
l-enantiomer
- 2-chloropropionate
-
enantiomers
-
2-haloacids
-
dl-2-haloacid
- monobromoacetate
- monochloroacetate
- dendrimer
-
tear
- halide
-
inflamed
-
subconjunctival
-
biodistribution
-
halogenated
The taxonomic range for the selected organisms is: Rhizobium sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-dex, d-2-haloacid dehalogenase, deh138, d-specific dehalogenase, hadd aj1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-haloalkanoic acid dehalogenase
-
-
-
-
2-haloalkanoid acid halidohydrolase
-
-
-
-
D-2-haloacid dehalogenase
D-DEX
-
-
-
-
D-2-haloacid dehalogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(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
(R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
the reaction mechanism of dehalogenation is catalysed by hydrolytic SN2-substitution reaction
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)]
CAS REGISTRY NUMBER
COMMENTARY
119345-29-8
-
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
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
additional information
three-dimensional structure of DehD wild-type and Y135A mutant
additional information
-
three-dimensional structure of DehD wild-type and Y135A mutant
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R134A
site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates
Y135A
site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dehD, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
D-specific dehalogenase DehD from Rhizobium sp. strain RC1 can be exploited as a potential target enzyme for industrial, pharmaceutical and other biotechnological applications
additional information
-
D-specific dehalogenase DehD from Rhizobium sp. strain RC1 can be exploited as a potential target enzyme for industrial, pharmaceutical and other biotechnological applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leigh, J.A.; Skinner, A.J.; Cooper, R.A.
Partial purification, stereospecificity and stoichiometry of three dehalogenases from a Rhizobium species
FEMS Microbiol. Lett.
49
353-356
1988
Rhizobium sp.
-
Soda, K.; Kurihara, T.; Liu, J.Q.; Nardi-Dei, V.; Park, C.; Miyagi, M.; Tsunasawa, S.; Esaki, N.
Bacterial 2-haloacid dehalogenases: Structures and catalytic properties
Pure Appl. Chem.
68
2097-2103
1996
Pseudomonas putida, Pseudomonas putida AJ1/23, Rhizobium sp.
-
Cairns, S.S.; Cornish, A.; Cooper, R.A.
Cloning, sequencing and expression in Escherichia coli of two Rhizobium sp. genes encoding haloalkonoate dehalogenases of opposite stereospecificity
Eur. J. Biochem.
235
744-749
1996
Rhizobium sp.
Sudi, I.Y.; Shamsir, M.S.; Jamaluddin, H.; Wahab, R.A.; Huyop, F.
Interactions of non-natural halogenated substrates with D-specific dehalogenase (DehD) mutants using in silico studies
Biotechnol. Biotechnol. Equip.
28
949-957
2014
Rhizobium sp. (Q8KLS9), Rhizobium sp.
EXTERNAL LINKS (specific for EC-Number 3.8.1.9)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
