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Literature summary for 3.8.1.9 extracted from

  • 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 (2014), Biotechnol. Biotechnol. Equip., 28, 949-957.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene dehD, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli Rhizobium sp.

Protein Variants

Protein Variants Comment Organism
R134A site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates Rhizobium sp.
Y135A site-directed mutagenesis, the DehD mutant variant demonstrates increased propensity for binding haloalkanoic acid and is non-stereospecific towards halogenated substrates Rhizobium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DL-2,3-dichloropropionate + H2O Rhizobium sp.
-
?
-
?
monobromoacetate + H2O Rhizobium sp.
-
2-hydroxyacetate + bromide
-
?
monochloroacetate + H2O Rhizobium sp.
-
2-hydroxyacetate + chloride
-
?
additional information Rhizobium sp. 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Rhizobium sp. Q8KLS9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Rhizobium sp.

Reaction

Reaction Comment Organism Reaction ID
(R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide the reaction mechanism of dehalogenation is catalysed by hydrolytic SN2-substitution reaction Rhizobium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2-dichloropropionate + H2O
-
Rhizobium sp. ?
-
?
3-chloropropionate + H2O
-
Rhizobium sp. 3-hydroxypropionate + chloride
-
?
dibromoacetate + H2O
-
Rhizobium sp. ?
-
?
dichloroacetate + H2O
-
Rhizobium sp. ?
-
?
DL-2,3-dichloropropionate + H2O
-
Rhizobium sp. ?
-
?
L-2-bromopropionate + H2O
-
Rhizobium sp. ?
-
?
L-2-chloropropionate + H2O
-
Rhizobium sp. ?
-
?
monobromoacetate + H2O
-
Rhizobium sp. 2-hydroxyacetate + bromide
-
?
monochloroacetate + H2O
-
Rhizobium sp. 2-hydroxyacetate + chloride
-
?
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 Rhizobium sp. ?
-
?
tribromoacetate + H2O
-
Rhizobium sp. ?
-
?
trichloroacetate + H2O
-
Rhizobium sp. ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure of DehD wild-type and Y135A mutant Rhizobium sp.

Synonyms

Synonyms Comment Organism
D-2-haloacid dehalogenase
-
Rhizobium sp.
D-specific dehalogenase
-
Rhizobium sp.
DehD
-
Rhizobium sp.