Application | Comment | Organism |
---|---|---|
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 | Rhodococcus rhodochrous |
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 | Rhodococcus rhodochrous |
Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged wild-type and mutant enzymes | Rhodococcus rhodochrous |
Protein Variants | Comment | Organism |
---|---|---|
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 | Rhodococcus rhodochrous |
I135F/C176Y/V245F/L246I/Y273F | structural modeling of the mutant compared to the wild-type DhaA31 using the wild-type crystal structure | Rhodococcus rhodochrous |
additional information | library screening for mutants with altered enantioselectivity with substrate 1,2,3-trichloropropane compared to DhaA31 wild-type, overview | Rhodococcus rhodochrous |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics with substrate1,2,3-trichloropropane, wild-type and mutant enzymes, overview | Rhodococcus rhodochrous |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2,3-trichloropropane + H2O | Rhodococcus rhodochrous | - |
(RS)-2,3-dichloropropan-1-ol + chloride | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus rhodochrous | - |
gene dhaA | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography | Rhodococcus rhodochrous |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2,3-trichloropropane + H2O | - |
Rhodococcus rhodochrous | (RS)-2,3-dichloropropan-1-ol + chloride | - |
? | |
1,2,3-trichloropropane + H2O | 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 | Rhodococcus rhodochrous | (RS)-2,3-dichloropropan-1-ol + chloride | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme is composed of a main domain and a cap domain, with a catalytic pentad located between these domains | Rhodococcus rhodochrous |
Synonyms | Comment | Organism |
---|---|---|
DhaA | - |
Rhodococcus rhodochrous |
DhaA31 | - |
Rhodococcus rhodochrous |
General Information | Comment | Organism |
---|---|---|
evolution | the haloalkane dehalogenases form a subclass of enzymes in the alpha/beta-hydrolase fold superfamily | Rhodococcus rhodochrous |