Application | Comment | Organism |
---|---|---|
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 | Rhizobium sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic studies | Rhizobium sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-2-haloacid + H2O | Rhizobium sp. | - |
(S)-2-hydroxyacid + halide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhizobium sp. | Q8KLS9 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(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 | Rhizobium sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-2-haloacid + H2O | - |
Rhizobium sp. | (S)-2-hydroxyacid + halide | - |
? | |
2,2-dichloropropionate + H2O | - |
Rhizobium sp. | ? | - |
? | |
3-chloropropionate + H2O | - |
Rhizobium sp. | 3-hydroxypropionate + chloride | - |
? | |
D-2-bromopropionate + H2O | - |
Rhizobium sp. | L-2-hydroxypropionate + bromide | - |
? | |
D-2-chloropropionate + H2O | - |
Rhizobium sp. | L-2-hydroxypropionate + chloride | - |
? | |
DL-2,3-dichloropropionate + H2O | - |
Rhizobium sp. | ? | - |
? | |
monobromoacetate + H2O | - |
Rhizobium sp. | hydroxyacetate + bromide | - |
? | |
monochloroacetate + H2O | - |
Rhizobium sp. | hydroxyacetate + chloride | - |
? | |
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 | Rhizobium sp. | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | 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 | Rhizobium sp. |
Synonyms | Comment | Organism |
---|---|---|
D-specific dehalogenase | - |
Rhizobium sp. |
DehD | - |
Rhizobium sp. |
General Information | Comment | Organism |
---|---|---|
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 | Rhizobium sp. |