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Literature summary for 3.8.1.5 extracted from
- Cloning, expression, purification and three-dimensional structure prediction of haloalkane dehalogenase from a recently isolated Ancylobacter aquaticus strain UV5 (2014), Protein Expr. Purif., 99, 10-17.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene dhlA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression in Escherichia coli strain BL21(DE3) | Ancylobacter aquaticus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| SDS | 76% inhibition at 1%, 94% at 5% | Ancylobacter aquaticus |  |
| Triton X100 | 35% inhibition at 1%, 83% at 5% | Ancylobacter aquaticus | |
| Tween 80 | 26% inhibition at 1%, 75% at 5% | Ancylobacter aquaticus | |
| Urea | 79% inhibitin at 4 M, 93% at 8 M | Ancylobacter aquaticus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Ancylobacter aquaticus | |
| 0.842 | - |
1,2-Dichloroethane | pH 9.0, 37°C, recombinant enzyme | Ancylobacter aquaticus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no effect by EDTA, Ca2+, Cu2+, Fe2+, Mn2+, Mg2+, and Zn2+ at 1-5 mM | Ancylobacter aquaticus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 35000 | - |
x * 35000, recombinant enzyme, SDS-PAGE, x * 35144, sequence calculation | Ancylobacter aquaticus |
| 35144 | - |
x * 35000, recombinant enzyme, SDS-PAGE, x * 35144, sequence calculation | Ancylobacter aquaticus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,2-dichloroethane + H2O | Ancylobacter aquaticus | - |
2-chloroethanol + chloride | - |
? | |
| 1,2-dichloroethane + H2O | Ancylobacter aquaticus UV5 | - |
2-chloroethanol + chloride | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ancylobacter aquaticus | B8YPW8 | gene dhlA | - |
| Ancylobacter aquaticus UV5 | B8YPW8 | gene dhlA | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme 28.1fold from Escherichia coli strain BL21(DE3) by ultrafiltration, anion exchange chromatography, and gel filtration | Ancylobacter aquaticus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 92.3 | - |
purified recombinant enzyme, substrate 1,2-dichloroethane, pH 9.0, 37°C | Ancylobacter aquaticus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,2-dichloroethane + H2O | - |
Ancylobacter aquaticus | 2-chloroethanol + chloride | - |
? | |
| 1,2-dichloroethane + H2O | - |
Ancylobacter aquaticus UV5 | 2-chloroethanol + chloride | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 35000, recombinant enzyme, SDS-PAGE, x * 35144, sequence calculation | Ancylobacter aquaticus |
| More | three-dimensional enzyme structure analysis modeling | Ancylobacter aquaticus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DhlA | - |
Ancylobacter aquaticus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Ancylobacter aquaticus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 65 | activity range, profile overview | Ancylobacter aquaticus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
purified recombinant enzyme, loss of 20% activity within 24 h | Ancylobacter aquaticus |
| 50 | - |
purified recombinant enzyme retains approximately 50% of its activity after 1 h of incubation at 50°C, inactivation after 4 h | Ancylobacter aquaticus |
| 70 | - |
purified recombinant enzyme inactivation within 1 h | Ancylobacter aquaticus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.37 | - |
1,2-Dichloroethane | pH 9.0, 37°C, recombinant enzyme | Ancylobacter aquaticus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Ancylobacter aquaticus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 11 | activity range, profile overview | Ancylobacter aquaticus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Ancylobacter aquaticus | sequence calculation | - |
4.65 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the alpha/beta hydrolase family with a catalytic triad composed of Asp-His-Asp in its active site | Ancylobacter aquaticus |
| additional information | three-dimensional enzyme structure analysis modeling | Ancylobacter aquaticus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.8 | - |
1,2-Dichloroethane | pH 9.0, 37°C, recombinant enzyme | Ancylobacter aquaticus | |
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