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Literature summary for 3.1.1.1 extracted from
- Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides (2017), Sci. Rep., 7, 3461 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged wild-type and truncated mutant EstPS1s in Escherichia coli, the mutant enzymes are found predominantly in inclusion bodies, the soluble enzyme is secreted | Pseudomonas synxantha |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of an AT domain-truncated carboxylesterase (EstPS1DELTAAT) mutant. The mutant shows a clearly decreased secretion rate, owing to the AT domain strongly improving secretory expression in the heterogeneous system. The mutant shows markedly reduced activity and thermostability compared to the wild-type enzyme | Pseudomonas synxantha |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| inner membrane | - |
Pseudomonas synxantha | - |
- |
| intracellular | the AT domain contains an N-terminal signal sequence that targets the enzyme to the Sec machinery in the inner membrane | Pseudomonas synxantha | 5622 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas synxantha | A0A0K0Q1Y2 | isolated from oil well-produced water | - |
| Pseudomonas synxantha PS1 | A0A0K0Q1Y2 | isolated from oil well-produced water | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and truncated mutant EstPS1s from Escherichia coli, the mutant enzymes are solubilized from inclusion bodies | Pseudomonas synxantha |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 13.6 | - |
purified recombinant wild-type enzyme, substrate carbaryl, pH 8.0, 60°C | Pseudomonas synxantha |
| 973 | - |
purified recombinant His-tagged AT-domain truncated enzyme mutant, substrate 4-nitrophenol butyrate, pH 8.0, 60°C | Pseudomonas synxantha |
| 2226 | - |
purified recombinant His-tagged wild-type enzyme, substrate 4-nitrophenol butyrate, pH 8.0, 60°C | Pseudomonas synxantha |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl acetate + H2O | - |
Pseudomonas synxantha | 4-nitrophenol + acetate | - |
? |  |
| 4-nitrophenyl acetate + H2O | - |
Pseudomonas synxantha PS1 | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl butyrate + H2O | best substrate | Pseudomonas synxantha | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | best substrate | Pseudomonas synxantha PS1 | 4-nitrophenol + butyrate | - |
? | |
| bifenthrin + H2O | - |
Pseudomonas synxantha | ? | - |
? | |
| carbaryl + H2O | - |
Pseudomonas synxantha | ? | - |
? | |
| cis-cypermethrin + H2O | - |
Pseudomonas synxantha | ? | - |
? | |
| cis-cypermethrin + H2O | - |
Pseudomonas synxantha PS1 | ? | - |
? | |
| fenpropathrin + H2O | - |
Pseudomonas synxantha | ? | - |
? | |
| fenvalerate + H2O | - |
Pseudomonas synxantha | ? | - |
? | |
| fenvalerate + H2O | - |
Pseudomonas synxantha PS1 | ? | - |
? | |
| additional information | enzyme EstPS1 degrades various pyrethroid pesticides, the hydrolysis efficiencies are dependent on the pyrethroid molecular structure. EstPS1 degrades all the tested pyrethroid pesticides and hydrolyses the p-nitrophenyl esters of medium- to short-chain fatty acids, indicating that EstPS1 is an esterase with broad specificity. EstPS1 hydrolyzes the pesticides at different hydrolysis rates in the following decreasing order: carbaryl, fenpropathrin, trans-cypermethrin, cis-cypermethrin, fenvalerate, and bifenthrin. High activity with 4-nitrophenyl ester substrates at chain lengths of C2-C8, low activity with substrates of C10 and C12 chain length, no activity with C14 and C16 substrates | Pseudomonas synxantha | ? | - |
? | |
| additional information | enzyme EstPS1 degrades various pyrethroid pesticides, the hydrolysis efficiencies are dependent on the pyrethroid molecular structure. EstPS1 degrades all the tested pyrethroid pesticides and hydrolyses the p-nitrophenyl esters of medium- to short-chain fatty acids, indicating that EstPS1 is an esterase with broad specificity. EstPS1 hydrolyzes the pesticides at different hydrolysis rates in the following decreasing order: carbaryl, fenpropathrin, trans-cypermethrin, cis-cypermethrin, fenvalerate, and bifenthrin. High activity with 4-nitrophenyl ester substrates at chain lengths of C2-C8, low activity with substrates of C10 and C12 chain length, no activity with C14 and C16 substrates | Pseudomonas synxantha PS1 | ? | - |
? | |
| trans-cypermethrin + H2O | - |
Pseudomonas synxantha | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 68000, about, enzyme without AT domain, sequence calculation | Pseudomonas synxantha |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EstPS1 | - |
Pseudomonas synxantha |
| pyrethroid-hydrolysing esterase | - |
Pseudomonas synxantha |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Pseudomonas synxantha |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 80 | over 80% of maximal activity within this range, profile overview | Pseudomonas synxantha |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | 100 | enzyme EstPS1 shows high thermostability, and the half-lives at 60, 70, 80, 90, and 100°C are 14 h, 2 h, 31 min, 10 min, and 1 min, respectively | Pseudomonas synxantha |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Pseudomonas synxantha |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | over 50% of maximal activity within this range, profile overview | Pseudomonas synxantha |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Pseudomonas synxantha | sequence calculation | - |
4.81 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | carboxylesterases are members of the alpha/beta hydrolase family, found in animals, plants, and microorganisms. EstPS1 has a single catalytic domain of the alpha/beta hydrolase family and belongs to the carboxylesterase family. And the EstPS1 carboxylesterase is an intracellular serine hydrolase that belongs to the lipase GDSL-2 family. Members of the GDSL family possess the GDSX motif (equivalent to the classical GXSXG motif of lipases/esterases), in which nucleophilic Ser is located in block I of the protein | Pseudomonas synxantha |
| additional information | structure homology analysis, the 640-amino acid carboxylesterase (EstPS1) contains an autotransporter (AT) domain (357-640 amino acids) that strongly improves secretory expression in the heterogeneous system | Pseudomonas synxantha |
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