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Literature summary for 3.1.1.1 extracted from
- Gene cloning, expression, and characterization of a new carboxylesterase from Serratia sp. SES-01: comparison with Escherichia coli BioHe enzyme (2009), J. Microbiol. Biotechnol., 19, 147-154.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | 10% activation of recombinant BioHs at 10 mM | Serratia sp. |  |
| Co2+ | 150% activation of recombinant BioHe at 5-10 mM | Escherichia coli | |
| Mn2+ | 10% activation of recombinant BioHs at 10 mM | Serratia sp. | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bioHe, DNA and amino acid sequence determination and analysis, sequence compariosns, overview | Escherichia coli |
| gene bioHs, cloned from the genomic DNA library, DNA and amino acid sequence determination and analysis, expression of the HIs-tagged enzyme in Escherichia coli strain JM109 | Serratia sp. |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1-butanol | 62% inhibition of BioHe at 30% | Escherichia coli | |
| 1-butanol | 95% inhibition of BioHs at 30% | Serratia sp. | |
| acetone | 15% inhibition of BioHe at 30% | Escherichia coli | |
| acetone | 96% inhibition of BioHs at 30% | Serratia sp. | |
| acetonitrile | 89% inhibition of BioHe at 30% | Escherichia coli | |
| acetonitrile | 97% inhibition of BioHs at 30% | Serratia sp. | |
| Cu2+ | 30% inhibition of recombinant BioHe at 5-10 mM | Escherichia coli | |
| DMSO | 22% inhibition of BioHs at 30% | Serratia sp. | |
| ethanol | 16% inhibition of BioHe at 30% | Escherichia coli | |
| ethanol | 95% inhibition of BioHs at 30% | Serratia sp. | |
| Isopropanol | 70% inhibition of BioHe at 30% | Escherichia coli | |
| Isopropanol | 96% inhibition of BioHs at 30% | Serratia sp. | |
| methanol | 7% inhibition of BioHe at 30% | Escherichia coli | |
| methanol | 98% inhibition of BioHs at 30% | Serratia sp. | |
| additional information | no inhibition by DMSO at 10-30% | Escherichia coli | |
| SDS | 52% inhibition of recombinant BioHe at 0.2% | Escherichia coli | |
| SDS | almost complete inhibition of recombinant BioHs at 0.2% | Serratia sp. | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no effects by EDTA, and 0.2% to 5% Triton X-100, Tween 20, and Tween 80. BioHe is no metalloenzyme | Escherichia coli | |
| additional information | no effects by EDTA, and 0.2% to 5% Triton X-100, Tween 20, and Tween 80. BioHs is no metalloenzyme | Serratia sp. |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28300 | - |
x * 28300, SDS-PAGE | Serratia sp. |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | BioHe shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHe BioH also shows low enzymatic activities for thioesterase, lipase, and aminopeptidase, but shows no detectable enzymatic activity for phosphatase, trypsin-like endopeptidase, or perhydrolase | ? | - |
? | |
| additional information | Serratia sp. | BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis | ? | - |
? | |
| additional information | Serratia sp. SES-01 | BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
gene bioHe | - |
| Serratia sp. | B0M0H6 | gene bioHs | - |
| Serratia sp. SES-01 | B0M0H6 | gene bioHs | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged BioHs from Escherichia coli strain JM109 by metal affinity chromatography | Serratia sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl acetate + H2O | - |
Escherichia coli | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Serratia sp. | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Serratia sp. SES-01 | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Escherichia coli | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Serratia sp. | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Serratia sp. SES-01 | 4-nitrophenol + butyrate | - |
? | |
| additional information | BioHe shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHe BioH also shows low enzymatic activities for thioesterase, lipase, and aminopeptidase, but shows no detectable enzymatic activity for phosphatase, trypsin-like endopeptidase, or perhydrolase | Escherichia coli | ? | - |
? | |
| additional information | BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis | Serratia sp. | ? | - |
? | |
| additional information | BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis | Serratia sp. SES-01 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 28300, SDS-PAGE | Serratia sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BioHe | - |
Escherichia coli |
| BioHs | - |
Serratia sp. |
| More | the enzyme belongs to the BioH enzyme family | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 30 | - |
Escherichia coli |
| 30 | 40 | - |
Serratia sp. |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 15 | 60 | activity profile, overview | Escherichia coli |
| 15 | 60 | activity profile, overview | Serratia sp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
inactivation of BioHs after 30 min | Serratia sp. |
| 55 | - |
30 min, purified recombinant enzyme, more than 95% activity of BioHe remaining at 55°C | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9 | 90% of maximal activity within this range | Escherichia coli |
| 7 | 9 | 90% of maximal activity within this range | Serratia sp. |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | activity profile, inactive at pH 3.0, overview | Escherichia coli |
| 4 | 10 | activity profile, inactive at pH 3.0, overview | Serratia sp. |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
inactivation after 1 h | Escherichia coli |
| 3 | - |
inactivation after 1 h | Serratia sp. |
| 3.5 | - |
50% activity remaining after 1 h | Escherichia coli |
| 4.5 | - |
50% activity remaining after 1 h | Serratia sp. |
| 5 | 10 | completely stable after 1 h | Escherichia coli |
| 5 | 10 | completely stable after 1 h | Serratia sp. |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | BioHe also functions as a pimeloyl-CoA thioesterase/acyltransferase for the biotin synthetic pathway | Escherichia coli |
| additional information | BioHs also functions as a pimeloyl-CoA thioesterase/acyltransferase for the biotin synthetic pathway | Serratia sp. |
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