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Literature summary extracted from
- Functional characterization of a marine Bacillus esterase and its utilization in the stereo-selective production of D-methyl lactate (2016), Appl. Biochem. Biotechnol., 180, 1467-1481 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.1 | n-heptane | the enzyme activity is activated at 10% v/v by 10% | Bacillus sp. SCSIO 15121 |  |
| 3.1.1.1 | n-hexane | the enzyme activity is activated at 5% v/v by 11% | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Sodium tripolyphosphate | STPP, activates at 0.1% w/v | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Triton X-100 | activates at 0.1% w/v | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Tween 20 | activates at 0.1% w/v | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Tween 80 | activates at 0.1% w/v | Bacillus sp. SCSIO 15121 | |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | synthesis | utilization of a marine bacillus esterase in the stereo-selective production of D-methyl lactate through enzymatic kinetic resolution reactions | Bacillus sp. SCSIO 15121 |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.1 | DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged BSE01701 esterase in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha | Bacillus sp. SCSIO 15121 |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.1 | Cu2+ | 93.5% inhibition at 5 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Fe2+ | slight inhibition at 1 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | K+ | slight inhibition at 1 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Mg2+ | slight inhibition at 1 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Mn2+ | activates at 1 mM, inhibits at 5 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Ni2+ | almost complete inhibition at 1-5 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Zn2+ | complete inhibition at 1-5 mM | Bacillus sp. SCSIO 15121 | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | additional information | - |
additional information | Michaelis-Menten kinetics | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | 0.5 | - |
4-nitrophenyl butyrate | pH 8.5, 35°C, recombinant enzyme | Bacillus sp. SCSIO 15121 | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.1 | Ca2+ | activates at 1-5 mM | Bacillus sp. SCSIO 15121 | |
| 3.1.1.1 | Mn2+ | activates at 1 mM, inhibits at 5 mM | Bacillus sp. SCSIO 15121 | |
Organic Solvent Stability
| EC Number | Organic Solvent | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | 1,4-dioxane | the enzyme activity is reduced by 60-95.5% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | Acetone | the enzyme activity is reduced by 44% at 10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | dichloromethane | the enzyme activity is reduced by 73-91% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | DMSO | the enzyme activity is stable at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | Methanol | the enzyme activity is reduced by 38% at 10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | n-decane | the enzyme activity is reduced by 11-23% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | n-heptane | the enzyme activity is stable at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | n-hexane | the enzyme activity is stable at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | n-octanol | the enzyme activity is reduced by 22-90% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | n-propanol | the enzyme activity is reduced by 93.5% at 10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | tetrahydrofuran | the enzyme activity is reduced by 33-96% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | toluene | the enzyme activity is reduced by 46.5-62% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | xylene | the enzyme activity is reduced by 44% at 5-10% v/v | Bacillus sp. SCSIO 15121 |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.1 | Bacillus sp. SCSIO 15121 | A0A1B2BII0 | isolated from the Indian Ocean | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.1 | recombinant His-tagged BSE01701 esterase from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Bacillus sp. SCSIO 15121 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.1 | 4-nitrophenyl acetate + H2O | high activity | Bacillus sp. SCSIO 15121 | 4-nitrophenol + acetate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl butyrate + H2O | best 4-nitrophenyl ester substrate | Bacillus sp. SCSIO 15121 | 4-nitrophenol + butyrate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl hexanoate + H2O | lower activity | Bacillus sp. SCSIO 15121 | 4-nitrophenol + hexanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl octanoate + H2O | low activity | Bacillus sp. SCSIO 15121 | 4-nitrophenol + octanoate | - |
? | |
| 3.1.1.1 | additional information | esterase BSE01701 can enzymatically resolve inexpensive racemic methyl lactate and generate chiral D-methyl lactate, BSE01701 is utilized to generate optically pure D-methyl lactate through enzymatic kinetic resolution reactions, optimum conditions are 35°C, pH 9.0, and 60 % n-heptane. Enzyme BSE01701 preferentially hydrolyzes 4-nitrophenyl esters with short-chain fatty acids and exhibits its highest activity toward 4-nitrophenyl butyrate. The hydrolysis activities of BSE01701 are much lower when the aliphatic acyl-chain of substrate is longer than C8. BSE01701 is an esterase | Bacillus sp. SCSIO 15121 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | ? | x * 28973, sequence calculation | Bacillus sp. SCSIO 15121 |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | Bacillus esterase | - |
Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | BSE01701 | - |
Bacillus sp. SCSIO 15121 |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 35 | - |
- |
Bacillus sp. SCSIO 15121 |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 20 | 50 | over 60% of maximal activity within this range | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | 30 | 45 | over 80% of maximal activity within this range | Bacillus sp. SCSIO 15121 |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 4 | - |
purified recombinant His-tagged enzyme, 12 h, loss of 40% activity | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | 25 | - |
purified recombinant His-tagged enzyme, 12 h, loss of 60% activity | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | 35 | - |
purified recombinant His-tagged enzyme, 12 h, loss of 70% activity | Bacillus sp. SCSIO 15121 |
| 3.1.1.1 | 45 | - |
purified recombinant His-tagged enzyme, 2 h, loss of over 95% activity, after 4 h inactivation | Bacillus sp. SCSIO 15121 |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 1044 | - |
4-nitrophenyl butyrate | pH 8.5, 35°C, recombinant enzyme | Bacillus sp. SCSIO 15121 | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 8.5 | - |
- |
Bacillus sp. SCSIO 15121 |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 7.5 | 9 | high activity within this range | Bacillus sp. SCSIO 15121 |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 7 | 8 | purified recombinant His-tagged enzyme, 35°C, over 60% activity retained after 12 h, a sharp decrease in hydrolysis activity is observed at over pH 9.0 | Bacillus sp. SCSIO 15121 |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.1.1.1 | Bacillus sp. SCSIO 15121 | sequence calculation | - |
5.62 |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 2088 | - |
4-nitrophenyl butyrate | pH 8.5, 35°C, recombinant enzyme | Bacillus sp. SCSIO 15121 | |
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