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Literature summary for 4.2.2.2 extracted from
- Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris (2008), Biochem. Eng. J., 40, 92-98.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinantly expressed in Pichia pastoris | Bacillus subtilis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ba2+ | decreases activity | Bacillus subtilis |  |
| Ca2+ | activity is not changed | Bacillus subtilis | |
| Co2+ | decreases activity | Bacillus subtilis | |
| Cu2+ | decreases activity | Bacillus subtilis | |
| Fe2+ | completely inactivates activity after incubation for 15 min | Bacillus subtilis | |
| Mg2+ | slightly increases activity | Bacillus subtilis | |
| Mn2+ | decreases activity | Bacillus subtilis | |
| Na+ | decreases activity | Bacillus subtilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 43640 | - |
deduced from cDNA | Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P39116 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using butyl-Toyopearl 650 column | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
pectate lyase activity as high as 100 U/ml is attained in the fermentation broth of Pichia pastoris GS 115, which is about 10 times higher than when the gene is expressed in Escherichia coli | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| polygalacturonic | analysis of polygalacturonic acid degradation products by electrospray ionization-mass spectrometry reveal that the degradation products are unsaturated trigalacturonic acid and unsaturated bigalacturonic acid, which confirms that the enzyme catalyzes a trans-elimination reaction | Bacillus subtilis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pectate lyase | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
- |
Bacillus subtilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
enzyme is stable to incubation up to 55°C when incubated at various temperatures for 20 min in glycine-NaOH buffer (pH 9.4) | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.4 | - |
- |
Bacillus subtilis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | 11 | recombinant enzyme shows a wider pH and thermal stability spectrum than the purified pectate lyase from Bacillus subtilis WSHB04-02 | Bacillus subtilis |
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