EC Number | Application | Comment | Organism |
---|---|---|---|
4.2.2.2 | environmental protection | biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process | Paenibacillus sp. |
4.2.2.2 | industry | biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process | Paenibacillus sp. |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.2.2 | gene pelN, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in recombinant Escherichia coli strain BL21(DE3) | Paenibacillus sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.2.2.2 | Ba2+ | causes a severe loss of activity, 88% inhibition at 0.5 mM, 97% at 1 mM | Paenibacillus sp. | |
4.2.2.2 | Ca2+ | inhibitory above 1 mM | Paenibacillus sp. | |
4.2.2.2 | Cu2+ | 20% inhibition at 0.5 mM | Paenibacillus sp. | |
4.2.2.2 | EDTA | complete inhibition at 0.5 mM | Paenibacillus sp. | |
4.2.2.2 | Fe2+ | 18% inhibition at 0.5 mM, 43% at 1 mM | Paenibacillus sp. | |
4.2.2.2 | Mn2+ | 25% inhibition at 0.5 mM, 43% at 1 mM | Paenibacillus sp. | |
4.2.2.2 | additional information | Triton X-100 and Tween-20 have a negligible influence on the activity at 0.5-1.0 mM | Paenibacillus sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.2.2.2 | Ca2+ | required, 7.3fold activation at 0.5 mM, 4.4fold at 1 mM, Ca2+-binding residues are D151, D173, and D177 in PelN | Paenibacillus sp. | |
4.2.2.2 | K+ | 19% activation at 0.5 mM | Paenibacillus sp. | |
4.2.2.2 | Mg2+ | 25% activation at 0.5 mM | Paenibacillus sp. | |
4.2.2.2 | Zn2+ | 16% activation at 0.5 mM | Paenibacillus sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.2.2 | pectin | Paenibacillus sp. | - |
? | - |
? | |
4.2.2.2 | polygalacturonic acid | Paenibacillus sp. | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.2.2 | Paenibacillus sp. | W8CR80 | gene pelN | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.2.2.2 | recombinant enzyme PelN 3fold from Escherichia coli strain BL21(DE3) | Paenibacillus sp. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.2.2.2 | 2060 | - |
purified recombinant enzyme, pH 9.8, 65°C | Paenibacillus sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.2.2 | additional information | PelN exhibits relatively high activity on methylated substrates. On pectin with relatively low degree (20-34%) of methylation, the remaining specific activity of PelN is approximately 100% of that on polygalacturonic acid. Highly methylated pectin (55-70%) results in slight inhibition of the PelN activity to 74% | Paenibacillus sp. | ? | - |
? | |
4.2.2.2 | pectin | - |
Paenibacillus sp. | ? | - |
? | |
4.2.2.2 | polygalacturonic acid | - |
Paenibacillus sp. | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.2.2.2 | 65 | - |
- |
Paenibacillus sp. |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.2.2.2 | 35 | 75 | activity range, recombinant enzyme, 14.8% of maximal activity at 35°C, 18% at 75°C | Paenibacillus sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.2.2.2 | 45 | 50 | purified recombinant PelN displays a half-life of around 9 h and 42 h at 50°C and 45°C, respectively | Paenibacillus sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.2.2.2 | 9.8 | - |
- |
Paenibacillus sp. |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
4.2.2.2 | 7.6 | 10.4 | activity range, recombinant enzyme | Paenibacillus sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.2.2 | evolution | the enzyme belongs to the polysaccharide lyase family 1 | Paenibacillus sp. |
4.2.2.2 | additional information | invariant amino acids involved in catalytic function mainly comprised the catalytic residues R275, K244, and R280, and the Ca2+-binding residues D151, D173, and D177 in PelN | Paenibacillus sp. |