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Literature summary for 3.2.1.39 extracted from
- Effective degradation of curdlan powder by a novel endo-beta-1->3-glucanase (2018), Carbohydr. Polym., 201, 122-130 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene CcGluE, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Cellulosimicrobium cellulans |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | 86% inhibition at 1 mM | Cellulosimicrobium cellulans |  |
| Fe2+ | 20% inhibition at 1 mM | Cellulosimicrobium cellulans | |
| Fe3+ | 72% inhibition at 1 mM | Cellulosimicrobium cellulans | |
| additional information | poor or no effects by 1 mM of DTT, urea, EDTA, Triton X-100, and Tween20 | Cellulosimicrobium cellulans | |
| Na+ | 24% inhibition at 0.7 M | Cellulosimicrobium cellulans | |
| SDS | 94.5% inhibition at 1 mM | Cellulosimicrobium cellulans | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics, Km for curdlan is 10 mg/ml | Cellulosimicrobium cellulans |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | 9% activation at 1 mM | Cellulosimicrobium cellulans | |
| Mn2+ | 20% activation at 1 mM | Cellulosimicrobium cellulans | |
| additional information | no or poor effects by 1 mM of Ba2+, Zn2+, Ni2+, Ca2+, and Mg2+, no effect by 1-100 mM K+ | Cellulosimicrobium cellulans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| curdlan + H2O | Cellulosimicrobium cellulans | degradation | glucobiose + glucotriose | - |
? | |
| curdlan + H2O | Cellulosimicrobium cellulans E4-5 | degradation | glucobiose + glucotriose | - |
? | |
| additional information | Cellulosimicrobium cellulans | cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity | ? | - |
? | |
| additional information | Cellulosimicrobium cellulans E4-5 | cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cellulosimicrobium cellulans | G1ED17 | i.e. Arthrobacter luteus | - |
| Cellulosimicrobium cellulans E4-5 | G1ED17 | i.e. Arthrobacter luteus | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Cellulosimicrobium cellulans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| barley beta-glucan + H2O | 16.20% activity compared to curdlan | Cellulosimicrobium cellulans | ? | - |
? | |
| barley beta-glucan + H2O | 16.20% activity compared to curdlan | Cellulosimicrobium cellulans E4-5 | ? | - |
? | |
| curdlan + H2O | degradation | Cellulosimicrobium cellulans | glucobiose + glucotriose | - |
? | |
| curdlan + H2O | beta-(1->3)-(glucose), substrate from Agrobacterium sp., recombinant CcGluE hydrolyses curdlan powder effectively. The hydrolytic products of curdlan are glucan oligosaccharides with degrees of polymerisation of 2-13, and the main products are glucobiose and glucotriose, overview | Cellulosimicrobium cellulans | glucobiose + glucotriose | - |
? | |
| curdlan + H2O | degradation | Cellulosimicrobium cellulans E4-5 | glucobiose + glucotriose | - |
? | |
| laminarin + H2O | beta-(1->3)-glucose, 44.47% activity compared to curdlan | Cellulosimicrobium cellulans | ? | - |
? | |
| laminarin + H2O | beta-(1->3)-glucose, 44.47% activity compared to curdlan | Cellulosimicrobium cellulans E4-5 | ? | - |
? | |
| additional information | cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity | Cellulosimicrobium cellulans | ? | - |
? | |
| additional information | cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin | Cellulosimicrobium cellulans | ? | - |
? | |
| additional information | cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity | Cellulosimicrobium cellulans E4-5 | ? | - |
? | |
| additional information | cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin | Cellulosimicrobium cellulans E4-5 | ? | - |
? | |
| zymosan + H2O | beta-(1->3)-glucose, substrate from Saccharomyces cerevisiae, 9.11% activity compared to curdlan | Cellulosimicrobium cellulans | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 44344, sequence calculation, x * 44000, recombinant enzyme, SDS-PAGE | Cellulosimicrobium cellulans |
| More | structure comparisons | Cellulosimicrobium cellulans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-1,3-glucanase | - |
Cellulosimicrobium cellulans |
| CcGluE | - |
Cellulosimicrobium cellulans |
| endo-beta-1->3-glucanase | - |
Cellulosimicrobium cellulans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Cellulosimicrobium cellulans |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
- |
80 | over 60% of maximal activity within this range, profile overview | Cellulosimicrobium cellulans |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 60 | purified recombinant enzyme, pH 4.6, 2 h, over 80% activity remaining | Cellulosimicrobium cellulans |
| 70 | 80 | purified recombinant enzyme, pH 4.6, 2 h, about 65% activity remaining | Cellulosimicrobium cellulans |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.6 | - |
- |
Cellulosimicrobium cellulans |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9.6 | over 50% activity within this range, profile overview | Cellulosimicrobium cellulans |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4.6 | 8.6 | purified recombinant enzyme, 48 h, over 80% activity remaining | Cellulosimicrobium cellulans |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Cellulosimicrobium cellulans | sequence calculation | - |
6.33 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the glycoside hydrolase (GH)16 family of endo-beta-(1->3)-glucanases | Cellulosimicrobium cellulans |
| additional information | in-silico analysis of the mechanism of degradation by enzyme CcGluE, overview | Cellulosimicrobium cellulans |
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Release 2023.1 (January 2023)
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