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Literature summary extracted from

  • Li, K.; Chen, W.; Wang, W.; Tan, H.; Li, S.; Yin, H.
    Effective degradation of curdlan powder by a novel endo-beta-1->3-glucanase (2018), Carbohydr. Polym., 201, 122-130 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.39 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

EC Number Inhibitors Comment Organism Structure
3.2.1.39 Cu2+ 86% inhibition at 1 mM Cellulosimicrobium cellulans
3.2.1.39 Fe2+ 20% inhibition at 1 mM Cellulosimicrobium cellulans
3.2.1.39 Fe3+ 72% inhibition at 1 mM Cellulosimicrobium cellulans
3.2.1.39 additional information poor or no effects by 1 mM of DTT, urea, EDTA, Triton X-100, and Tween20 Cellulosimicrobium cellulans
3.2.1.39 Na+ 24% inhibition at 0.7 M Cellulosimicrobium cellulans
3.2.1.39 SDS 94.5% inhibition at 1 mM Cellulosimicrobium cellulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.39 additional information
-
 additional information Michaelis-Menten kinetics, Km for curdlan is 10 mg/ml Cellulosimicrobium cellulans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.39 Co2+ 9% activation at 1 mM Cellulosimicrobium cellulans
3.2.1.39 Mn2+ 20% activation at 1 mM Cellulosimicrobium cellulans
3.2.1.39 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.39 curdlan + H2O Cellulosimicrobium cellulans degradation glucobiose + glucotriose
-
 ?
3.2.1.39 curdlan + H2O Cellulosimicrobium cellulans E4-5 degradation glucobiose + glucotriose
-
 ?
3.2.1.39 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 ?
-
 ?
3.2.1.39 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

EC Number Organism UniProt Comment Textmining
3.2.1.39 Cellulosimicrobium cellulans G1ED17 i.e. Arthrobacter luteus
-
3.2.1.39 Cellulosimicrobium cellulans E4-5 G1ED17 i.e. Arthrobacter luteus
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.39 recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Cellulosimicrobium cellulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.39 barley beta-glucan + H2O 16.20% activity compared to curdlan Cellulosimicrobium cellulans ?
-
 ?
3.2.1.39 barley beta-glucan + H2O 16.20% activity compared to curdlan Cellulosimicrobium cellulans E4-5 ?
-
 ?
3.2.1.39 curdlan + H2O degradation Cellulosimicrobium cellulans glucobiose + glucotriose
-
 ?
3.2.1.39 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
-
 ?
3.2.1.39 curdlan + H2O degradation Cellulosimicrobium cellulans E4-5 glucobiose + glucotriose
-
 ?
3.2.1.39 laminarin + H2O beta-(1->3)-glucose, 44.47% activity compared to curdlan Cellulosimicrobium cellulans ?
-
 ?
3.2.1.39 laminarin + H2O beta-(1->3)-glucose, 44.47% activity compared to curdlan Cellulosimicrobium cellulans E4-5 ?
-
 ?
3.2.1.39 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 ?
-
 ?
3.2.1.39 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 ?
-
 ?
3.2.1.39 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 ?
-
 ?
3.2.1.39 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 ?
-
 ?
3.2.1.39 zymosan + H2O beta-(1->3)-glucose, substrate from Saccharomyces cerevisiae, 9.11% activity compared to curdlan Cellulosimicrobium cellulans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.39 ? x * 44344, sequence calculation, x * 44000, recombinant enzyme, SDS-PAGE Cellulosimicrobium cellulans
3.2.1.39 More structure comparisons Cellulosimicrobium cellulans

Synonyms

EC Number Synonyms Comment Organism
3.2.1.39 beta-1,3-glucanase
-
 Cellulosimicrobium cellulans
3.2.1.39 CcGluE
-
 Cellulosimicrobium cellulans
3.2.1.39 endo-beta-1->3-glucanase
-
 Cellulosimicrobium cellulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.39 50
-
-
 Cellulosimicrobium cellulans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.39
-
 80 over 60% of maximal activity within this range, profile overview Cellulosimicrobium cellulans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.39 20 60 purified recombinant enzyme, pH 4.6, 2 h, over 80% activity remaining Cellulosimicrobium cellulans
3.2.1.39 70 80 purified recombinant enzyme, pH 4.6, 2 h, about 65% activity remaining Cellulosimicrobium cellulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.39 4.6
-
-
 Cellulosimicrobium cellulans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.39 4 9.6 over 50% activity within this range, profile overview Cellulosimicrobium cellulans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.39 4.6 8.6 purified recombinant enzyme, 48 h, over 80% activity remaining Cellulosimicrobium cellulans

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.39 Cellulosimicrobium cellulans sequence calculation
-
 6.33

General Information

EC Number General Information Comment Organism
3.2.1.39 evolution the enzyme belongs to the glycoside hydrolase (GH)16 family of endo-beta-(1->3)-glucanases Cellulosimicrobium cellulans
3.2.1.39 additional information in-silico analysis of the mechanism of degradation by enzyme CcGluE, overview Cellulosimicrobium cellulans