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Literature summary for 3.2.1.73 extracted from
- A designed bifunctional laccase/beta-1,3-1,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse (2013), Protein Eng. Des. Sel., 26, 15-23.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bglS, expression of mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme in Escherichia coli | Bacillus subtilis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the crystal structure of the enzyme is used for structure modelling, PDB ID 3O5S | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.1 | - |
lichenan | pH 6.0, 50°C, mutant chimeric enzyme | Bacillus subtilis |  |
| 3.1 | - |
lichenan | pH 6.0, 50°C, wild-type enzyme | Bacillus subtilis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28000 | - |
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE | Bacillus subtilis |
| 96000 | - |
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lichenan + H2O | Bacillus subtilis | - |
? | - |
? | |
| lichenan + H2O | Bacillus subtilis 168 | - |
? | - |
? | |
| additional information | Bacillus subtilis | the enzyme hydrolyzes plant cell wall beta-glucans | ? | - |
? | |
| additional information | Bacillus subtilis 168 | the enzyme hydrolyzes plant cell wall beta-glucans | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P04957 | gene bglS | - |
| Bacillus subtilis 168 | P04957 | gene bglS | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lichenan + H2O | - |
Bacillus subtilis | ? | - |
? | |
| lichenan + H2O | - |
Bacillus subtilis 168 | ? | - |
? | |
| additional information | the enzyme hydrolyzes plant cell wall beta-glucans | Bacillus subtilis | ? | - |
? | |
| additional information | the enzyme hydrolyzes plant cell wall beta-glucans | Bacillus subtilis 168 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-1,3-1,4-glucanase | - |
Bacillus subtilis |
| BglS | - |
Bacillus subtilis |
| Lichenase | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan | Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1120 | - |
lichenan | pH 6.0, 50°C, mutant chimeric enzyme | Bacillus subtilis | |
| 1220 | - |
lichenan | pH 6.0, 50°C, wild-type enzyme | Bacillus subtilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan | Bacillus subtilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals | Bacillus subtilis |
| additional information | the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity | Bacillus subtilis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 394 | - |
lichenan | pH 6.0, 50°C, wild-type enzyme | Bacillus subtilis | |
| 534 | - |
lichenan | pH 6.0, 50°C, mutant chimeric enzyme | Bacillus subtilis | |
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