EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.39 | gene TmLam, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Thermotoga maritima |
3.2.1.73 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Fibrobacter succinogenes |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.39 | additional information | engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of mutant hybrid glucanases | Thermotoga maritima |
3.2.1.73 | additional information | engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of parental TFsW203F and mutant hybrid glucanases | Fibrobacter succinogenes |
3.2.1.73 | W203F | site-directed mutagenesis, truncated and mutated 1,31,4-beta-D-glucanase, no activity with laminarin | Fibrobacter succinogenes |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.39 | additional information | - |
additional information | 8.3 mg/ml with lichenan and 1.3 mg/ml with laminarin, pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain, kinetic properties of mutant hybrid glucanases, overview | Thermotoga maritima | |
3.2.1.73 | additional information | - |
additional information | 5.3 mg/ml for mutant TFsW203F with lichenan, pH 6.0-7.0, 45°C. Kinetic properties of parental TFsW203F and mutant hybrid glucanases, overview | Fibrobacter succinogenes |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.39 | Thermotoga maritima | - |
gene TmLam | - |
3.2.1.39 | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | - |
gene TmLam | - |
3.2.1.73 | Fibrobacter succinogenes | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.39 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ncikel affiniyt chromatography | Thermotoga maritima |
3.2.1.73 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Fibrobacter succinogenes |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.73 | 626 | - |
substrate lichenan, pH 6.0-7.0, 45°C, mutant TFsW203F | Fibrobacter succinogenes |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.39 | laminarin + H2O | the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product | Thermotoga maritima | laminaritriose + ? | major product | ? | |
3.2.1.39 | laminarin + H2O | the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | laminaritriose + ? | major product | ? | |
3.2.1.39 | lichenan + H2O | - |
Thermotoga maritima | ? | - |
? | |
3.2.1.39 | lichenan + H2O | - |
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | ? | - |
? | |
3.2.1.73 | laminarin + H2O | - |
Fibrobacter succinogenes | ? | - |
? | |
3.2.1.73 | lichenan + H2O | - |
Fibrobacter succinogenes | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.39 | 1,3-beta-D-glucanase | - |
Thermotoga maritima |
3.2.1.39 | laminarinase | - |
Thermotoga maritima |
3.2.1.39 | TmLam | - |
Thermotoga maritima |
3.2.1.73 | 1,3-1,4-beta-D-glucanase | - |
Fibrobacter succinogenes |
3.2.1.73 | Lichenase | - |
Fibrobacter succinogenes |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.39 | 95 | - |
- |
Thermotoga maritima |
3.2.1.73 | 45 | - |
assay at | Fibrobacter succinogenes |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.39 | 30 | 90 | temperature effects on wild-type and mutant hybrid enzymes, overview | Thermotoga maritima |
3.2.1.73 | 30 | 90 | temperature effects on mutant W203F and on W203F mutant bifunctional hybrid enzymes, the latter is more resistant to heat treatment than the parental TFsW203F, overview | Fibrobacter succinogenes |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.39 | 38 | - |
lichenan | pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain | Thermotoga maritima | |
3.2.1.39 | 109 | - |
Laminarin | pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain | Thermotoga maritima | |
3.2.1.73 | 10100 | - |
lichenan | pH 6.0-7.0, 45°C, mutant TFsW203F | Fibrobacter succinogenes |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.39 | 6 | 8 | - |
Thermotoga maritima |
3.2.1.73 | 6 | 7 | assay at | Fibrobacter succinogenes |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.39 | evolution | the thermostable laminarinase is composed of a GH family 16 catalytic domain flanked by two family 4 carbohydrate-binding modules (CBM4-1 and CBM4-2) at each terminus | Thermotoga maritima |
3.2.1.39 | physiological function | fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It hydrolyzes internal beta-1,3-glycosidic linkages in beta-1,3-glucans, which form the main component of the cell wall in yeasts and filamentous fungi and the major structural and storage polysaccharide in marine macroalgae such as Laminaria saccharina | Thermotoga maritima |
3.2.1.73 | additional information | Glu56, Asp58 and Glu60 residues located in the active site cavity of the enzyme play key roles in enzyme catalysis, functioning as general acid-base residues, structure and functional relationships of Fsbeta-glucanase | Fibrobacter succinogenes |
3.2.1.73 | physiological function | fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It is responsible for precisely hydrolyzing beta-1,4-glycosidic bonds adjacent to the beta-1,3-linkages in lichenan or mixed-linked beta-D-glucans, yielding mainly cellotriose, cellotetraose and cellopentaose | Fibrobacter succinogenes |