EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.1.73 | purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit | Paecilomyces sp. 'thermophila' |
3.2.1.73 | purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit | Paecilomyces sp. (in: Eurotiomycetes) |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.73 | E113A | inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration | Paecilomyces sp. 'thermophila' |
3.2.1.73 | E113A | inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration | Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | W108A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | W108A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | W108F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | W108F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | W108Y | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | W108Y | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | W253A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | W253A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | W253F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | W253F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | W253Y | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. 'thermophila' |
3.2.1.73 | W253Y | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Paecilomyces sp. (in: Eurotiomycetes) |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.73 | additional information | Paecilomyces sp. 'thermophila' | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan | ? | - |
? | |
3.2.1.73 | additional information | Paecilomyces sp. (in: Eurotiomycetes) | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan | ? | - |
? | |
3.2.1.73 | additional information | Paecilomyces sp. (in: Eurotiomycetes) J18 | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.73 | Paecilomyces sp. 'thermophila' | - |
- |
- |
3.2.1.73 | Paecilomyces sp. (in: Eurotiomycetes) | E0XN39 | - |
- |
3.2.1.73 | Paecilomyces sp. (in: Eurotiomycetes) J18 | E0XN39 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.73 | beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose | the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview | Paecilomyces sp. 'thermophila' | |
3.2.1.73 | beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose | the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview | Paecilomyces sp. (in: Eurotiomycetes) |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.73 | barley beta-glucan + H2O | - |
Paecilomyces sp. 'thermophila' | ? | - |
? | |
3.2.1.73 | barley beta-glucan + H2O | - |
Paecilomyces sp. (in: Eurotiomycetes) | ? | - |
? | |
3.2.1.73 | barley beta-glucan + H2O | - |
Paecilomyces sp. (in: Eurotiomycetes) J18 | ? | - |
? | |
3.2.1.73 | lichenan + H2O | - |
Paecilomyces sp. 'thermophila' | ? | - |
? | |
3.2.1.73 | lichenan + H2O | - |
Paecilomyces sp. (in: Eurotiomycetes) | ? | - |
? | |
3.2.1.73 | lichenan + H2O | - |
Paecilomyces sp. (in: Eurotiomycetes) J18 | ? | - |
? | |
3.2.1.73 | additional information | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan | Paecilomyces sp. 'thermophila' | ? | - |
? | |
3.2.1.73 | additional information | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan | Paecilomyces sp. (in: Eurotiomycetes) | ? | - |
? | |
3.2.1.73 | additional information | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview | Paecilomyces sp. 'thermophila' | ? | - |
? | |
3.2.1.73 | additional information | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview | Paecilomyces sp. (in: Eurotiomycetes) | ? | - |
? | |
3.2.1.73 | additional information | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan | Paecilomyces sp. (in: Eurotiomycetes) J18 | ? | - |
? | |
3.2.1.73 | additional information | the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview | Paecilomyces sp. (in: Eurotiomycetes) J18 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.73 | monomer | - |
Paecilomyces sp. 'thermophila' |
3.2.1.73 | monomer | - |
Paecilomyces sp. (in: Eurotiomycetes) |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.73 | 1,3-1,4-beta-glucanase | - |
Paecilomyces sp. 'thermophila' |
3.2.1.73 | 1,3-1,4-beta-glucanase | - |
Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | Lichenase | - |
Paecilomyces sp. 'thermophila' |
3.2.1.73 | Lichenase | - |
Paecilomyces sp. (in: Eurotiomycetes) |
3.2.1.73 | PtLic16A | - |
Paecilomyces sp. 'thermophila' |
3.2.1.73 | PtLic16A | - |
Paecilomyces sp. (in: Eurotiomycetes) |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.73 | additional information | the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview | Paecilomyces sp. 'thermophila' |
3.2.1.73 | additional information | the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview | Paecilomyces sp. (in: Eurotiomycetes) |