Protein Variants | Comment | Organism |
---|---|---|
additional information | elimination of all of the glycosylation sites induces expression of the unfolded protein response target genes, and secretion of this CBH1 variant is severely compromised in a calnexin gene deletion strain. The thermal reactivity of CBH1 is significantly decreased by removal of either Asn45 or Asn384 glycosylation site during the catalyzed hydrolysis of soluble substrate. Combinatorial loss of these two N-linked glycans further exacerbates the temperature-dependent inactivation. Removal of N-glycosylation at Asn384 has a more pronounced effect on the integrity of regular secondary structure compared to the loss of Asn45 or Asn270 | Trichoderma reesei |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.352 | - |
4-nitrophenyl D-cellobioside | N-glycosylation mutant residue D270, pH 4.8, 45°C | Trichoderma reesei | |
0.363 | - |
4-nitrophenyl D-cellobioside | wild-type, pH 4.8, 45°C | Trichoderma reesei | |
0.369 | - |
4-nitrophenyl D-cellobioside | N-glycosylation mutant residue D45, pH 4.8, 45°C | Trichoderma reesei | |
0.426 | - |
4-nitrophenyl D-cellobioside | N-glycosylation mutant residue 384, pH 4.8, 45°C | Trichoderma reesei |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Trichoderma reesei | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trichoderma reesei | P62694 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | removal of one or two N-glycosylation sites hardly affects the extracellular secretion of CBH1. Elimination of all of the glycosylation sites induces expression of the unfolded protein response target genes, and secretion of this CBH1 variant is severely compromised in a calnexin gene deletion strain. The thermal reactivity of CBH1 is significantly decreased by removal of either Asn45 or Asn384 glycosylation site during the catalyzed hydrolysis of soluble substrate. Combinatorial loss of these two N-linked glycans further exacerbates the temperature-dependent inactivation. Removal of N-glycosylation at Asn384 has a more pronounced effect on the integrity of regular secondary structure compared to the loss of Asn45 or Asn270 | Trichoderma reesei |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl D-cellobioside + H2O | - |
Trichoderma reesei | 4-nitrophenol + cellobiose | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cellobiohydrolase I | - |
Trichoderma reesei |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
63.7 | - |
N-glycosylation mutant residue D384, melting temperature | Trichoderma reesei |
65.79 | - |
N-glycosylation mutant residue D45, melting temperature | Trichoderma reesei |
65.94 | - |
wild-type, melting temperature | Trichoderma reesei |
65.99 | - |
N-glycosylation mutant residue D270, melting temperature | Trichoderma reesei |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0178 | - |
4-nitrophenyl D-cellobioside | N-glycosylation mutant residue D45, pH 4.8, 45°C | Trichoderma reesei | |
0.018 | - |
4-nitrophenyl D-cellobioside | N-glycosylation mutant residue D270, pH 4.8, 45°C | Trichoderma reesei | |
0.019 | - |
4-nitrophenyl D-cellobioside | wild-type, pH 4.8, 45°C | Trichoderma reesei | |
0.02 | - |
4-nitrophenyl D-cellobioside | N-glycosylation mutant residue 384, pH 4.8, 45°C | Trichoderma reesei |