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Literature summary for 3.2.1.4 extracted from

  • Qi, F.; Zhang, W.; Zhang, F.; Chen, G.; Liu, W
    Deciphering the effect of the different N-glycosylation sites on the secretion, activity, and stability of cellobiohydrolase I from Trichoderma reesei (2014), Appl. Environ. Microbiol., 80, 3962-3971.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.4

Protein Variants

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 [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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Trichoderma reesei
-
-

Organism

Organism UniProt Comment Textmining
Trichoderma reesei P62694
-
-

Posttranslational Modification

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl D-cellobioside + H2O
-
 Trichoderma reesei 4-nitrophenol + cellobiose
-
 ?

Synonyms

Synonyms Comment Organism
cellobiohydrolase I
-
 Trichoderma reesei

Temperature Stability [°C]

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 [1/s]

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