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Literature summary extracted from

  • Zheng, F.; Vermaas, J.; Zheng, J.; Wang, Y.; Tu, T.; Wang, X.; Xie, X.; Yao, B.; Beckham, G.; Luo, H.
    Activity and thermostability of GH5 endoglucanase chimeras from mesophilic and thermophilic parents (2018), Appl. Environ. Microbiol., 85, e02079-18 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.4 sequence comparisons, design and production of a chimeric enzyme library, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115 Rasamsonia emersonii
3.2.1.4 sequence comparisons, design and production of a chimeric enzyme library, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115 Stegonsporium opalus
3.2.1.4 sequence comparisons, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115 Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.4 additional information creation of 10 hybrid enzymes of GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A) with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). Five of the expressed hybrid enzymes exhibit enzyme activity. Two of these hybrids exhibit pronounced increases in the temperature optimum (10 and 20°C), the temperature T50 at which the protein loses 50% of its activity (15 and 19°C), and the melting temperature Tm (16.5 and 22.9°C) and extended half-lives (240fold and 650fold at 55°C) relative to the values for the mesophilic parent enzyme. The mutants demonstrate improved catalytic efficiency on selected substrates. Method validation, molecular dynamics simulations of both the SoCel5 and TeEgl5A parent enzymes, overview. Improved hydrophobic packing of the interface between alpha2 and alpha3 is the primary mechanism by which the hybrid enzymes increase their thermostability relative to that of the mesophilic parent SoCel5. Comparison of structures and molecular masses of the SoCel5-TeEgl5A hybrid enzymes. Mechanism of improved thermostability Rasamsonia emersonii
3.2.1.4 additional information creation of 10 hybrid enzymes of GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A) with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). Five of the expressed hybrid enzymes exhibit enzyme activity. Two of these hybrids exhibit pronounced increases in the temperature optimum (10 and 20°C), the temperature T50 at which the protein loses 50% of its activity (15 and 19°C), and the melting temperature Tm (16.5 and 22.9°C) and extended half-lives (240fold and 650fold at 55°C) relative to the values for the mesophilic parent enzyme. The mutants demonstrate improved catalytic efficiency on selected substrates. Method validation, molecular dynamics simulations of both the SoCel5 and TeEgl5A parent enzymes, overview. Improved hydrophobic packing of the interface between alpha2 and alpha3 is the primary mechanism by which the hybrid enzymes increase their thermostability relative to that of the mesophilic parent SoCel5. Comparison of structures and molecular masses of the SoCel5-TeEgl5A hybrid enzymes. Mechanism of improved thermostability Stegonsporium opalus
3.2.1.4 additional information creation of a hybrid enzyme of GH5 endoglucanase AnCel5A from Aspergillus niger with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). The expressed hybrid enzyme exhibits increased enzyme activity relative to the values for the mesophilic parent enzyme. The mutant demonstrates improved catalytic efficiency on selected substrates. Method validation, overview Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.4 extracellular the N-terminal 19 amino acids are predicted to be a signal peptide Stegonsporium opalus
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Aspergillus niger O74706
-
-
3.2.1.4 Rasamsonia emersonii Q8WZD7
-
-
3.2.1.4 Stegonsporium opalus A0A1W6R2C1
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.4 glycoprotein three N-linked glycosylation sites (Asn23, Asn64, and Asn76) are possible, based on protein sequence and structure. Treatment with endo-beta-N-acetylglucosaminidase H (endo H) to remove glycosylation Stegonsporium opalus
3.2.1.4 glycoprotein treatment with endo-beta-N-acetylglucosaminidase H (endo H) to remove glycosylation Rasamsonia emersonii

Subunits

EC Number Subunits Comment Organism
3.2.1.4 ? x * 35000, about, sequence calculation Stegonsporium opalus
3.2.1.4 More the GH5 endoglucanase exhibits a (betaalpha)8 TIM barrel structure Rasamsonia emersonii
3.2.1.4 More the GH5 endoglucanase exhibits a (betaalpha)8 TIM barrel structure Stegonsporium opalus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 AnCel5A
-
 Aspergillus niger
3.2.1.4 Cel5
-
 Stegonsporium opalus
3.2.1.4 Cel5A
-
 Aspergillus niger
3.2.1.4 Egl5a
-
 Rasamsonia emersonii
3.2.1.4 eglB gene name, UniProt Aspergillus niger
3.2.1.4 GH5 endoglucanase
-
 Rasamsonia emersonii
3.2.1.4 GH5 endoglucanase
-
 Aspergillus niger
3.2.1.4 GH5 endoglucanase
-
 Stegonsporium opalus
3.2.1.4 mesophilic endoglucanase
-
 Stegonsporium opalus
3.2.1.4 SoCel5
-
 Stegonsporium opalus
3.2.1.4 TeEgl5A
-
 Rasamsonia emersonii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.4 additional information
-
 temperature optima of chimeric mutant enzymes, overview Rasamsonia emersonii
3.2.1.4 additional information
-
 temperature optima of chimeric mutant enzymes, overview Stegonsporium opalus
3.2.1.4 60
-
 recombinant wild-type enzyme Stegonsporium opalus
3.2.1.4 90
-
 recombinant wild-type enzyme Rasamsonia emersonii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.4 additional information
-
 mechanism of improved thermostability of hybrid mutant enzymes compared to parent wild-type enzymes Rasamsonia emersonii
3.2.1.4 additional information
-
 mechanism of improved thermostability of hybrid mutant enzymes compared to parent wild-type enzymes Stegonsporium opalus
3.2.1.4 53.6
-
 Tm of the recombinant deglycosylated wild-type enzyme Stegonsporium opalus
3.2.1.4 57
-
 T1/2 of the recombinant deglycosylated wild-type enzyme Stegonsporium opalus
3.2.1.4 70
-
 1 h, almost all activity remaining Rasamsonia emersonii
3.2.1.4 70
-
 10 min, less than 20% activity remaining Stegonsporium opalus
3.2.1.4 78.1
-
 Tm of the recombinant deglycosylated wild-type enzyme Rasamsonia emersonii
3.2.1.4 87
-
 T1/2 of the recombinant deglycosylated wild-type enzyme Rasamsonia emersonii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.4 additional information
-
 pH optima of chimeric mutant enzymes, overview Rasamsonia emersonii
3.2.1.4 additional information
-
 pH optima of chimeric mutant enzymes, overview Stegonsporium opalus
3.2.1.4 4
-
 recombinant wild-type enzyme Rasamsonia emersonii
3.2.1.4 5
-
 recombinant wild-type enzyme Stegonsporium opalus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.4 Stegonsporium opalus sequence calculation
-
 4.94

General Information

EC Number General Information Comment Organism
3.2.1.4 evolution the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 family shares a canonical (betaalpha)8-barrel structure, where each (betaalpha) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications Rasamsonia emersonii
3.2.1.4 evolution the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 family shares a canonical (betaalpha)8-barrel structure, where each (betaalpha) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications Aspergillus niger
3.2.1.4 evolution the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 family shares a canonical (betaalpha)8-barrel structure, where each (betaalpha) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications Stegonsporium opalus
3.2.1.4 additional information relationship between structure and thermostability in fungal GH5 endoglucanases Aspergillus niger
3.2.1.4 additional information relationship between structure and thermostability in fungal GH5 endoglucanases, hydrogen bond propensities at 25°C across all simulations for residues within the alpha1-4 or beta1-4 modules, excluding hydrogen bonds involved in helical interactions, of wild-type parent and mutant enzymes, overview, barrel stabilization by hydrogen bond networks Rasamsonia emersonii
3.2.1.4 additional information relationship between structure and thermostability in fungal GH5 endoglucanases, hydrogen bond propensities at 25°C across all simulations for residues within the alpha1-4 or beta1-4 modules, excluding hydrogen bonds involved in helical interactions, of wild-type parent and mutant enzymes, overview, barrel stabilization by hydrogen bond networks Stegonsporium opalus