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  • Lin, M.; Hiyama, A.; Kondo, K.; Nagata, T.; Katahira, M.
    Classification of fungal glucuronoyl esterases (FGEs) and characterization of two new FGEs from Ceriporiopsis subvermispora and Pleurotus eryngii (2018), Appl. Microbiol. Biotechnol., 102, 9635-9645 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.117 degradation fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization Gelatoporia subvermispora
3.1.1.117 degradation fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization Pleurotus eryngii
3.1.1.117 additional information fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization Gelatoporia subvermispora
3.1.1.117 additional information fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization Pleurotus eryngii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.117 expression in Pichia pastoris Gelatoporia subvermispora
3.1.1.117 expression in Pichia pastoris Pleurotus eryngii
3.1.1.117 gene csge, functional recombinant expression of His6-tagged full-length enzyme and catalytic domain (residues 25-352) of enzyme CsGE in Pichia pastoris strain X-33, the recombinant enzyme is secreted to the culture medium Gelatoporia subvermispora
3.1.1.117 gene pege, functional recombinant expression of His6-tagged His6-tagged full-length enzyme and catalytic domain (residues 108-429) of enzyme PeGE in Pichia pastoris strain X-33, recombinant enzyme is secreted to the culture medium Pleurotus eryngii

General Stability

EC Number General Stability Organism
3.1.1.117 enzyme PeGE exhibits high tolerance toward several denaturing agents Pleurotus eryngii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.117 CHAPS 1%, 30°C, 20 min, about 10% loss of activity Pleurotus eryngii
3.1.1.117 EDTA 10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM Gelatoporia subvermispora
3.1.1.117 EDTA 10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM Pleurotus eryngii
3.1.1.117 glycerol 46% inhibition at 5% glycerol; 5%, 30°C, 20 min, about 45% loss of activity Gelatoporia subvermispora
3.1.1.117 glycerol 46% inhibition at 5% glycerol; 5%, 30°C, 20 min, about 45% loss of activity Pleurotus eryngii
3.1.1.117 imidazole 5 mM, 30°C, 20 min, about 30% loss of activity Gelatoporia subvermispora
3.1.1.117 imidazole 5 mM, 30°C, 20 min, about 10% loss of activity Pleurotus eryngii
3.1.1.117 NaN3 5 mM, 30°C, 20 min, about 15% loss of activity Pleurotus eryngii
3.1.1.117 PMSF 5 mM, 30°C, 20 min, about 25% loss of activity Gelatoporia subvermispora
3.1.1.117 PMSF 5 mM, 30°C, 20 min, about 5% loss of activity Pleurotus eryngii
3.1.1.117 SDS 1%, 30°C, 20 min, complete loss of activity; almost complete inhibition at 1% Gelatoporia subvermispora
3.1.1.117 SDS 1%, 30°C, 20 min, about 95% loss of activity; almost complete inhibition at 1% Pleurotus eryngii
3.1.1.117 tris(2-carboxyethyl)phosphine 5 mM, 30°C, 20 min, about 35% loss of activity Gelatoporia subvermispora
3.1.1.117 tris(2-carboxyethyl)phosphine 5 mM, 30°C, 20 min, about 20% loss of activity Pleurotus eryngii
3.1.1.117 Tween 80 2%, 30°C, 20 min, about 10% loss of activity Pleurotus eryngii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.117 23.9
-
 benzyl glucuronic acid pH 6.2, 30°C Pleurotus eryngii
3.1.1.117 55.8
-
 benzyl glucuronic acid pH 6.2, 30°C Gelatoporia subvermispora

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.117 additional information divalent metal ions, such as Mg2+ and Ca2+, are not necessary for the enzyme to exert its activity Gelatoporia subvermispora
3.1.1.117 additional information divalent metal ions, such as Mg2+ and Ca2+, are not necessary for the enzyme to exert its activity Pleurotus eryngii

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.117 Gelatoporia subvermispora A0A386GY48
-
-
3.1.1.117 Pleurotus eryngii A0A386GY52
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.117 glycoprotein the enzyme contains a CBM domain at residues 23-50 Pleurotus eryngii

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.117
-
 Gelatoporia subvermispora
3.1.1.117
-
 Pleurotus eryngii
3.1.1.117 recombinant His6-tagged His6-tagged full-length enzyme and catalytic domain (residues 108-429) of enzyme PeGE from Pichia pastoris strain X-33 by ultrafiltration, nickel affinity chromatography, and again ultrafiltration Pleurotus eryngii
3.1.1.117 recombinant His6-tagged His6-tagged full-length enzyme and catalytic domain (residues 25-352) of enzyme CsGE from Pichia pastoris strain X-33 by ultrafiltration, nickel affinity chromatography, and again ultrafiltration Gelatoporia subvermispora

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.117 benzyl D-glucuronate + H2O
-
 Gelatoporia subvermispora benzyl alcohol + D-glucuronic acid
-
 ?
3.1.1.117 benzyl D-glucuronate + H2O
-
 Pleurotus eryngii benzyl alcohol + D-glucuronic acid
-
 ?
3.1.1.117 benzyl glucuronic acid + H2O
-
 Gelatoporia subvermispora benzyl alcohol + glucuronic acid
-
 ?
3.1.1.117 benzyl glucuronic acid + H2O
-
 Pleurotus eryngii benzyl alcohol + glucuronic acid
-
 ?
3.1.1.117 additional information UDH-coupled spectrophotometric assaying of GE enzymatic reaction, hydrolysis of BnGlcA catalyzed by GE and spectrophotometric assaying by NAD+-dependent oxidation of GlcA using uronate dehydrogenase (UDH), overview Gelatoporia subvermispora ?
-
-
3.1.1.117 additional information UDH-coupled spectrophotometric assaying of GE enzymatic reaction, hydrolysis of BnGlcA catalyzed by GE and spectrophotometric assaying by NAD+-dependent oxidation of GlcA using uronate dehydrogenase (UDH), overview Pleurotus eryngii ?
-
-

Subunits

EC Number Subunits Comment Organism
3.1.1.117 ? x * 46000, recombinant His-tagged enzyme, SDS-PAGE Gelatoporia subvermispora

Synonyms

EC Number Synonyms Comment Organism
3.1.1.117 CsGE
-
 Gelatoporia subvermispora
3.1.1.117 FGE
-
 Gelatoporia subvermispora
3.1.1.117 FGE
-
 Pleurotus eryngii
3.1.1.117 fungal glucuronoyl esterase
-
 Gelatoporia subvermispora
3.1.1.117 fungal glucuronoyl esterase
-
 Pleurotus eryngii
3.1.1.117 PeGE
-
 Pleurotus eryngii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.117 30
-
 assay at Gelatoporia subvermispora
3.1.1.117 30
-
 assay at Pleurotus eryngii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.117 23.6
-
 benzyl glucuronic acid pH 6.2, 30°C Gelatoporia subvermispora
3.1.1.117 104.6
-
 benzyl glucuronic acid pH 6.2, 30°C Pleurotus eryngii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.117 6.2
-
 assay at Gelatoporia subvermispora
3.1.1.117 6.2
-
 assay at Pleurotus eryngii

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.117 Gelatoporia subvermispora calculated
-
 4.48
3.1.1.117 Gelatoporia subvermispora sequence calculation
-
 4.48
3.1.1.117 Pleurotus eryngii sequence calculation, CBM domain
-
 5.08
3.1.1.117 Pleurotus eryngii calculated
-
 7.3
3.1.1.117 Pleurotus eryngii sequence calculation, full-length enzyme
-
 7.3
3.1.1.117 Pleurotus eryngii sequence calculation, catalytic domain (CE15 domain)
-
 8.38

General Information

EC Number General Information Comment Organism
3.1.1.117 evolution building of a phylogenetic tree from almost 400 putative FGEs obtained on BLAST analysis and definition of six main clades. In the phylogenetic tree, all the putative FGEs of ascomycetes cluster in clades I to IV, and most of the putative FGEs of basidiomycetes (B-FGEs) cluster in clades V to VI, several B-FGEs are found to cluster in clade II. Most FGEs of clade II have higher theoretical isoelectric points than those in the other five clades. The enzyme from Ceriporiopsis subvermispora belongs to clade V Gelatoporia subvermispora
3.1.1.117 evolution building of a phylogenetic tree from almost 400 putative FGEs obtained on BLAST analysis and definition of six main clades. In the phylogenetic tree, all the putative FGEs of ascomycetes cluster in clades I to IV, and most of the putative FGEs of basidiomycetes (B-FGEs) cluster in clades V to VI, several B-FGEs are found to cluster in clade II. Most FGEs of clade II have higher theoretical isoelectric points than those in the other five clades. The enzyme from Pleurotus eryngii belongs to clade II Pleurotus eryngii
3.1.1.117 physiological function fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes Gelatoporia subvermispora
3.1.1.117 physiological function fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes Pleurotus eryngii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.117 0.42
-
 benzyl glucuronic acid pH 6.2, 30°C Gelatoporia subvermispora
3.1.1.117 4.38
-
 benzyl glucuronic acid pH 6.2, 30°C Pleurotus eryngii