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Literature summary for 3.1.1.117 extracted from

  • 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
Search for more literature for 3.1.1.117

Application

Application Comment Organism
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
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
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
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)

Cloned (Comment) Organism
expression in Pichia pastoris Gelatoporia subvermispora
expression in Pichia pastoris Pleurotus eryngii
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
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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Gelatoporia subvermispora A0A386GY48
-
-
Pleurotus eryngii A0A386GY52
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
-
 Gelatoporia subvermispora
-
 Pleurotus eryngii
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
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyl D-glucuronate + H2O
-
 Gelatoporia subvermispora benzyl alcohol + D-glucuronic acid
-
 ?
benzyl D-glucuronate + H2O
-
 Pleurotus eryngii benzyl alcohol + D-glucuronic acid
-
 ?
benzyl glucuronic acid + H2O
-
 Gelatoporia subvermispora benzyl alcohol + glucuronic acid
-
 ?
benzyl glucuronic acid + H2O
-
 Pleurotus eryngii benzyl alcohol + glucuronic acid
-
 ?
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 ?
-
-
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

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

pI Value

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

General Information

General Information Comment Organism
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
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
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
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]

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