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Literature summary extracted from

  • Topakas, E.; Moukouli, M.; Dimarogona, M.; Vafiadi, C.; Christakopoulos, P.
    Functional expression of a thermophilic glucuronyl esterase from Sporotrichum thermophile identification of the nucleophilic serine (2010), Appl. Microbiol. Biotechnol., 87, 1765-1772 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.117 expression in Pichia pastoris Thermothelomyces thermophilus
3.1.1.117 gene ge2, DNA and amino acid sequence determination and analysis, sequence comparisons, gene ge2 from the genomic DNA is successfully cloned in frame with the sequence for the Saccharomyces cerevisiae alpha-factor secretion signal under the transcriptional control of alcohol oxidase (AOX1) promoter and integrated in Pichia pastoris strain X-33 Thermothelomyces thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.117 S213A complete loss of activity Thermothelomyces thermophilus
3.1.1.117 S213A site-directed mutagenesis Thermothelomyces thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.117 PMSF 10 mM, 10 min, 60% loss of activity Thermothelomyces thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.117 extracellular
-
 Thermothelomyces thermophilus
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.117 Thermothelomyces thermophilus G2QJR6
-
-
3.1.1.117 Thermothelomyces thermophilus G2QJR6 Sporotrichum thermophile
-
3.1.1.117 Thermothelomyces thermophilus ATCC 42464 G2QJR6 Sporotrichum thermophile
-
3.1.1.117 Thermothelomyces thermophilus BCRC 31852 G2QJR6 Sporotrichum thermophile
-
3.1.1.117 Thermothelomyces thermophilus DSM 1799 G2QJR6
-
-
3.1.1.117 Thermothelomyces thermophilus DSM 1799 G2QJR6 Sporotrichum thermophile
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.117 recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, dialysis, immobilized metal-ion affinity chromatography, and again ultrafiltration and dialysis Thermothelomyces thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.117 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
-
 Thermothelomyces thermophilus methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
 ?
3.1.1.117 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
-
 Thermothelomyces thermophilus ATCC 42464 methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
 ?
3.1.1.117 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
-
 Thermothelomyces thermophilus BCRC 31852 methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
 ?
3.1.1.117 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
-
 Thermothelomyces thermophilus DSM 1799 methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
 ?
3.1.1.117 methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus ATCC 42464 methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus BCRC 31852 methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus DSM 1799 methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus methanol + 4-O-methyl-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus ATCC 42464 methanol + 4-O-methyl-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus BCRC 31852 methanol + 4-O-methyl-D-glucopyranuronate
-
 ?
3.1.1.117 methyl 4-O-methyl-D-glucopyranuronate + H2O
-
 Thermothelomyces thermophilus DSM 1799 methanol + 4-O-methyl-D-glucopyranuronate
-
 ?
3.1.1.117 additional information enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus ?
-
 ?
3.1.1.117 additional information the enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus ?
-
-
3.1.1.117 additional information enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus ATCC 42464 ?
-
 ?
3.1.1.117 additional information the enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus ATCC 42464 ?
-
-
3.1.1.117 additional information enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus BCRC 31852 ?
-
 ?
3.1.1.117 additional information the enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus BCRC 31852 ?
-
-
3.1.1.117 additional information enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus DSM 1799 ?
-
 ?
3.1.1.117 additional information the enzyme is active on substrates containing glucuronic acid methyl ester Thermothelomyces thermophilus DSM 1799 ?
-
-

Subunits

EC Number Subunits Comment Organism
3.1.1.117 ? x * 42881, calulated, x * 43000, recombinant protein with His-tag Thermothelomyces thermophilus
3.1.1.117 ? x * 43000, recombinant enzyme, SDS-PAGE, x * 40056, sequence calculation Thermothelomyces thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.117 4-O-methyl-glucuronoyl methylesterase UniProt Thermothelomyces thermophilus
3.1.1.117 Ge2
-
 Thermothelomyces thermophilus
3.1.1.117 glucuronoyl esterase
-
 Thermothelomyces thermophilus
3.1.1.117 glucuronoyl esterase 2
-
 Thermothelomyces thermophilus
3.1.1.117 StGE2
-
 Thermothelomyces thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.117 55
-
-
 Thermothelomyces thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.117 30 70 over 60% of maximal activity within this range, profile overview Thermothelomyces thermophilus
3.1.1.117 60 70 more than 70% of maximum activity Thermothelomyces thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.117 50
-
 stable up to Thermothelomyces thermophilus
3.1.1.117 50
-
 recombinant purified enzyme, pH 7.0, stable up to for 24 h Thermothelomyces thermophilus
3.1.1.117 55
-
 pH 7.0, 24 h, 53% loss of activity Thermothelomyces thermophilus
3.1.1.117 55 60 recombinant purified enzyme, pH 7.0, 55°C for 24 h, loss of 53% activity, inactivation above 60°C, half-lives are 22.5 h and 0.5 h at 55°C and 60°C, respectively Thermothelomyces thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.117 7
-
-
 Thermothelomyces thermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.117 5 8 over 70% of maximal activity within this range, profile overview Thermothelomyces thermophilus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.117 4 10
-
 Thermothelomyces thermophilus
3.1.1.117 4 10 recombinant purified esterase displays broad pH range stability between 4-10 Thermothelomyces thermophilus
3.1.1.117 7
-
 55°C, 24 h, 53% loss of activity Thermothelomyces thermophilus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.117 Thermothelomyces thermophilus sequence calculation
-
 5.76

General Information

EC Number General Information Comment Organism
3.1.1.117 evolution the enzyme belongs to the carbohydrate esterase family 15 (CE-15) Thermothelomyces thermophilus
3.1.1.117 additional information the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family, the candidate nucleophilic residue Ser213 is responsible for catalyzing the enzymatic reaction Thermothelomyces thermophilus
3.1.1.117 physiological function the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family Thermothelomyces thermophilus