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Literature summary extracted from

  • Xu, Y.; Feng, X.; Jia, J.; Chen, X.; Jiang, T.; Rasool, A.; Lv, B.; Qu, L.; Li, C.
    A novel beta-glucuronidase from Talaromyces pinophilus Li-93 precisely hydrolyzes glycyrrhizin into glycyrrhetinic acid 3-O-mono-bea-D-glucuronide (2018), Appl. Environ. Microbiol., 84, e00755-18 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.B44 dithiothreitol 10 mM, about 1.1fold activation Talaromyces pinophilus
3.2.1.B44 EDTA 10 mM, about 1.1fold activation Talaromyces pinophilus
3.2.1.B44 glutathione 10 mM, about 1.2fold activation Talaromyces pinophilus

Application

EC Number Application Comment Organism
3.2.1.B44 synthesis the enzyme is potentially a powerful biocatalyst for environmentally friendly and cost-effective production of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide Talaromyces pinophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.B44 heterologous expression in Pichia pastoris Talaromyces pinophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.B44 C331A the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at less than 5% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 C331D the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 25% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 C331H the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 30% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 C331K the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 25% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 C331L the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 65% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 C331S the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 30% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 H365A the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 40% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 H365C the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 50% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 H365D the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 20% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 H365K the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 60% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 H365L the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 70% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 H365S the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 50% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y330A the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 5% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y330C the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 40% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y330D the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 45% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y330F the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 40% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y330N the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 55% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y330R the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 55% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y372A the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at less than 5% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y372C the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 60% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y372D the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 20% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y372K the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 20% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y372L the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 70% of the activity compared to the wild-type enzyme Talaromyces pinophilus
3.2.1.B44 Y372S the mutant enzyme catalyzes the hydrolysis of glycyrrhizin at about 55% of the activity compared to the wild-type enzyme Talaromyces pinophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.B44 Al3+ 10 mM, more than 90% loss of activity Talaromyces pinophilus
3.2.1.B44 Ca2+ 10 mM, about 35% loss of activity Talaromyces pinophilus
3.2.1.B44 Cu2+ 10 mM, more than 90% loss of activity Talaromyces pinophilus
3.2.1.B44 Fe2+ 10 mM, more than 90% loss of activity Talaromyces pinophilus
3.2.1.B44 Mn2+ 10 mM, about 40% loss of activity Talaromyces pinophilus
3.2.1.B44 Ni2+ 10 mM, about 35% loss of activity Talaromyces pinophilus
3.2.1.B44 SDS 5 mM, about 70% loss of activity Talaromyces pinophilus
3.2.1.B44 Triton X-100 5 mM, about 40% loss of activity Talaromyces pinophilus
3.2.1.B44 Zn2+ 10 mM, about 60% loss of activity Talaromyces pinophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.B44 0.54
-
 glycyrrhizin pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 0.76
-
 quercetin 3-O-beta-D-glucuronide pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 6.88
-
 Baicalin pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 25.56
-
 4-nitrophenyl beta-D-glucuronopyranoside pH 4.5, 45°C Talaromyces pinophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.B44 extracellular
-
 Talaromyces pinophilus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.B44 47200
-
 calculated from sequence Talaromyces pinophilus
3.2.1.B44 85000
-
 SDS-PAGE Talaromyces pinophilus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B44 Talaromyces pinophilus
-
-
-
3.2.1.B44 Talaromyces pinophilus Li-93
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.B44 glycoprotein highly N-glycosylated protein Talaromyces pinophilus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.B44
-
 Talaromyces pinophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.B44 11.97
-
 pH 4.5, 45°C Talaromyces pinophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.B44 4-nitrophenyl beta-D-glucuronopyranoside + H2O at 5.8% as compared to hydrolysis of glycyrrhizin Talaromyces pinophilus 4-nitrophenol + D-glucuronate
-
 ?
3.2.1.B44 4-nitrophenyl beta-D-glucuronopyranoside + H2O at 5.8% as compared to hydrolysis of glycyrrhizin Talaromyces pinophilus Li-93 4-nitrophenol + D-glucuronate
-
 ?
3.2.1.B44 baicalin + H2O at 13.2% as compared to hydrolysis of glycyrrhizin Talaromyces pinophilus 5,6,7-trihydroxyflavone + D-glucuronate
-
 ?
3.2.1.B44 baicalin + H2O at 13.2% as compared to hydrolysis of glycyrrhizin Talaromyces pinophilus Li-93 5,6,7-trihydroxyflavone + D-glucuronate
-
 ?
3.2.1.B44 glycyrrhizin + H2O the enzyme recognizes and hydrolyzed the distal glucuronic bond of glycyrrhizin but can not cleave the glucuronic bond in glycyrrhetinic acid 3-O-mono-beta-D-glucuronide Talaromyces pinophilus glycyrrhetinate 3-O-beta-D-glucuronide + D-glucuronate
-
 ?
3.2.1.B44 glycyrrhizin + H2O the enzyme recognizes and hydrolyzed the distal glucuronic bond of glycyrrhizin but can not cleave the glucuronic bond in glycyrrhetinic acid 3-O-mono-beta-D-glucuronide Talaromyces pinophilus Li-93 glycyrrhetinate 3-O-beta-D-glucuronide + D-glucuronate
-
 ?
3.2.1.B44 quercetin 3-O-beta-D-glucuronide + H2O at 51.2% as compared to hydrolysis of glycyrrhizin Talaromyces pinophilus quercetin + D-glucuronate
-
 ?
3.2.1.B44 quercetin 3-O-beta-D-glucuronide + H2O at 51.2% as compared to hydrolysis of glycyrrhizin Talaromyces pinophilus Li-93 quercetin + D-glucuronate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.B44 monomer 1 * 85000, SDS-PAGE, N-glycosylated protein Talaromyces pinophilus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.B44 glycyrrhizin glucuronohydrolase (glycyrrhetinic acid 3-O-mono-beta-D-glucuronide-forming)
-
 Talaromyces pinophilus
3.2.1.B44 TCE0_044r16781
-
 Talaromyces pinophilus
3.2.1.B44 TpGUS79A
-
 Talaromyces pinophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.B44 50
-
-
 Talaromyces pinophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.B44 35 60 35°C: about 50% of maximal activity, 60°C: about 40% of maximal activity Talaromyces pinophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.B44 40
-
 30 min, stable Talaromyces pinophilus
3.2.1.B44 60
-
 30 min, the enzyme loses most of its activity Talaromyces pinophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.B44 0.26
-
 4-nitrophenyl beta-D-glucuronopyranoside pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 2.9
-
 Baicalin pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 2.9
-
 quercetin 3-O-beta-D-glucuronide pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 6
-
 glycyrrhizin pH 4.5, 45°C Talaromyces pinophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.B44 4.5
-
-
 Talaromyces pinophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.B44 4 5.5 pH 4.0: about 30% of maximal activity, pH 5.5: about 30% of maximal activity Talaromyces pinophilus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.B44 2 7.5 the enzyme is stable in the pH range of 2.0 to 7.5 at 4°C for 12 h Talaromyces pinophilus

Expression

EC Number Organism Comment Expression
3.2.1.B44 Talaromyces pinophilus induced by glycyrrhizin up

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.B44 0.01
-
 4-nitrophenyl beta-D-glucuronopyranoside pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 0.29
-
 Baicalin pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 3.83
-
 quercetin 3-O-beta-D-glucuronide pH 4.5, 45°C Talaromyces pinophilus
3.2.1.B44 11.14
-
 glycyrrhizin pH 4.5, 45°C Talaromyces pinophilus