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Literature summary for 3.2.1.189 extracted from

  • Li, H.; Wang, X.; Ma, Y.; Yang, N.; Zhang, X.; Xu, Z.; Shi, J.
    Purification and characterization of a glycosidase with hydrolyzing multi-3-O-glycosides of spirostanol saponin activity from Gibberella intermedia (2016), J. Mol. Catal. B, 128, 46-51 .
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Fusarium proliferatum
Fe2+
-
Fusarium proliferatum
Fe3+
-
Fusarium proliferatum
Mn2+
-
Fusarium proliferatum

Metals/Ions

Metals/Ions Comment Organism Structure
K+ slightly activating Fusarium proliferatum
Mg2+ slightly activating Fusarium proliferatum
additional information poor effects by Na+, Ca2+, Al3+, Ni2+, and Zn2+ Fusarium proliferatum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Fusarium proliferatum strain WX12 has ability to hydrolyze dioscin, trillin and polyphyllin VII into diosgenin as the final product. But it is inactive toward the terminal rhamnosyl, glucosyl and galactosyl of ginsenoside Re and saikosaponin A ?
-
?
additional information Fusarium proliferatum WX12 strain WX12 has ability to hydrolyze dioscin, trillin and polyphyllin VII into diosgenin as the final product. But it is inactive toward the terminal rhamnosyl, glucosyl and galactosyl of ginsenoside Re and saikosaponin A ?
-
?

Organism

Organism UniProt Comment Textmining
Fusarium proliferatum
-
-
-
Fusarium proliferatum WX12
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 8.51fold by ammonium sulfate fractionation, ultrafiltration, and anion exchange and hydrophobic interaction chromatography Fusarium proliferatum

Source Tissue

Source Tissue Comment Organism Textmining
additional information the optimum conditions are glucose 10 g/l, yeast 25 g/l, MgSO4 0.3 g/l, NaCl 1.16 g/l, KH2PO 42.72 g/l, pH 6.0, 30°C, resulting in 550 U/ml activity Fusarium proliferatum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
purified native enzyme shows 37.6 U/ml activity Fusarium proliferatum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-O-[alpha-L-Ara-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + H2O i.e. sinodiosgenin or trillin Fusarium proliferatum D-glucose + L-rhamnose + L-arabinose + diosgenin
-
?
3-O-[alpha-L-Ara-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + H2O i.e. sinodiosgenin or trillin Fusarium proliferatum WX12 D-glucose + L-rhamnose + L-arabinose + diosgenin
-
?
3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 3 H2O
-
Fusarium proliferatum D-glucose + 2 L-rhamnose + diosgenin
-
?
3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 3 H2O
-
Fusarium proliferatum WX12 D-glucose + 2 L-rhamnose + diosgenin
-
?
additional information strain WX12 has ability to hydrolyze dioscin, trillin and polyphyllin VII into diosgenin as the final product. But it is inactive toward the terminal rhamnosyl, glucosyl and galactosyl of ginsenoside Re and saikosaponin A Fusarium proliferatum ?
-
?
additional information enzyme GiGly shows high substrate specificity for multi-3-O-glycosides of spirostanol saponins such as dioscin, trillin and polyphyllin VII, and is inactive toward substrates with terminal groups of rhamnosyl, glucosyl, galactosyl of ginsenoside Re and saikosaponin A. It can only hydrolyze glycosidic bonds at the C-3 position on steroidal saponins, which have similar structure with dioscin, and can be transformed into diosgenin. Substrate specificity, overview. GiGly is able tohydrolyze the terminal alpha-1,2-linked rhamnosyl residues, alpha-1,4-linked rhamnosyl residues, alpha-1,4-linked arabinosyl residues and beta-D-glucosyl residues at C-3 position.. The hydrolyzed substrates of GiGly have a double bond between carbons 5 and 6 position. By contrast, the non-substrates lack the said double bond and have substituents at carbon 4 position Fusarium proliferatum ?
-
?
additional information strain WX12 has ability to hydrolyze dioscin, trillin and polyphyllin VII into diosgenin as the final product. But it is inactive toward the terminal rhamnosyl, glucosyl and galactosyl of ginsenoside Re and saikosaponin A Fusarium proliferatum WX12 ?
-
?
additional information enzyme GiGly shows high substrate specificity for multi-3-O-glycosides of spirostanol saponins such as dioscin, trillin and polyphyllin VII, and is inactive toward substrates with terminal groups of rhamnosyl, glucosyl, galactosyl of ginsenoside Re and saikosaponin A. It can only hydrolyze glycosidic bonds at the C-3 position on steroidal saponins, which have similar structure with dioscin, and can be transformed into diosgenin. Substrate specificity, overview. GiGly is able tohydrolyze the terminal alpha-1,2-linked rhamnosyl residues, alpha-1,4-linked rhamnosyl residues, alpha-1,4-linked arabinosyl residues and beta-D-glucosyl residues at C-3 position.. The hydrolyzed substrates of GiGly have a double bond between carbons 5 and 6 position. By contrast, the non-substrates lack the said double bond and have substituents at carbon 4 position Fusarium proliferatum WX12 ?
-
?
polyphyllin VII + 4 H2O
-
Fusarium proliferatum 3 L-rhamnose + D-glucose + (22zeta,25R)-9zeta-spirost-5-en-3beta,17-diol
-
?
polyphyllin VII + 4 H2O
-
Fusarium proliferatum WX12 3 L-rhamnose + D-glucose + (22zeta,25R)-9zeta-spirost-5-en-3beta,17-diol
-
?

Subunits

Subunits Comment Organism
monomer 1 * 45000, SDS-PAGE Fusarium proliferatum
More peptide mass fingerprinting, analysis through mass spectrometry and SDS-PAGE Fusarium proliferatum

Synonyms

Synonyms Comment Organism
GiGly
-
Fusarium proliferatum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Fusarium proliferatum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4
-
purified native enzyme GiGly conserved more than 70% of the original activity after 10 h of incubation at 4°C Fusarium proliferatum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Fusarium proliferatum

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 8 purified enzyme GiGly, stable at pH 5.0-8.0 retaining 80% activity at pH 7.0 after 12 h Fusarium proliferatum