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Literature summary for 3.2.1.193 extracted from
- An amino acid at position 512 in beta-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII (2015), Appl. Microbiol. Biotechnol., 99, 7987-7996 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of wild-type and mutant enzymes in Escherichia coli strain ER2566 | Clavibacter michiganensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | the hydrolytic pathways of enzyme mutants E83A, R131A, R199A, H238A, E332A, and L509A convert GypXVII to GypLXXV, showing the same regioselectivity as the wild-type enzyme. But mutant W512A converts GypXVII to GypLXXV and F2 (cf. EC 3.2.1.193), indicating that the variant simultaneously hydrolyzes the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position in GypXVII. Mutant W512F variant enzyme containing an aromatic side chain converts GypXVII as a substrate to GypLXXV, while mutant W512R containing a positively charged side chain converts GypXVII to F2 | Clavibacter michiganensis |
| W512A | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows slightly decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme. Mutant W512A converts GypXVII to GypLXXV and F2 (cf.. EC 3.2.1.193) | Clavibacter michiganensis |
| W512K | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
| W512R | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme. mutant W512R containing a positively charged side chain converts GypXVII to F2, cf. EC 3.2.1.193 | Clavibacter michiganensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clavibacter michiganensis | - |
- |
- |
| Clavibacter michiganensis DSM 46364 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| gypenoside XVII + H2O | GypXVI, enzyme mutants W512A and W512K hydrolyze the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position of GypXVII to produce GypLXXV (cf. EC 3.2.1.191) and F2. Mutant W512R hydrolyzes only the outer glucose linked to the C-20 position of GypXVII to produce F2. The wild-type enzyme hydrolyzes GypXVI only to gypenoside LXXV, GypLXXV | Clavibacter michiganensis | F2 + D-glucose | - |
? |  |
| gypenoside XVII + H2O | GypXVI, enzyme mutants W512A and W512K hydrolyze the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position of GypXVII to produce GypLXXV (cf. EC 3.2.1.191) and F2. Mutant W512R hydrolyzes only the outer glucose linked to the C-20 position of GypXVII to produce F2. The wild-type enzyme hydrolyzes GypXVI only to gypenoside LXXV, GypLXXV | Clavibacter michiganensis DSM 46364 | F2 + D-glucose | - |
? | |
| additional information | recombinant wild-type beta-glucosidase from Clavibacter michiganensis specifically hydrolyzes the outer and inner glucose linked to the C-3 position in protopanaxadiol (PPD)-type ginsenosides (EC 3.2.1.191) and the C-6 position in protopanaxatriol (PPT)-type ginsenosides (EC 3.2.1.194) except for the hydrolysis of gypenoside LXXV (GypLXXV). The enzyme converts gypenoside XVII (GypXVII) to GypLXXV by hydrolyzing the inner glucose linked to the C-3 position | Clavibacter michiganensis | ? | - |
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| additional information | recombinant wild-type beta-glucosidase from Clavibacter michiganensis specifically hydrolyzes the outer and inner glucose linked to the C-3 position in protopanaxadiol (PPD)-type ginsenosides (EC 3.2.1.191) and the C-6 position in protopanaxatriol (PPT)-type ginsenosides (EC 3.2.1.194) except for the hydrolysis of gypenoside LXXV (GypLXXV). The enzyme converts gypenoside XVII (GypXVII) to GypLXXV by hydrolyzing the inner glucose linked to the C-3 position | Clavibacter michiganensis DSM 46364 | ? | - |
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Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | cf. EC 3.2.1.191 and EC 3.2.1.194 | Clavibacter michiganensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
- |
Clavibacter michiganensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Clavibacter michiganensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the amino acid at position 512 in beta-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII, obtained from the GypXVII-docked homology models of beta-glucosidase. Homology modeling of Clavibacter michiganensis beta-glucosidase based on the crystal structure of beta-D-glucan exohydrolase from Hordeum vulgare (PDB ID 1EX1) as a template | Clavibacter michiganensis |
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