EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.191 | recombinant expression of wild-type and mutant enzymes in Escherichia coli strain ER2566 | Clavibacter michiganensis |
3.2.1.193 | recombinant expression of wild-type and mutant enzymes in Escherichia coli strain ER2566 | Clavibacter michiganensis |
3.2.1.194 | recombinant expression of wild-type and mutant enzymes in Escherichia coli strain ER2566 | Clavibacter michiganensis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.191 | E332A | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | E83A | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows increased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | H238A | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | L509A | 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 | Clavibacter michiganensis |
3.2.1.191 | 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 |
3.2.1.191 | R131A | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | R199A | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows increased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | W331A | site-directed mutagenesis, mutation of a potential catalytic residue, inactive mutant | Clavibacter michiganensis |
3.2.1.191 | 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 |
3.2.1.191 | W512D | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and no activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | W512E | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows decreased activity with ginsenoside Rb1 and no activity with gypenoside XVII compared to the wild-type enzyme | Clavibacter michiganensis |
3.2.1.191 | W512F | site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows slightly decreased activity with ginsenoside Rb1 and increased activity with gypenoside XVII compared to the wild-type enzyme. Mutant W512F variant enzyme containing an aromatic side chain converts GypXVII as a substrate to GypLXXV | Clavibacter michiganensis |
3.2.1.191 | 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 |
3.2.1.191 | 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 |
3.2.1.191 | Y288A | site-directed mutagenesis, mutation of a potential catalytic residue, inactive mutant | Clavibacter michiganensis |
3.2.1.193 | 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 |
3.2.1.193 | 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 |
3.2.1.193 | 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 |
3.2.1.193 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.191 | 0.18 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant wild-type enzyme | Clavibacter michiganensis | |
3.2.1.191 | 0.2 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512A | Clavibacter michiganensis | |
3.2.1.191 | 0.21 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512R | Clavibacter michiganensis | |
3.2.1.191 | 0.32 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant mutant W512R | Clavibacter michiganensis | |
3.2.1.191 | 0.43 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant mutant W512A | Clavibacter michiganensis | |
3.2.1.191 | 0.46 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512E | Clavibacter michiganensis | |
3.2.1.191 | 0.62 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant wild-type enzyme | Clavibacter michiganensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.191 | ginsenoside C-Mc1 + H2O | Clavibacter michiganensis | - |
ginsenoside C-Mc + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside C-O + H2O | Clavibacter michiganensis | - |
ginsenoside C-Y + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside F2 + H2O | Clavibacter michiganensis | - |
ginsenoside C-K + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rb1 + H2O | Clavibacter michiganensis | - |
gypenoside XVII + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rb1 + H2O | Clavibacter michiganensis | - |
gypenoside XVII + ? | - |
? | |
3.2.1.191 | ginsenoside Rb2 + H2O | Clavibacter michiganensis | - |
ginsenoside C-O + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rc + H2O | Clavibacter michiganensis | - |
ginsenoside C-Mc1 + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rd + H2O | Clavibacter michiganensis | - |
ginsenoside F2 + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rg3 + H2O | Clavibacter michiganensis | - |
ginsenoside Rh2 + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rh2 + H2O | Clavibacter michiganensis | - |
protopanaxadiol aglycone + D-glucopyranose | - |
? | |
3.2.1.191 | gypenoside LXXV + H2O | Clavibacter michiganensis | - |
ginsenoside C-K + D-glucopyranose | - |
? | |
3.2.1.191 | gypenoside XVII + H2O | Clavibacter michiganensis | - |
gypenoside LXXV + D-glucose | - |
? | |
3.2.1.191 | additional information | Clavibacter michiganensis | the specific activity of beta-glucosidase from Clavibacter michiganensis for the PPD-type ginsenosides as substrates followed the order Rb2 > Rd > Rc > Rg3 > Rb1 > compound O (C-O) > compound Mc1 (C-Mc1) > GypXVII > F2 > Rh2 > gypenside LXXV (GypLXXV) and the products of which are C-O, F2, C-Mc1, Rh2, GypXVII, compound Y (C-Y), compound Mc (C-Mc), GypLXXV, compound K (C-K), APPD, and C-K, respectively. The specific activity of beta-glucosidase from Clavibacter michiganensis for the PPT-type ginsenosides as substrates follows the order Rf > Rh1 > Rg1 and the products of which are Rh1, APPT, and F1, respectively | ? | - |
? | |
3.2.1.194 | ginsenoside Rf + H2O | Clavibacter michiganensis | - |
ginsenoside Rh1 + D-glucose | - |
? | |
3.2.1.194 | ginsenoside Rf + H2O | Clavibacter michiganensis DSM 46364 | - |
ginsenoside Rh1 + D-glucose | - |
? | |
3.2.1.194 | ginsenoside Rg1 + H2O | Clavibacter michiganensis | - |
ginsenoside F1 + D-glucose | - |
? | |
3.2.1.194 | ginsenoside Rh1 + H2O | Clavibacter michiganensis | - |
protopanaxatriol aglycone + D-glucose | - |
? | |
3.2.1.194 | additional information | Clavibacter michiganensis | the specific activity of beta-glucosidase from Clavibacter michiganensis for the PPD-type ginsenosides as substrates followed the order Rb2 > Rd > Rc > Rg3 > Rb1 > compound O (C-O) > compound Mc1 (C-Mc1) > GypXVII > F2 > Rh2 > gypenside LXXV (GypLXXV) and the products of which are C-O, F2, C-Mc1, Rh2, GypXVII, compound Y (C-Y), compound Mc (C-Mc), GypLXXV, compound K (C-K), APPD, and C-K, respectively. The specific activity of beta-glucosidase from Clavibacter michiganensis for the PPT-type ginsenosides as substrates followed the order Rf > Rh1 > Rg1 and the products of which are Rh1, APPT, and F1, respectively | ? | - |
? | |
3.2.1.194 | additional information | Clavibacter michiganensis DSM 46364 | the specific activity of beta-glucosidase from Clavibacter michiganensis for the PPD-type ginsenosides as substrates followed the order Rb2 > Rd > Rc > Rg3 > Rb1 > compound O (C-O) > compound Mc1 (C-Mc1) > GypXVII > F2 > Rh2 > gypenside LXXV (GypLXXV) and the products of which are C-O, F2, C-Mc1, Rh2, GypXVII, compound Y (C-Y), compound Mc (C-Mc), GypLXXV, compound K (C-K), APPD, and C-K, respectively. The specific activity of beta-glucosidase from Clavibacter michiganensis for the PPT-type ginsenosides as substrates followed the order Rf > Rh1 > Rg1 and the products of which are Rh1, APPT, and F1, respectively | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.191 | Clavibacter michiganensis | - |
- |
- |
3.2.1.191 | Clavibacter michiganensis DSM 46364 | - |
- |
- |
3.2.1.193 | Clavibacter michiganensis | - |
- |
- |
3.2.1.193 | Clavibacter michiganensis DSM 46364 | - |
- |
- |
3.2.1.194 | Clavibacter michiganensis | - |
- |
- |
3.2.1.194 | Clavibacter michiganensis DSM 46364 | - |
- |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.191 | 0.0136 | - |
recombinant mutant W512K, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0196 | - |
recombinant mutant W512A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0204 | - |
recombinant mutant H238A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0273 | - |
recombinant mutant R131A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0326 | - |
recombinant mutant L509A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0333 | - |
recombinant mutant W512R, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0335 | - |
recombinant mutant R199A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0348 | - |
recombinant mutant E332A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0354 | - |
recombinant mutant E83A, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0421 | - |
recombinant wild-type enzyme, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 0.0647 | - |
recombinant mutant W512F, pH 7.5, 35°C, substrate gypenoside XVII | Clavibacter michiganensis |
3.2.1.191 | 1.173 | - |
recombinant mutant W512K, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 1.248 | - |
recombinant mutant W512D, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 1.474 | - |
recombinant mutant W512R, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 1.665 | - |
recombinant mutant H238A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 1.896 | - |
recombinant mutant R131A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 1.998 | - |
recombinant mutant E332A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2 | - |
recombinant mutant W512E, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2.109 | - |
recombinant mutant L509A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2.119 | - |
recombinant mutant W512F, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2.135 | - |
recombinant mutant W512A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2.189 | - |
recombinant wild-type enzyme, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2.22 | - |
recombinant mutant E83A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
3.2.1.191 | 2.301 | - |
recombinant mutant R199A, pH 7.5, 35°C, substrate ginsenoside Rb1 | Clavibacter michiganensis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.191 | ginsenoside C-Mc1 + H2O | - |
Clavibacter michiganensis | ginsenoside C-Mc + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside C-O + H2O | - |
Clavibacter michiganensis | ginsenoside C-Y + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside F2 + H2O | - |
Clavibacter michiganensis | ginsenoside C-K + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rb1 + H2O | - |
Clavibacter michiganensis | gypenoside XVII + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rb1 + H2O | - |
Clavibacter michiganensis | gypenoside XVII + ? | - |
? | |
3.2.1.191 | ginsenoside Rb2 + H2O | - |
Clavibacter michiganensis | ginsenoside C-O + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rc + H2O | - |
Clavibacter michiganensis | ginsenoside C-Mc1 + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rd + H2O | - |
Clavibacter michiganensis | ginsenoside F2 + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rg3 + H2O | - |
Clavibacter michiganensis | ginsenoside Rh2 + D-glucopyranose | - |
? | |
3.2.1.191 | ginsenoside Rh2 + H2O | - |
Clavibacter michiganensis | protopanaxadiol aglycone + D-glucopyranose | - |
? | |
3.2.1.191 | gypenoside LXXV + H2O | - |
Clavibacter michiganensis | ginsenoside C-K + D-glucopyranose | - |
? | |
3.2.1.191 | gypenoside LXXV + H2O | GypLXXV, low activity | Clavibacter michiganensis | ginsenoside C-K + D-glucopyranose | - |
? | |
3.2.1.191 | gypenoside XVII + H2O | - |
Clavibacter michiganensis | gypenoside LXXV + D-glucose | - |
? | |
3.2.1.191 | 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 and F2. W512R hydrolyzes only the outer glucose linked to the C-20 position of GypXVII to produce F2. Mutants W512E and W512D exhibit no activity for GypXVII | Clavibacter michiganensis | gypenoside LXXV + D-glucose | - |
? | |
3.2.1.191 | additional information | the specific activity of beta-glucosidase from Clavibacter michiganensis for the PPD-type ginsenosides as substrates followed the order Rb2 > Rd > Rc > Rg3 > Rb1 > compound O (C-O) > compound Mc1 (C-Mc1) > GypXVII > F2 > Rh2 > gypenside LXXV (GypLXXV) and the products of which are C-O, F2, C-Mc1, Rh2, GypXVII, compound Y (C-Y), compound Mc (C-Mc), GypLXXV, compound K (C-K), APPD, and C-K, respectively. The specific activity of beta-glucosidase from Clavibacter michiganensis for the PPT-type ginsenosides as substrates follows the order Rf > Rh1 > Rg1 and the products of which are Rh1, APPT, and F1, respectively | Clavibacter michiganensis | ? | - |
? | |
3.2.1.191 | additional information | recombinant 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 | ? | - |
? | |
3.2.1.193 | 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 | - |
? | |
3.2.1.193 | 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 | - |
? | |
3.2.1.193 | 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 | ? | - |
? | |
3.2.1.193 | 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 | ? | - |
? | |
3.2.1.194 | ginsenoside Rf + H2O | - |
Clavibacter michiganensis | ginsenoside Rh1 + D-glucose | - |
? | |
3.2.1.194 | ginsenoside Rf + H2O | - |
Clavibacter michiganensis DSM 46364 | ginsenoside Rh1 + D-glucose | - |
? | |
3.2.1.194 | ginsenoside Rg1 + H2O | - |
Clavibacter michiganensis | ginsenoside F1 + D-glucose | - |
? | |
3.2.1.194 | ginsenoside Rh1 + H2O | - |
Clavibacter michiganensis | protopanaxatriol aglycone + D-glucose | - |
? | |
3.2.1.194 | additional information | the specific activity of beta-glucosidase from Clavibacter michiganensis for the PPD-type ginsenosides as substrates followed the order Rb2 > Rd > Rc > Rg3 > Rb1 > compound O (C-O) > compound Mc1 (C-Mc1) > GypXVII > F2 > Rh2 > gypenside LXXV (GypLXXV) and the products of which are C-O, F2, C-Mc1, Rh2, GypXVII, compound Y (C-Y), compound Mc (C-Mc), GypLXXV, compound K (C-K), APPD, and C-K, respectively. The specific activity of beta-glucosidase from Clavibacter michiganensis for the PPT-type ginsenosides as substrates followed the order Rf > Rh1 > Rg1 and the products of which are Rh1, APPT, and F1, respectively | Clavibacter michiganensis | ? | - |
? | |
3.2.1.194 | additional information | recombinant 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 | ? | - |
? | |
3.2.1.194 | additional information | the specific activity of beta-glucosidase from Clavibacter michiganensis for the PPD-type ginsenosides as substrates followed the order Rb2 > Rd > Rc > Rg3 > Rb1 > compound O (C-O) > compound Mc1 (C-Mc1) > GypXVII > F2 > Rh2 > gypenside LXXV (GypLXXV) and the products of which are C-O, F2, C-Mc1, Rh2, GypXVII, compound Y (C-Y), compound Mc (C-Mc), GypLXXV, compound K (C-K), APPD, and C-K, respectively. The specific activity of beta-glucosidase from Clavibacter michiganensis for the PPT-type ginsenosides as substrates followed the order Rf > Rh1 > Rg1 and the products of which are Rh1, APPT, and F1, respectively | Clavibacter michiganensis DSM 46364 | ? | - |
? | |
3.2.1.194 | additional information | recombinant 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.191 | More | cf. EC 3.2.1.195, EC 3.2.1.193, and EC 3.2.1.194 | Clavibacter michiganensis |
3.2.1.193 | More | cf. EC 3.2.1.191 and EC 3.2.1.194 | Clavibacter michiganensis |
3.2.1.194 | More | cf. EC 3.2.1.191 | Clavibacter michiganensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.191 | 35 | - |
- |
Clavibacter michiganensis |
3.2.1.193 | 35 | - |
- |
Clavibacter michiganensis |
3.2.1.194 | 35 | - |
- |
Clavibacter michiganensis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.191 | 9 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant mutant W512A | Clavibacter michiganensis | |
3.2.1.191 | 9 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant mutant W512R | Clavibacter michiganensis | |
3.2.1.191 | 22 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant wild-type enzyme | Clavibacter michiganensis | |
3.2.1.191 | 343 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512R | Clavibacter michiganensis | |
3.2.1.191 | 795 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512A | Clavibacter michiganensis | |
3.2.1.191 | 1025 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant wild-type enzyme | Clavibacter michiganensis | |
3.2.1.191 | 1151 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512E | Clavibacter michiganensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.191 | 7.5 | - |
- |
Clavibacter michiganensis |
3.2.1.193 | 7.5 | - |
- |
Clavibacter michiganensis |
3.2.1.194 | 7.5 | - |
- |
Clavibacter michiganensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.191 | 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 |
3.2.1.193 | 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 |
3.2.1.194 | 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 |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.191 | 20.9 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant mutant W512A | Clavibacter michiganensis | |
3.2.1.191 | 28.125 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant mutant W512R | Clavibacter michiganensis | |
3.2.1.191 | 35.5 | - |
gypenoside XVII | pH 7.5, 35°C, recombinant wild-type enzyme | Clavibacter michiganensis | |
3.2.1.191 | 1633 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512R | Clavibacter michiganensis | |
3.2.1.191 | 2502 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512E | Clavibacter michiganensis | |
3.2.1.191 | 3975 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant mutant W512A | Clavibacter michiganensis | |
3.2.1.191 | 5694 | - |
ginsenoside Rb1 | pH 7.5, 35°C, recombinant wild-type enzyme | Clavibacter michiganensis |