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Literature summary for 3.2.1.31 extracted from
- Cloning and expression of beta-glucuronidase from Lactobacillus brevis in E. coli and application in the bioconversion of baicalin and wogonoside (2009), J. Microbiol. Biotechnol., 19, 1650-1655.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| GUS, DNA and amino acid sequence determination, analysis and comparison, overexpression of the His-tagged enzyme in Escherichia coli strain GMS407 | Levilactobacillus brevis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 71000 | - |
x * 71000, recombinant enzyme, SDS-PAGE | Levilactobacillus brevis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Levilactobacillus brevis | - |
- |
- |
| Levilactobacillus brevis RO1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GUS from Escherichia coli strain GMS407 | Levilactobacillus brevis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1284 | - |
purified recombinant enzyme | Levilactobacillus brevis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl beta-D-glucuronide + H2O | - |
Levilactobacillus brevis | 4-nitrophenol + beta-D-glucuronate | - |
? |  |
| 4-nitrophenyl beta-D-glucuronide + H2O | - |
Levilactobacillus brevis RO1 | 4-nitrophenol + beta-D-glucuronate | - |
? | |
| baicalin + H2O | - |
Levilactobacillus brevis | baicalein + beta-D-glucuronate | - |
? | |
| baicalin + H2O | - |
Levilactobacillus brevis RO1 | baicalein + beta-D-glucuronate | - |
? | |
| wogonin 7-O-beta-D-glucuronide + H2O | - |
Levilactobacillus brevis | wogonin + beta-D-glucuronate | - |
? | |
| wogonin 7-O-beta-D-glucuronide + H2O | - |
Levilactobacillus brevis RO1 | wogonin + beta-D-glucuronate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 71000, recombinant enzyme, SDS-PAGE | Levilactobacillus brevis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GUS | - |
Levilactobacillus brevis |
| More | the enzyme belongs to glycosyl hydrolase family 2 with three conserved domains | Levilactobacillus brevis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
recombinant enzyme | Levilactobacillus brevis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
80 min, purified recombinant enzyme, pH 5.0-8.0, completely stable | Levilactobacillus brevis |
| 50 | - |
purified recombinant enzyme, half-life is over 2 h | Levilactobacillus brevis |
| 60 | - |
purified recombinant enzyme, half-life is 1 h | Levilactobacillus brevis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant enzyme | Levilactobacillus brevis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | 80 min, purified recombinant enzyme, 37°C, completely stable | Levilactobacillus brevis |
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