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Literature summary for 2.3.2.2 extracted from
- Secretion of Bacillus amyloliquefaciens gamma-glutamyltranspeptidase from Bacillus subtilis and its application in enzymatic synthesis of L-theanine (2019), J. Agric. Food Chem., 67, 14129-14136 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the recombinant extracellular enzyme is used for enzymatic synthesis of L-theanine, which is performed at optimal conditions: 20 mM L-Gln, 100 mM ethylamine-HCl, 0.5 U/ml BaGGT, incubated at 40°C for 6 h, 200 rpm | Bacillus amyloliquefaciens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ggt, recombinant expression of His6-tagged enzyme in Bacillus subtilis strain 168 (pHT43-spAmyQ-ggtDELTAsp) under control of the Plac promoter, extracellular secretion, subcloning in Escherichia coli strain DH5alpha, method optimization. Dual-signal peptides promote more secretion than a single signal peptide | Bacillus amyloliquefaciens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.214 | - |
L-gamma-glutamyl-4-nitroanilide | recombinant extracellular enzyme, pH 9.0, 40°C | Bacillus amyloliquefaciens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a (5-L-glutamyl)-peptide + an amino acid | Bacillus amyloliquefaciens | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
| a (5-L-glutamyl)-peptide + an amino acid | Bacillus amyloliquefaciens BH072 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus amyloliquefaciens | - |
- |
- |
| Bacillus amyloliquefaciens BH072 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged eextracellular enzyme from Bacillus subtilis strain 168 by nickel affinity chromatography | Bacillus amyloliquefaciens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 55 | - |
purified recombinant extracellular enzyme, pH 9.0, 40°C, substrate L-gamma-glutamyl-4-nitroanilide | Bacillus amyloliquefaciens |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 40°C, purified recombinant extracellular enzyme, 72 h, 90% of initial activity remaining, and more than 50% of initial activity after being maintained at different pH values for 24 h | Bacillus amyloliquefaciens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus amyloliquefaciens | a peptide + a 5-L-glutamyl amino acid | - |
? | |
| a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus amyloliquefaciens BH072 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus amyloliquefaciens BH072 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
| L-glutamine + ethylamine | GGT transfers the gamma-glutamyl moiety from L-Gln to ethylamine to form the product gamma-glutamylethylamine (L-theanine), product identification by mass spectrometry, optimization of reaction conditions, overview | Bacillus amyloliquefaciens | NH3 + gamma-glutamylethylamine | - |
? | |
| L-glutamine + ethylamine | GGT transfers the gamma-glutamyl moiety from L-Gln to ethylamine to form the product gamma-glutamylethylamine (L-theanine), product identification by mass spectrometry, optimization of reaction conditions, overview | Bacillus amyloliquefaciens BH072 | NH3 + gamma-glutamylethylamine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 46000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE | Bacillus amyloliquefaciens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BaGGT | - |
Bacillus amyloliquefaciens |
| gamma-glutamyltranspeptidase | - |
Bacillus amyloliquefaciens |
| GGT | - |
Bacillus amyloliquefaciens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
recombinant enzyme | Bacillus amyloliquefaciens |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | 40/56/34/20/6% relative activity at 20/30/50/60/70°C, respectively, recombinant enzyme, profile overview | Bacillus amyloliquefaciens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 50 | there is hardly any activity loss of the purified recombinant enzyme after preincubation at 40 °C for 72 h, but the activity drops to 7.5% after preincubation for 8 h at 50°C | Bacillus amyloliquefaciens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
recombinant enzyme | Bacillus amyloliquefaciens |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 11 | 46/75/64% relative activity at pH 7.0/8.0/10.0, respectively, recombinant enzyme, profile overview | Bacillus amyloliquefaciens |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 11 | 25°C, 7 h, 80% activity or higher is retained at pH 7.0-10.0 and, in all cases, it is above 50% at pH 5.0-11.0 | Bacillus amyloliquefaciens |
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