EC Number | Application | Comment | Organism |
---|---|---|---|
2.3.2.2 | synthesis | using recombinant Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) in a straightforward procedure for the biocatalytic synthesis of gamma-glutamyl-phenylalanine (gamma-Glu-Phe), qualitative analysis of reaction products, mass spectrometry/nuclear magnetic resonance analyses | Bacillus licheniformis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.2.2 | gene ggt, recombinant expression of His-tagged enzyme GGT in Escherichia coli strain M15 | Bacillus licheniformis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis | - |
a peptide + a 5-L-glutamyl amino acid | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.2 | Bacillus licheniformis | A0A415J2H1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.2.2 | recombinant His-tagged GGT from Escherichia coli strain M15 by nickel affinity chromatography | Bacillus licheniformis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-phenylalanine | the synthetic substrate L-gamma-Glu-4-nitroanilide is used as a gamma-glutamyl donor, biocatalytic synthesis of gamma-Glu-Phe, reaction via formation of a gamma-glutamyl-enzyme intermediate. The intermediate can then react with water to release glutamate in a hydrolysis reaction or with amino acids or peptides to produce other gamma-glutamyl compounds in a transpeptidation reaction. Product analysis by thin layer chromatography | Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-phenylalanine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.2.2 | BlGGT | - |
Bacillus licheniformis |
2.3.2.2 | gamma-glutamyltranspeptidase | - |
Bacillus licheniformis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 50 | - |
- |
Bacillus licheniformis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 59.5 | 70 | the melting temperature of enzyme BlGGT is around 59.5°C, the irreversible denaturation of this enzyme occurs at 70°C | Bacillus licheniformis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 9 | - |
optimal pH for gamma-Glu-Phe synthesis | Bacillus licheniformis |