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Literature summary for 2.3.2.2 extracted from
- Improving the catalytic properties and stability of immobilized gamma-glutamyltranspeptidase by post-immobilization with PharmalyteMT 8-10.5 (2017), Int. J. Biol. Macromol., 105, 1581-1586 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ggt, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-pET22b | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | immobilization of purified recombinant His-tagged enzyme on a mesoporous titania oxide whisker (MTWs) carrier further modified with PharmalyteMT (Phar) 8.0-10.5 to yield MTWs-GGT-Phar, method optimization and evaluation, overview. Modified MTWs-GGT-Phar exhibits a stable enzyme activity in the pH range of pH 6.0-11.0 and an optimum temperature 10°C higher than GGT. Its pH stability at pH 11.0 and thermalstability at 50°C are 23.7 times and 19.4 times higher, respectively, than those of free GGT. In addition, the affinity constant Km of MTWs-GGT-Phar towards GpNA is slightly lower than that of free GGT, indicating that Phar has a protective effect on the structure of GGT | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | thermodynamics and kinetic analysis of free and immobilized recombinant enzymes, overview | Bacillus subtilis | |
| 0.579 | - |
L-gamma-glutamyl-4-nitroanilide | recombinant immobilized modified wild-type enzyme MTWs-GGT-Phar, pH 8.0, 37°C | Bacillus subtilis |  |
| 0.597 | - |
L-gamma-glutamyl-4-nitroanilide | recombinant free wild-type enzyme GGT, pH 8.0, 37°C | Bacillus subtilis | |
| 0.879 | - |
L-gamma-glutamyl-4-nitroanilide | recombinant immobilized wild-type enzyme, MTWs-GGT, pH 8.0, 37°C | Bacillus subtilis | |
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 subtilis | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
| a (5-L-glutamyl)-peptide + an amino acid | Bacillus subtilis 168 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Bacillus subtilis 168 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-pET22b by nickel affinity chromatography and dialysis | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 43.1 | - |
purified recombinant His-tagged enzyme, pH 8.0, 37°C | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus subtilis | a peptide + a 5-L-glutamyl amino acid | - |
? | |
| a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus subtilis 168 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus subtilis 168 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | - |
Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| gamma-glutamyltranspeptidase | - |
Bacillus subtilis |
| GGT | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
recombinant wild-type free enzyme | Bacillus subtilis |
| 45 | - |
recombinant wild-type immobilized enzyme MTWs-GGT | Bacillus subtilis |
| 50 | - |
recombinant wild-type immobilized modified enzyme MTWs-GGT-Phar | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Bacillus subtilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 11 | 50% of maximal activity within this range, recombinant wild-type free enzyme, over 80% of maximal activity within this range, recombinant wild-type immobilized enzyme modified MTWs-GGT-Phar, the activity of recombinant immobilized enzyme MTWs-GGT is abolished above pH 10.0 | Bacillus subtilis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 11 | pH stabilities of free GGT, immobilized MTWs-GGT, and immobilized modified MTWs-GGT-Phar, overview | Bacillus subtilis |
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