Any feedback?
Literature summary for 3.4.19.13 extracted from
- Heterologous expression and enzymatic characterization of gamma-glutamyltranspeptidase from Bacillus amyloliquefaciens (2017), J. Microbiol., 55, 147-152 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene BaGGT469, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Bacillus subtilis strain KCTC 3135 and in Escherichia coli strain BL21(DE3) | Bacillus amyloliquefaciens |
| gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus licheniformis |
| gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus velezensis |
| gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Bacillus licheniformis | - |
- |
| extracellular | - |
Bacillus subtilis | - |
- |
| extracellular | - |
Bacillus amyloliquefaciens | - |
- |
| extracellular | - |
Bacillus velezensis | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 64509 | - |
sequence calculation | Bacillus amyloliquefaciens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus amyloliquefaciens | A0A1S5V3K5 | Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang | - |
| Bacillus amyloliquefaciens SMB469 | A0A1S5V3K5 | Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang | - |
| Bacillus licheniformis | Q65KZ6 | - |
- |
| Bacillus licheniformis ATCC 14580 | Q65KZ6 | - |
- |
| Bacillus licheniformis DSM 13 | Q65KZ6 | - |
- |
| Bacillus licheniformis Gibson 46 | Q65KZ6 | - |
- |
| Bacillus licheniformis JCM 2505 | Q65KZ6 | - |
- |
| Bacillus licheniformis NBRC 12200 | Q65KZ6 | - |
- |
| Bacillus licheniformis NCIMB 9375 | Q65KZ6 | - |
- |
| Bacillus licheniformis NRRL NRS-1264 | Q65KZ6 | - |
- |
| Bacillus subtilis | P54422 | - |
- |
| Bacillus subtilis 168 | P54422 | - |
- |
| Bacillus velezensis | A7Z5E0 | - |
- |
| Bacillus velezensis BGSC 10A6 | A7Z5E0 | - |
- |
| Bacillus velezensis DSM 23117 | A7Z5E0 | - |
- |
| Bacillus velezensis FZB42 | A7Z5E0 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus licheniformis |
| proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus subtilis |
| proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus velezensis |
| proteolytic modification | the two separate polypeptide chains of 45.7 and 19.7 kDa forming the GGT heterodimeric enzyme are generated via autocatalytic cleavage from a precursor | Bacillus amyloliquefaciens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus licheniformis |
| recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
| recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus amyloliquefaciens |
| recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus velezensis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.8 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus licheniformis |
| 5 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus subtilis |
| 6.3 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus velezensis |
| 6.7 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus amyloliquefaciens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus licheniformis | 4-nitroaniline + L-glutamate | - |
? |  |
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus subtilis | 4-nitroaniline + L-glutamate | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus amyloliquefaciens | 4-nitroaniline + L-glutamate | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis | 4-nitroaniline + L-glutamate | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis BGSC 10A6 | 4-nitroaniline + L-glutamate | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis DSM 23117 | 4-nitroaniline + L-glutamate | - |
? | |
| L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis FZB42 | 4-nitroaniline + L-glutamate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | - |
Bacillus licheniformis |
| heterodimer | - |
Bacillus subtilis |
| heterodimer | - |
Bacillus velezensis |
| heterodimer | 1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE | Bacillus amyloliquefaciens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BaGGT42 | - |
Bacillus velezensis |
| BaGGT469 | - |
Bacillus amyloliquefaciens |
| BlGGT13 | - |
Bacillus licheniformis |
| BsGGT168 | - |
Bacillus subtilis |
| More | see also EC 2.3.2.2 | Bacillus licheniformis |
| More | see also EC 2.3.2.2 | Bacillus subtilis |
| More | see also EC 2.3.2.2 | Bacillus amyloliquefaciens |
| More | see also EC 2.3.2.2 | Bacillus velezensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Bacillus licheniformis |
| 40 | - |
assay at | Bacillus subtilis |
| 40 | - |
assay at | Bacillus amyloliquefaciens |
| 40 | - |
assay at | Bacillus velezensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 60 | thermal stability of BaGGT469 is extremely low and its residual activity is completely lost within 10 min at 60°C. But BaGGT469 is quite stable in the presence of substrate at 40°C | Bacillus amyloliquefaciens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
assay at | Bacillus licheniformis |
| 9 | - |
assay at | Bacillus subtilis |
| 9 | - |
assay at | Bacillus amyloliquefaciens |
| 9 | - |
assay at | Bacillus velezensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala) | Bacillus amyloliquefaciens |
| evolution | the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala) | Bacillus velezensis |
| physiological function | gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors | Bacillus licheniformis |
| physiological function | gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors | Bacillus subtilis |
| physiological function | gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors | Bacillus amyloliquefaciens |
| physiological function | gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors | Bacillus velezensis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
