EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.2.2 | 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 |
2.3.2.2 | gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus licheniformis |
2.3.2.2 | gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus velezensis |
2.3.2.2 | gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
3.4.19.13 | 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 |
3.4.19.13 | gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus licheniformis |
3.4.19.13 | gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus velezensis |
3.4.19.13 | gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.3.2.2 | extracellular | - |
Bacillus licheniformis | - |
- |
2.3.2.2 | extracellular | - |
Bacillus subtilis | - |
- |
2.3.2.2 | extracellular | - |
Bacillus amyloliquefaciens | - |
- |
2.3.2.2 | extracellular | - |
Bacillus velezensis | - |
- |
3.4.19.13 | extracellular | - |
Bacillus licheniformis | - |
- |
3.4.19.13 | extracellular | - |
Bacillus subtilis | - |
- |
3.4.19.13 | extracellular | - |
Bacillus amyloliquefaciens | - |
- |
3.4.19.13 | extracellular | - |
Bacillus velezensis | - |
- |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 64509 | - |
sequence calculation | Bacillus amyloliquefaciens |
3.4.19.13 | 64509 | - |
sequence calculation | Bacillus amyloliquefaciens |
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 | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus subtilis | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus amyloliquefaciens | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus velezensis | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus subtilis 168 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis NCIMB 9375 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis Gibson 46 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis JCM 2505 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis NRRL NRS-1264 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus velezensis BGSC 10A6 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus velezensis DSM 23117 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus amyloliquefaciens SMB469 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis NBRC 12200 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis ATCC 14580 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus velezensis FZB42 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Bacillus licheniformis DSM 13 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.2 | Bacillus amyloliquefaciens | A0A1S5V3K5 | Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang | - |
2.3.2.2 | Bacillus amyloliquefaciens SMB469 | A0A1S5V3K5 | Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang | - |
2.3.2.2 | Bacillus licheniformis | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis ATCC 14580 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis DSM 13 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis Gibson 46 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis JCM 2505 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis NBRC 12200 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis NCIMB 9375 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus licheniformis NRRL NRS-1264 | Q65KZ6 | - |
- |
2.3.2.2 | Bacillus subtilis | P54422 | - |
- |
2.3.2.2 | Bacillus subtilis 168 | P54422 | - |
- |
2.3.2.2 | Bacillus velezensis | A7Z5E0 | - |
- |
2.3.2.2 | Bacillus velezensis BGSC 10A6 | A7Z5E0 | - |
- |
2.3.2.2 | Bacillus velezensis DSM 23117 | A7Z5E0 | - |
- |
2.3.2.2 | Bacillus velezensis FZB42 | A7Z5E0 | - |
- |
3.4.19.13 | Bacillus amyloliquefaciens | A0A1S5V3K5 | Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang | - |
3.4.19.13 | Bacillus amyloliquefaciens SMB469 | A0A1S5V3K5 | Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang | - |
3.4.19.13 | Bacillus licheniformis | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis ATCC 14580 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis DSM 13 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis Gibson 46 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis JCM 2505 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis NBRC 12200 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis NCIMB 9375 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus licheniformis NRRL NRS-1264 | Q65KZ6 | - |
- |
3.4.19.13 | Bacillus subtilis | P54422 | - |
- |
3.4.19.13 | Bacillus subtilis 168 | P54422 | - |
- |
3.4.19.13 | Bacillus velezensis | A7Z5E0 | - |
- |
3.4.19.13 | Bacillus velezensis BGSC 10A6 | A7Z5E0 | - |
- |
3.4.19.13 | Bacillus velezensis DSM 23117 | A7Z5E0 | - |
- |
3.4.19.13 | Bacillus velezensis FZB42 | A7Z5E0 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
2.3.2.2 | proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus licheniformis |
2.3.2.2 | proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus subtilis |
2.3.2.2 | proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus velezensis |
2.3.2.2 | 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 |
3.4.19.13 | proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus licheniformis |
3.4.19.13 | proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus subtilis |
3.4.19.13 | proteolytic modification | the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor | Bacillus velezensis |
3.4.19.13 | 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 |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.2.2 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus licheniformis |
2.3.2.2 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
2.3.2.2 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus amyloliquefaciens |
2.3.2.2 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus velezensis |
3.4.19.13 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus licheniformis |
3.4.19.13 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
3.4.19.13 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus amyloliquefaciens |
3.4.19.13 | recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus velezensis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 10.4 | - |
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C | Bacillus licheniformis |
2.3.2.2 | 12.9 | - |
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C | Bacillus subtilis |
2.3.2.2 | 16.1 | - |
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C | Bacillus velezensis |
2.3.2.2 | 17.8 | - |
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C | Bacillus amyloliquefaciens |
3.4.19.13 | 1.8 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus licheniformis |
3.4.19.13 | 5 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus subtilis |
3.4.19.13 | 6.3 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus velezensis |
3.4.19.13 | 6.7 | - |
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C | Bacillus amyloliquefaciens |
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 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus subtilis | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus amyloliquefaciens | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus velezensis | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus subtilis 168 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis NCIMB 9375 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis Gibson 46 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis JCM 2505 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis NRRL NRS-1264 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus velezensis BGSC 10A6 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus velezensis DSM 23117 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus amyloliquefaciens SMB469 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis NBRC 12200 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis ATCC 14580 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus velezensis FZB42 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Bacillus licheniformis DSM 13 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycine | very low activity | Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-glycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycine | very low activity | Bacillus amyloliquefaciens SMB469 | 4-nitroaniline + 5-L-glutamyl-glycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus velezensis | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus subtilis 168 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis NCIMB 9375 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis Gibson 46 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis JCM 2505 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis NRRL NRS-1264 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus velezensis BGSC 10A6 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus velezensis DSM 23117 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus amyloliquefaciens SMB469 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis NBRC 12200 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis ATCC 14580 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Bacillus velezensis FZB42 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | best substrate | Bacillus licheniformis DSM 13 | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus subtilis 168 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis NCIMB 9375 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis Gibson 46 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis JCM 2505 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis NRRL NRS-1264 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus amyloliquefaciens SMB469 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis NBRC 12200 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis ATCC 14580 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-arginine | - |
Bacillus licheniformis DSM 13 | 4-nitroaniline + 5-L-glutamyl-L-arginine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus subtilis 168 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis NCIMB 9375 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis Gibson 46 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis JCM 2505 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis NRRL NRS-1264 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis NBRC 12200 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis ATCC 14580 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-asparagine | - |
Bacillus licheniformis DSM 13 | 4-nitroaniline + 5-L-glutamyl-L-asparagine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-histidine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-histidine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-histidine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-histidine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-histidine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-histidine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-isoleucine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-isoleucine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-isoleucine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-isoleucine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-isoleucine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-isoleucine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-leucine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-leucine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-leucine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-leucine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-leucine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-leucine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-lysine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-lysine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-lysine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-lysine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-lysine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-lysine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-methionine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-methionine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-methionine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-methionine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-methionine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-methionine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-phenylalanine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-phenylalanine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-phenylalanine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-phenylalanine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-phenylalanine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-phenylalanine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-proline | very low activity | Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-proline | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-threonine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-threonine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-threonine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-threonine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-threonine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-threonine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-tryptophan | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-tryptophan | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-tryptophan | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-tryptophan | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-tryptophan | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-tryptophan | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-valine | - |
Bacillus licheniformis | 4-nitroaniline + 5-L-glutamyl-L-valine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-valine | - |
Bacillus subtilis | 4-nitroaniline + 5-L-glutamyl-L-valine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + L-valine | - |
Bacillus amyloliquefaciens | 4-nitroaniline + 5-L-glutamyl-L-valine | - |
? | |
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline and glycine | Bacillus subtilis | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline, poor activity with glycine | Bacillus amyloliquefaciens | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline and glycine | Bacillus subtilis 168 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis NCIMB 9375 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis Gibson 46 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis JCM 2505 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis NRRL NRS-1264 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline, poor activity with glycine | Bacillus amyloliquefaciens SMB469 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis NBRC 12200 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis ATCC 14580 | ? | - |
- |
|
2.3.2.2 | additional information | substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine | Bacillus licheniformis DSM 13 | ? | - |
- |
|
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus licheniformis | 4-nitroaniline + L-glutamate | - |
? | |
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus subtilis | 4-nitroaniline + L-glutamate | - |
? | |
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus amyloliquefaciens | 4-nitroaniline + L-glutamate | - |
? | |
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis | 4-nitroaniline + L-glutamate | - |
? | |
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis BGSC 10A6 | 4-nitroaniline + L-glutamate | - |
? | |
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis DSM 23117 | 4-nitroaniline + L-glutamate | - |
? | |
3.4.19.13 | L-gamma-glutamyl-4-nitroanilide + H2O | - |
Bacillus velezensis FZB42 | 4-nitroaniline + L-glutamate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.2.2 | heterodimer | - |
Bacillus licheniformis |
2.3.2.2 | heterodimer | - |
Bacillus subtilis |
2.3.2.2 | heterodimer | - |
Bacillus velezensis |
2.3.2.2 | heterodimer | 1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE | Bacillus amyloliquefaciens |
3.4.19.13 | heterodimer | - |
Bacillus licheniformis |
3.4.19.13 | heterodimer | - |
Bacillus subtilis |
3.4.19.13 | heterodimer | - |
Bacillus velezensis |
3.4.19.13 | heterodimer | 1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE | Bacillus amyloliquefaciens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.2.2 | BaGGT42 | - |
Bacillus velezensis |
2.3.2.2 | BaGGT469 | - |
Bacillus amyloliquefaciens |
2.3.2.2 | BlGGT13 | - |
Bacillus licheniformis |
2.3.2.2 | BsGGT168 | - |
Bacillus subtilis |
2.3.2.2 | gamma-glutamyltranspeptidase | - |
Bacillus licheniformis |
2.3.2.2 | gamma-glutamyltranspeptidase | - |
Bacillus subtilis |
2.3.2.2 | gamma-glutamyltranspeptidase | - |
Bacillus amyloliquefaciens |
2.3.2.2 | gamma-glutamyltranspeptidase | - |
Bacillus velezensis |
2.3.2.2 | GGT | - |
Bacillus licheniformis |
2.3.2.2 | GGT | - |
Bacillus subtilis |
2.3.2.2 | GGT | - |
Bacillus amyloliquefaciens |
2.3.2.2 | GGT | - |
Bacillus velezensis |
2.3.2.2 | More | see also EC 3.4.19.13 | Bacillus licheniformis |
2.3.2.2 | More | see also EC 3.4.19.13 | Bacillus subtilis |
2.3.2.2 | More | see also EC 3.4.19.13 | Bacillus amyloliquefaciens |
2.3.2.2 | More | see also EC 3.4.19.13 | Bacillus velezensis |
3.4.19.13 | BaGGT42 | - |
Bacillus velezensis |
3.4.19.13 | BaGGT469 | - |
Bacillus amyloliquefaciens |
3.4.19.13 | BlGGT13 | - |
Bacillus licheniformis |
3.4.19.13 | BsGGT168 | - |
Bacillus subtilis |
3.4.19.13 | More | see also EC 2.3.2.2 | Bacillus licheniformis |
3.4.19.13 | More | see also EC 2.3.2.2 | Bacillus subtilis |
3.4.19.13 | More | see also EC 2.3.2.2 | Bacillus amyloliquefaciens |
3.4.19.13 | More | see also EC 2.3.2.2 | Bacillus velezensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 40 | - |
- |
Bacillus licheniformis |
2.3.2.2 | 40 | - |
assay at | Bacillus velezensis |
2.3.2.2 | 45 | - |
- |
Bacillus subtilis |
2.3.2.2 | 60 | - |
- |
Bacillus amyloliquefaciens |
3.4.19.13 | 40 | - |
assay at | Bacillus licheniformis |
3.4.19.13 | 40 | - |
assay at | Bacillus subtilis |
3.4.19.13 | 40 | - |
assay at | Bacillus amyloliquefaciens |
3.4.19.13 | 40 | - |
assay at | Bacillus velezensis |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 30 | 70 | activity range, 8.9% of maximal activity at 70°C, profile overview | Bacillus amyloliquefaciens |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 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 |
3.4.19.13 | 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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 6 | 8 | - |
Bacillus licheniformis |
2.3.2.2 | 9 | - |
assay at | Bacillus velezensis |
2.3.2.2 | 9 | 9.5 | - |
Bacillus subtilis |
2.3.2.2 | 10 | - |
- |
Bacillus amyloliquefaciens |
3.4.19.13 | 9 | - |
assay at | Bacillus licheniformis |
3.4.19.13 | 9 | - |
assay at | Bacillus subtilis |
3.4.19.13 | 9 | - |
assay at | Bacillus amyloliquefaciens |
3.4.19.13 | 9 | - |
assay at | Bacillus velezensis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.3.2.2 | 4 | 10 | BaGGT469 shows the highest activity towards L-gamma-glutamyl-4-nitroanilide with diglycine acceptor in 50 mM borate-NaOH buffer at pH 10.0. The enzymatic activity at the alkaline pH range of pH 8.0-9.0 is 92.6-95.9% relative to that at optimum pH. BaGGT469 is much less active in the acidic pH range from pH 4.0-6.0 | Bacillus amyloliquefaciens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.2.2 | 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 |
2.3.2.2 | 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 |
2.3.2.2 | 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 |
2.3.2.2 | 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 |
2.3.2.2 | 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 |
2.3.2.2 | 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 |
3.4.19.13 | 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 |
3.4.19.13 | 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 |
3.4.19.13 | 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 |
3.4.19.13 | 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 |
3.4.19.13 | 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 |
3.4.19.13 | 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 |