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Literature summary extracted from

  • Lee, J.; Lee, J.; Nam, G.; Son, B.; Jang, M.; Lee, S.; Hurh, B.; Kim, T.
    Heterologous expression and enzymatic characterization of gamma-glutamyltranspeptidase from Bacillus amyloliquefaciens (2017), J. Microbiol., 55, 147-152 .
    View publication on PubMed

Cloned(Commentary)

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

Localization

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
-
-

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

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
-
-

Posttranslational Modification

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

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

General Information

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