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Literature summary extracted from

  • Minami, H.; Suzuki, H.; Kumagai, H.
    Salt-tolerant gamma-glutamyltranspeptidase from Bacillus subtilis 168 with glutaminase activity (2003), Enzyme Microb. Technol., 32, 431-438.
No PubMed abstract available

Application

EC Number Application Comment Organism
2.3.2.2 nutrition the enzyme is suitable for food fermentation under high salt conditions, e.g. the fermentation of soy sauce and miso Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 GGT of Bacillus subtilis is synthesized only during the mid-stationary phase, which is inconvenient for industrial use, a strain overexpressing GGT for a sufficiently long period is generated to obtain large quantities of GGT. A plasmid vector, pHY300PLK, containing the ggt gene cloned from chromosomal DNA is introduced into a spo0A abrB double mutant strain, in which the level of GGT activity is high after the mid-stationary phase. The level of GGT activity in this strain increases steadily after the exponential phase, becoming 15fold higher than that in the parental strain Bacillus subtilis

General Stability

EC Number General Stability Organism
2.3.2.2 the enzyme is highly salt-tolerant, at pH 5.5 in presence of 18% NaCl, 49% of the transpeptidation activity and 86% of the hydrolysis activity remains, conversion of Gln to Glu shows 76% residual activity Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 6-diazo-5-oxo-L-norleucine
-
 Bacillus subtilis
2.3.2.2 L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
-
 Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.2 extracellular
-
 Bacillus subtilis
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 21000
-
 1 * 45000 + 1 * 21000, SDS-PAGE Bacillus subtilis
2.3.2.2 45000
-
 1 * 45000 + 1 * 21000, SDS-PAGE Bacillus subtilis
2.3.2.2 63000
-
 gel filtration Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Bacillus subtilis
-
 168
-
2.3.2.2 Bacillus subtilis 168
-
 168
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 recombinant Bacillus subtilis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.2 cell culture in wild-type the enzyme is synthesized only during the mid-stationary phase Bacillus subtilis
-

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 7.49
-
 hydrolysis Bacillus subtilis
2.3.2.2 100
-
 transpeptidation Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 5-L-glutamyl-4-nitroanilide + Gly 37.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-Gly
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + Gly 37.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 168 4-nitroaniline + 5-L-glutamyl-Gly
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + Gly-Gly
-
 Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + Gly-Gly
-
 Bacillus subtilis 168 4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + H2O
-
 Bacillus subtilis 4-nitroaniline + Glu
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + H2O
-
 Bacillus subtilis 168 4-nitroaniline + Glu
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Ala 9.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Ala
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Ala 9.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 168 4-nitroaniline + 5-L-glutamyl-L-Ala
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Arg 21.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Arg
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Asn 24.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Asn
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Asp 20.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Asp
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Cys 11.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Cys
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Gln 5.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Gln
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Glu 8.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Glu
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-His 35.7% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-His
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Ile 19.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Ile
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Leu 21.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Leu
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Lys 11.2% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Lys
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Met 50.6% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Met
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Phe 38.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Phe
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Pro 12.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Pro
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Ser 12.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Ser
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Thr 34% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Thr
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Trp 30.9% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Trp
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + L-Val 30.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-L-Val
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + taurine 68.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis 4-nitroaniline + 5-L-glutamyl-taurine
-
 ?
2.3.2.2 5-L-glutamyl-L-His + Gly-Gly 106% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis L-His + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-L-Met + Gly-Gly 114% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis L-Met + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-L-Phe + Gly-Gly 103% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis L-Phe + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-L-Trp + Gly-Gly 127% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis L-Trp + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-L-Tyr + Gly-Gly 94.7% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis L-Tyr + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 5-L-glutamyl-L-Val + Gly-Gly 113% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis L-Val + 5-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 Gln + H2O
-
 Bacillus subtilis Glu + NH3
-
 ?
2.3.2.2 Gln + H2O
-
 Bacillus subtilis 168 Glu + NH3
-
 ?
2.3.2.2 GSH + Gly-Gly 98.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis ?
-
 ?
2.3.2.2 L-Gln + Gly-Gly 78.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly Bacillus subtilis NH3 + 5-L-glutamyl-Gly-Gly
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 dimer 1 * 45000 + 1 * 21000, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 GGT
-
 Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.2.2 45
-
 pH 8.7, 15 min, stable up to Bacillus subtilis
2.3.2.2 50
-
 pH 8.7, 15 min, 44% inactivation Bacillus subtilis
2.3.2.2 60
-
 pH 8.7, 15 min, complete inactivation Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 8 8.5 glutaminase activity Bacillus subtilis
2.3.2.2 8.5 11 hydrolysis of 5-L-glutamyl-4-nitroanilide Bacillus subtilis
2.3.2.2 9 9.5 transpeptidation with 5-L-glutamyl-4-nitroanilide and glycylglycine Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 8 11 pH 8.0: about 60% of maximal activity, pH 11: about 75% of maximal activity, transpeptidation with 5-L-glutamyl-4-nitroanilide and glycylglycine Bacillus subtilis
2.3.2.2 8 11 pH 8.0: about 60% of maximal activity, pH 8.5-11: optimum, hydrolysis of 5-L-glutamyl-4-nitroanilide Bacillus subtilis