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Literature summary extracted from

  • Tiwary, E.; Gupta, R.
    Improved catalytic efficiency of a monomeric gamma-glutamyl transpeptidase from Bacillus licheniformis in presence of subtilisin (2010), Biotechnol. Lett., 32, 1137-1141.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.2.2 Subtilisin subtilisin enhances transpeptidase activity of the 30000 Da and 67000 Da enzyme forms by nearly 1.5 and 2fold, respectively Bacillus licheniformis

Application

EC Number Application Comment Organism
3.4.21.62 biotechnology subtilisin-30 kDa gamma-glutamyl transpeptidase complex exhibits better catalytic properties and can be exploited in various biotechnological applications synthetic construct

General Stability

EC Number General Stability Organism
2.3.2.2 transpeptidase activity is salt-sensitive Bacillus licheniformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 0.22
-
 5-L-glutamyl-4-nitroanilide monomeric 30-kDa enzyme, at pH 11.0, in the presence of subtilisin, at 80°C Bacillus licheniformis
2.3.2.2 0.25
-
 5-L-glutamyl-4-nitroanilide heterodimeric 67-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60°C Bacillus licheniformis
2.3.2.2 5.2
-
 5-L-glutamyl-4-nitroanilide monomeric 30-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60°C Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 30000
-
 one of two active enzyme forms, gel filtration Bacillus licheniformis
2.3.2.2 67000
-
 one of two active enzyme forms, gel filtration Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Bacillus licheniformis
-
-
-
2.3.2.2 Bacillus licheniformis ER-15
-
-
-
3.4.21.62 synthetic construct
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 Q-Sepharose column chromatography and G-75 Sephadex gel filtration Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Bacillus licheniformis 5-L-glutamyl-glycylglycine + 4-nitroaniline
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Bacillus licheniformis ER-15 5-L-glutamyl-glycylglycine + 4-nitroaniline
-
 ?
3.4.21.62 67 kDa gamma-glutamyl transpeptidase + H2O proteolytic digestion of 67 kDa gamma-glutamyl transpeptidase from Bacillus licheniformis ER-15 by subtilisin to the 30 kDa form, which in turn remains associated with subtilisin as a heterodimeric protein synthetic construct 30 kDa gamma-glutamyl transpeptidase + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 monomer or heterodimer two active enzyme forms of 30000 Da and 67000 Da Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 gamma-glutamyl transpeptidase
-
 Bacillus licheniformis
2.3.2.2 GGT
-
 Bacillus licheniformis
3.4.21.62 subtilisin
-
 synthetic construct

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 60
-
 monomeric 30-kDa enzyme and heterodimeric 67000-Da enzyme, in the absence of subtilisin Bacillus licheniformis
2.3.2.2 70
-
 monomeric 30-kDa enzyme, in presence of subtilisin Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.2.2 60
-
 the monomeric 30-kDa enzyme has a half-life of 240 min and 120 min at 60°C in the absence and presence of subtilisin, respectively. The heterodimeric 67-kDa enzyme has a half-life of 20 min at 60°C in the absence of subtilisin Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 8
-
 monomeric 30-kDa enzyme and heterodimeric 67000-Da enzyme, in the absence of subtilisin Bacillus licheniformis
2.3.2.2 11
-
 monomeric 30-kDa enzyme, in presence of subtilisin Bacillus licheniformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 7 11
-
 Bacillus licheniformis

General Information

EC Number General Information Comment Organism
3.4.21.62 physiological function subtilisin enhances transpeptidase activity of 67 kDa gamma-glutamyl transpeptidase and 30 kDa gamma-glutamyl transpeptidase, by nearly 1.5- and 2fold, respectively. In presence of subtilisin, 30 kDa gamma-glutamyl transpeptidase has improved catalytic efficiency, altered pH and temperature optima and has salt-tolerant glutaminase activity synthetic construct