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Literature summary extracted from

  • Minami, H.; Suzuki, H.; Kumagai, H.
    A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity (2003), FEMS Microbiol. Lett., 224, 169-173.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.2.2 nutrition mutant enzyme D445A is suitable for fermentation of soy sauce and miso Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 expression of mutant enzymes in Escherichia coli Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 D445A mutation abolishes transpeptidation activity, specific activity for hydrolysis is 40.2% of that of the wild-type enzyme, salt tolerant like the wild-type enzyme Bacillus subtilis
2.3.2.2 D445E transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity Bacillus subtilis
2.3.2.2 D445N transpeptidation activity is 42% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity Bacillus subtilis
2.3.2.2 D445Y transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity Bacillus subtilis
2.3.2.2 R113K transpeptidation activity is 72% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 10.4
-
 5-L-glutamyl-4-nitroanilide wild-type enzyme Bacillus subtilis
2.3.2.2 15.3
-
 5-L-glutamyl-4-nitroanilide mutant enzyme D445A Bacillus subtilis

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 mutant enzymes from Escherichia coli 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 + glycylglycine in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity Bacillus subtilis 4-nitroaniline + 5-L-glutamylglycylglycine
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + H2O in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity Bacillus subtilis p-nitroaniline + Glu
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.2.2 43.33
-
 5-L-glutamyl-4-nitroanilide wild-type enzyme Bacillus subtilis
2.3.2.2 56.33
-
 5-L-glutamyl-4-nitroanilide mutant enzyme D445A Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 7.5 8 glutaminase activity of mutant enzyme D445A Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 7.5 10 pH 7.5: about 40% of maximal activity, pH 10.0: about 35% of maximal activity, glutaminase activity of mutant enzyme D445A Bacillus subtilis