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Literature summary for 2.3.2.2 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
Search for more literature for 2.3.2.2

Application

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

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzymes from Escherichia coli Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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