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Literature summary for 3.5.1.93 extracted from

  • Suzuki, H.; Yamada, C.; Kijima, K.; Ishihara, S.; Wada, K.; Fukuyama, K.; Kumagai, H.
    Enhancement of glutaryl-7-aminocephalosporanic acid acylase activity of gamma-glutamyltranspeptidase of Bacillus subtilis (2010), Biotechnol. J., 5, 829-837.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D445G kcat increased, turnover rate improved up to about 10fold compared to the glutaryl-7-aminocephalosporanic acid acylase activity of gamma-glutamyltranspeptidase Bacillus subtilis
E423Y/E442Q/D445N kcat/Km is increased, the catalytic efficiency improved up to 1000fold compared to the glutaryl-7-aminocephalosporanic acid acylase activity of gamma-glutamyltranspeptidase Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cephalosporin C + H2O
-
Bacillus subtilis 7-aminocephalosporanic acid + 2-amino-5-hydroxypentanoate
-
?

Synonyms

Synonyms Comment Organism
glutaryl-7-aminocephalosporanic acid acylase activity of gamma-glutamyltranspeptidase Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0485
-
7-aminocephalosporanic acid pH and temperature not specified in the publication Bacillus subtilis
0.508
-
7-aminocephalosporanic acid D445G mutant, pH and temperature not specified in the publication Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.41
-
7-aminocephalosporanic acid E423/E442Q/D445N mutant, pH and temperature not specified in the publication Bacillus subtilis