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Literature summary for 3.5.1.93 extracted from

  • Kim, S.; Kim, Y.
    Active site residues of cephalosporin acylase are critical not only for enzymatic catalysis but also for post-translational modification (2001), J. Biol. Chem., 276, 48376-48381.
    View publication on PubMed
Search for more literature for 3.5.1.93

Protein Variants

Protein Variants Comment Organism
F177H beta-subunit mutant, 17.6% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
F177P beta-subunit mutant, only partial intramolecular cleavage and no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid Brevundimonas diminuta
F177T beta-subunit mutant, 4.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate. Only partial intermolecular cleavage in posttranslational modification Brevundimonas diminuta
Q50L beta-subunit mutant, 9.9% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Q50M beta-subunit mutant, 7.5% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Q50R beta-subunit mutant, 2.1% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Q50T beta-subunit mutant, 72.5% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Q50Y beta-subunit mutant, 15.7% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
R57C beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid Brevundimonas diminuta
R57I beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid Brevundimonas diminuta
R57K beta-subunit mutant, 0.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate, only partial intermolecular cleavage in posttranslational modification Brevundimonas diminuta
S1A beta-subunit mutant, no processing takes place, no activity with glutaryl-7-aminocephalosporanic acid Brevundimonas diminuta
S1C beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid Brevundimonas diminuta
Y149C alpha-subunit mutant, 16.4% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y149G alpha-subunit mutant, 0.7% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y149L alpha-subunit mutant, 6.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y149N alpha-subunit mutant, 30.8% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y149P alpha-subunit mutant, 1.1% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y149R alpha-subunit mutant, 13.6% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y33F beta-subunit mutant, 65.4% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate Brevundimonas diminuta
Y33I beta-subunit mutant, 9.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate only partial intermolecular cleavage in posttranslational modification Brevundimonas diminuta
Y33S beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid Brevundimonas diminuta

Organism

Organism UniProt Comment Textmining
Brevundimonas diminuta Q9L5D6
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme is translated as an inactive single chain precursor, being post-translationally modified into an active enzyme. The post-translational modification takes place in two steps. The first intramolecular autocatalytic proteolysis takes place at one end of the spacer peptide by a nucleophilic Ser or Thr, which in turn becomes a new N-terminal Ser or Thr. The second intermolecular modification cleaves off the other end of the spacer peptide by another enzyme molecule Brevundimonas diminuta

Purification (Commentary)

Purification (Comment) Organism
-
 Brevundimonas diminuta

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutaryl-7-aminocephalosporanic acid + H2O
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 Brevundimonas diminuta 7-aminocephalosporanate + glutarate
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