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 | UniProt | Comment | Textmining |
---|---|---|---|
Brevundimonas diminuta | Q9L5D6 | - |
- |
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 (Comment) | Organism |
---|---|
- |
Brevundimonas diminuta |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glutaryl-7-aminocephalosporanic acid + H2O | - |
Brevundimonas diminuta | 7-aminocephalosporanate + glutarate | - |
? |