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Literature summary extracted from

  • Li, Y.; Chen, J.; Jiang, W.; Mao, X.; Zhao, G.; Wang, E.
    In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130 (1999), Eur. J. Biochem., 262, 713-719.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.93 additional information substitution of the first residue of the beta-subunit, Ser, results in a complete loss of enzyme activity, and substitution of the last residue of the spacer, Gly, leads to an inactive and unprocessed precursor Pseudomonas sp. 130

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.93 Pseudomonas sp. 130 O86089
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Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.93 proteolytic modification the gene encoding the enzyme is expressed as a precursor polypeptide consisting of a signal peptide followed by alpha- and beta-subunits, which are separated by a spacer peptide. Removing the signal peptide has little effect on precursor processing or enzyme activity. The precursor is supposed to be processed autocatalytically, probably intramolecularly Pseudomonas sp. 130

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.93 cephalosporin C + H2O low activity Pseudomonas sp. 130 cephalosporanic acid + 2-amino-5-hydroxypentanoate
-
 ?
3.5.1.93 glutaryl 7-aminodeacetoxycephalosporanic acid + H2O
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 Pseudomonas sp. 130 7-aminodeacetoxycephalosporanic acid + glutarate
-
 ?
3.5.1.93 glutaryl-7-aminocephalosporanic acid + H2O
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 Pseudomonas sp. 130 7-aminocephalosporanate + glutarate
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 ?
3.5.1.93 penicillin G + H2O low activity Pseudomonas sp. 130 (2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
 ?