Literature summary for 3.5.1.93 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.

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Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Pseudomonas sp. 130	O86089	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cephalosporin C + H2O	low activity	Pseudomonas sp. 130	cephalosporanic acid + 2-amino-5-hydroxypentanoate	-	?
glutaryl 7-aminodeacetoxycephalosporanic acid + H2O	-	Pseudomonas sp. 130	7-aminodeacetoxycephalosporanic acid + glutarate	-	?
glutaryl-7-aminocephalosporanic acid + H2O	-	Pseudomonas sp. 130	7-aminocephalosporanate + glutarate	-	?
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	-	?

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Release 2023.1 (January 2023)