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Information on EC 3.5.1.93 - glutaryl-7-aminocephalosporanic-acid acylase

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IUBMB Comments
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
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UNIPROT: O86089
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cephalosporin acylase, gl-7-aca acylase, cephalosporin c acylase, glutaryl-7-aminocephalosporanic acid acylase, glutaryl acylase, cpc acylase, scpcacy, gl-7aca acylase, glutaryl-7-aca acylase, j1 acylase, more
SYSTEMATIC NAME
IUBMB Comments
(7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
CAS REGISTRY NUMBER
COMMENTARY hide
56645-46-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cephalosporin C + H2O
cephalosporanic acid + 2-amino-5-hydroxypentanoate
show the reaction diagram
low activity
-
-
?
glutaryl 7-aminodeacetoxycephalosporanic acid + H2O
7-aminodeacetoxycephalosporanic acid + glutarate
show the reaction diagram
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanate + glutarate
show the reaction diagram
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
low activity
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O86089_9PROT
720
0
79672
TrEMBL
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Eur. J. Biochem.
262
713-719
1999
Pseudomonas sp. 130 (O86089)
Manually annotated by BRENDA team