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http://purl.uniprot.org/citations/11755403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11755403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11755403http://www.w3.org/2000/01/rdf-schema#comment"

Background

Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is obtained by environmentally toxic chemical deacylation of cephalosporin C (CPC). Thus, the enzymatic conversion of CPC to 7-ACA by cephalosporin acylase (CA) would be of great interest. However, CAs use glutaryl-7-ACA (GL-7-ACA) as a primary substrate and the enzyme has low turnover rates for CPC.

Results

The binary complex structures of CA with GL-7-ACA and glutarate (the side-chain of GL-7-ACA) show extensive interactions between the glutaryl moiety of GL-7-ACA and the seven residues that form the side-chain pocket. These interactions explain why the D-alpha-aminoadipyl side-chain of CPC yields a poorer substrate than GL-7-ACA.

Conclusions

This understanding of the nature of substrate specificity may be useful in the design of an enzyme with an improved performance for the conversion of CPC to 7-ACA. Additionally, the catalytic mechanism of the deacylation reaction was revealed by the ligand bound structures."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.org/dc/terms/identifier"doi:10.1016/s1074-5521(01)00092-8"xsd:string
http://purl.uniprot.org/citations/11755403http://purl.org/dc/terms/identifier"doi:10.1016/s1074-5521(01)00092-8"xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/author"Kim Y."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/author"Kim Y."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/author"Hol W.G.J."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/author"Hol W.G.J."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/pages"1253-1264"xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/pages"1253-1264"xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/title"Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/title"Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity."xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11755403http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11755403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11755403
http://purl.uniprot.org/citations/11755403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11755403
http://purl.uniprot.org/citations/11755403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11755403
http://purl.uniprot.org/citations/11755403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11755403
http://purl.uniprot.org/uniprot/Q9L5D6http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11755403
http://purl.uniprot.org/uniprot/#_Q9L5D6-citation-11755403http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11755403
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