These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and characterization of cloned isopenicillin N synthetase.
    Author: Baldwin JE, Killin SJ, Pratt AJ, Sutherland JD, Turner NJ, Crabbe MJ, Abraham EP, Willis AC.
    Journal: J Antibiot (Tokyo); 1987 May; 40(5):652-9. PubMed ID: 3301770.
    Abstract:
    Isopenicillin N synthetase (IPS) cloned from Cephalosporium acremonium has been isolated from transformed Escherichia coli and purified to homogeneity. The resulting, abundant, recombinant protein, whilst undergoing slightly different N-terminal processing to that observed for the fungally-derived protein, has identical kinetics for the conversion of LLD-aminoadipoyl-cysteinyl-valine to isopenicillin N. Recombinant IPS converts analogue substrates into unusual beta-lactam antibiotics in exactly the same way as the fungal protein.
    [Abstract] [Full Text] [Related] [New Search]