Site-directed mutagenesis of arginine-89 supports the role of its guanidino side-chain in substrate binding by Cephalosporium acremonium isopenicillin N synthase.

doi:10.1111/j.1574-6968.1999.tb08758.x

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Article

Site-directed mutagenesis of arginine-89 supports the role of its guanidino side-chain in substrate binding by Cephalosporium acremonium isopenicillin N synthase.

FEMS microbiology letters - 15 Oct 1999

Loke P, Sim T

Abstract excerpt

Isopenicillin N synthase (IPNS) catalyses a key step in the penicillin and cephalosporin biosynthetic pathway which involves the oxidative cyclisation of the acyclic peptide delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N. Based on crystallographic evidence from the Aspergillus nidulans IPNS crystal structure complexed with the substrate ACV (Roach et al. (1997) Nature 387, 827-830), we...

Topics

Acremonium
Amino Acid Sequence
Arginine
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Oxidoreductases
Protein Structure, Secondary
Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 10518746
DOI: 10.1111/j.1574-6968.1999.tb08758.x

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