Mutation of key residues in the C-methyltransferase domain of a fungal highly reducing polyketide synthase.
Site directed mutations of the C-methyltransferase domain of squalestatin tetraketide synthase were made in an attempt to alter the methylation pattern of the synthase expressed in vivo: mutation resulted in either no effect or in complete abrogation of polyketide production.
Skellam
Elizabeth J
EJ
School of Chemistry, University of Bristol, Cantock's Close, Bristol, UK.
Hurley
Deirdre
D
Davison
Jack
J
Lazarus
Colin M
CM
Simpson
Thomas J
TJ
Cox
Russell J
RJ
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001236:Aspergillus oryzae / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D017931:DNA Primers / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D048630:Polyketide Synthases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D049490:Systems Biology
D017931:DNA Primers; D004269:DNA, Bacterial; D005656:Fungal Proteins; D011994:Recombinant Proteins; D048630:Polyketide Synthases