Details
| Original language | English |
|---|---|
| Pages (from-to) | 680-682 |
| Number of pages | 3 |
| Journal | Molecular BioSystems |
| Volume | 6 |
| Issue number | 4 |
| Publication status | Published - 26 Mar 2010 |
| Externally published | Yes |
Abstract
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.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
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In: Molecular BioSystems, Vol. 6, No. 4, 26.03.2010, p. 680-682.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Mutation of key residues in the C-methyltransferase domain of a fungal highly reducing polyketide synthase
AU - Skellam, Elizabeth J.
AU - Hurley, Deirdre
AU - Davison, Jack
AU - Lazarus, Colin M.
AU - Simpson, Thomas J.
AU - Cox, Russell J.
PY - 2010/3/26
Y1 - 2010/3/26
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77949685299&partnerID=8YFLogxK
U2 - 10.1039/b923990a
DO - 10.1039/b923990a
M3 - Article
C2 - 20237645
AN - SCOPUS:77949685299
VL - 6
SP - 680
EP - 682
JO - Molecular BioSystems
JF - Molecular BioSystems
SN - 1742-206X
IS - 4
ER -