Substrate Specificity of the Loading Didomain of the Erythromycin Polyketide Synthase †
✍ Scribed by Lau, Janice; Cane, David E.; Khosla, Chaitan
- Book ID
- 126206304
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 70 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0006-2960
No coin nor oath required. For personal study only.
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## Background: Polyketides are important compounds with antibiotic and anticancer activities. several modular polyketide synthases (pkss) contain a terminal thioesterase (te) domain probably responsible for the release and concomitant cyclization of the fully processed polyketide chain. because the
DEBS 1 + TE is a recombinant modular polyketide synthase (PKS) in which the first two biosynthetic modules of the 6-deoxyerythronolide B synthase are linked to the thioesterase domain normally found at the C-terminus of DEBS 3. Incubation of DEBS 1 + TE with propionyl-CoA, methylamalonyl-CoA, and NA