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What do Structures tell us about the 'Factory Line’ Synthesis of Polyketides
Author(s) -
KeatingeClay Adrian,
Stroud Robert M.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a1472-c
Subject(s) - polyketide synthase , polyketide , modular design , atp synthase , computational biology , chemistry , stereochemistry , biology , combinatorial chemistry , biochemistry , biosynthesis , gene , computer science , programming language
Modular polyketide synthases are multienzyme factories that condense small carbon precursors into complex molecules such as antibiotic, erythromycin, and anti‐cancer agent, epothilone. Due to a lack of structural information, synthases engineered to produce novel polyketides are usually inactive. We describe how current structural data, including high resolution structures of synthase components, enable us to piece together the overall quaternary structure of a synthase.