Abstract
The fatty acid biosynthetic (FAS-B)pathway of Brevibacterium ammoniagenes was used to produce triacetic acid lactone (TAL) from glucose rather than a petroleum-based raw material. The ketoreductase (KR) domain of the FAS-B was inactivated by mutating its key catalytic residue to enable it to produce TAL. It was assumed that the KR domain would include the sequence from amino acid residue 2051 to 2319. This sequence turned out to be a member of the short-chain dehydrogenase/reductase (SDR) superfamily. A replacement in the sequence was made to inactivate it. Saccharomyces cerevisiae yeast was transformed to express the modified FAS-B and also phosphopantethiene tranferase (PPT1) from B. ammoniagenes. The yeast was able to produce TAL in vivo.
| Original language | English |
|---|---|
| Pages (from-to) | 4-5 |
| Number of pages | 2 |
| Journal | Industrial Bioprocessing |
| Volume | 26 |
| Issue number | 5 |
| State | Published - May 2004 |
ASJC Scopus subject areas
- Energy (miscellaneous)