685879-20-3

Upstream product

• 1730-97-8 (S)-2-methylbutyraldehyde 
• 131685-53-5 (S)-4-benzyl-3-propionyl-2-oxazolidinone 
• 105-30-6 (S)-2-methyl-1-pentanol 
• 1565-80-6 (2S)-2-methyl-1-butanol 
• 96-17-3 2-Methylbutyraldehyde 
• 69739-34-0 t-butyldimethylsiyl triflate 
• 248251-87-8 (4S)-4-benzyl-3-[(2S,3R,4S)-3-hydroxy-2,4-dimethylhexanoyl]oxazolidin-2-one 

Downstream Products

• 685879-19-0 (4R)-4-benzyl-3-[(2R,3S,4R,5R,6S)-5-[(tert-butyl)dimethylsilyloxy]-3-hydroxy-2,4,6-trimethyloctanoyl]oxazolidin-2-one 

Relevant academic research and scientific papers

Total synthesis and structural elucidation of ent-micropyrone and (+)-ascosalipyrone

The total synthesis of 6-[(1S,3S)-1,3-dimethyl-2-oxopentyl]-4-hydroxy-3,5- dimethyl-2H-pyran-2-one (22), the enantiomer of the natural product micropyrone (1), was achieved in 9 linear steps (10% overall yield), from Evans auxiliary (R)-12 with key coupli

Precursor-Directed Biosynthesis: Stereospecificity for Branched-Chain Diketides of the β-Ketoacyl-ACP Synthase Domain 2 of 6-Deoxyerythronolide B Synthase

Modular polyketide synthases such as 6-deoxyerythronolide B synthase (DEBS) catalyze the biosynthesis of structurally complex natural products. Streptomyces coelicolor CH999/pJRJ2 harbors a plasmid encoding DEBS(KS1 0), a mutant form of 6-deoxyerythronolide B synthase that is blocked in the formation of 6-deoxyerythronolide B (1, 6-dEB) due to a mutation in the active site of the ketosynthase (KS1) domain that normally catalyzes the first polyketide chain-elongation step of 6-dEB biosynthesis. Administration of (2S,3R,4S)- and (2S,3R,4R)-3-hydroxy-2,4-dimethylhexanoic acid N-acetylcysteamine (SNAC) thioesters (= S-[2-(acetylamino)ethyl] (2S,3R,4S)- and (2S,3R,4R)-3-hydroxy-2,4-dimethylhexanethioates) 3 and 4 in separate experiments to cultures of Streptomyces coelicolor CH999/pJRJ2 led to production of the corresponding (14S)- and (14R)-14-methyl analogues of 6-dEB, 10 and 11, respectively. Unexpectedly, when a 3:2 mixture of 4 and 3 was fed under the same conditions, exclusively branched-chain macrolactone 11 was isolated. In similar experiments, feeding of 3 and 4 to S. coelicolor CH999/pCK16, an engineered strain harboring DEBS1 + TE(KS10), resulted in formation of the branched-chain triketide lactones 13 and 14, while feeding of the 3:2 mixture of 4 and 3 gave exclusively 14. The biochemical basis for this stereochemical discrimination was established by using purified DEBS module 2 + TE to determine the steady-state kinetic parameters for 3 and 4, with the kcat/KM for 4 shown to be sevenfold greater than that of 3.