Add time:08/20/2019         Source:sciencedirect.com

Publisher SummaryThis chapter focuses on β-hydroxydecanoyl thioester dehydrase, the present preparations of which are homogeneous in the ultracentrifuge and migrate as a single entity on polyacrylamide gels. The thioester derivatives of the straight-chain 10-carbon acids are the most active substrates for dehydrase. The dehydration step leading to the olefinic precursor of palmitoleate and vaccenate occurs only at the C10 stage. The negligible activity of the next lower (C8) and the next higher (C12) even-numbered homologues as dehydrase substrates rationalizes the absence of Δ11-C16 and Δ13-C18 acids in E. coli lipids. Although the activity of the C9 and C11 substrates is substantial, dehydrase operates as a C10 specific enzyme in the cell since odd-numbered fatty acids do not normally occur in E. coli lipids. The introduction of branches into the carbon chain also lowers activity drastically. The active site of dehydrase is designed to accommodate only linear hydrocarbon chains and these cannot be longer than C11 or shorter than C9.

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