Anil K. Joshi

TL;DR: The results suggest that the role of the Cys --> Gln beta-ketoacyl synthases found in the loading domains of some modular polyketide synthases likely is to act as malonyl, or methylmalonyL, decarboxylases that provide a source of primer for the chain extension reactions catalyzed by associated modules containing fully competent beta- ketoacyL synthases.

TL;DR: A revised model for the fatty acid synthase is suggested in which the two polypeptides are oriented such that head-to-tail contacts are formed both between and within subunits.

TL;DR: The new FAS structure provides a new paradigm for understanding the architecture of FAS and the related modular polyketide synthases and indicates that only limited local rearrangements are required for catalytic interaction among different functional domains.

TL;DR: A single candidate 4′-phosphopantetheine transferase, identified by BLAST searches of the human genome sequence data base, has been cloned, expressed, and characterized and appears to utilize a single, broad specificity enzyme for all posttrans lysine catabolism reactions.

TL;DR: Examination of the completed domain map for the animal fatty acid synthase indicates that the catalytic domains are clustered in two groups separated by a central structural core: the ketoacyl synthase, malonyl/acetyltransferase, and dehydrase in the amino-terminal half and the enoyl reductase, ketoreductase, acyl carrier protein, and thioesterase in the carboxyl- terminus of the transferase domain.