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Stuart Smith

Researcher at Children's Hospital Oakland Research Institute

Publications -  75
Citations -  6640

Stuart Smith is an academic researcher from Children's Hospital Oakland Research Institute. The author has contributed to research in topics: Fatty acid synthase & Acyl carrier protein. The author has an hindex of 40, co-authored 75 publications receiving 6328 citations. Previous affiliations of Stuart Smith include University of California, San Francisco.

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Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine.

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.
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Structural and functional organization of the animal fatty acid synthase.

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.
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The animal fatty acid synthase: one gene, one polypeptide, seven enzymes.

TL;DR: The animal fatty acid synthase comprises two multifunctional polypeptide chains, each containing seven discrete functional domains, juxtaposed head‐to‐tail such that two separate centers for fatty acid assembly are formed at the subunit interface.
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The type I fatty acid and polyketide synthases: a tale of two megasynthases.

TL;DR: This review chronicles the synergistic growth of the fields of fatty acid and polyketide synthesis over the last century and the potential of the basic design has been exploited to the full for the elaboration of a wide range of secondary metabolites of extraordinary structural diversity.