S
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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Journal ArticleDOI
Isolation of a functional transferase component from the rat fatty acid synthase by limited trypsinization of the subunit monomer. Formation of a stable functional complex between transferase and acyl carrier protein domains.
TL;DR: The results provide the first direct evidence that, in the head-to-tail oriented fatty acid synthase homodimer, functional communication between the transferase domain located near the end of one polypeptide and the acyl carrier protein domain located at the opposite end of the other polyPEptide is facilitated by a stable physical interaction between these domains.
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Regulatory elements in the first intron of the rat fatty acid synthase gene
TL;DR: The results suggest that the dominant negative element of the first intron may play a role in determining the tissue-specific expression of the FAS gene.
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The carboxyl-terminal region of thioesterase II participates in the interaction with fatty acid synthase. Use of electrospray ionization mass spectrometry to identify a carboxyl-terminally truncated form of the enzyme.
TL;DR: The results of modification of Cys256 by thionitrobenzoate and removal of residues 262 and 263 by endogenous proteases indicate that integrity of the carboxyl-terminal region is important for interaction with its acyl-fatty acid synthase substrate.
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Fatty Acid Synthase Dimers Containing Catalytically Active β-Ketoacyl Synthase or Malonyl/Acetyltransferase Domains in Only One Subunit Can Support Fatty Acid Synthesis at the Acyl Carrier Protein Domains of Both Subunits
TL;DR: The results support a modified model for the animal fatty acid synthase in which head-to-tail functional contacts are possible both within as well as between subunits.
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Interaction of rat mammary gland thioesterase II with fatty acid synthetase is dependent on the presence of acyl chains on the synthetase.
TL;DR: Results indicate that the two enzymes associate when an acyl chain is present on the synthetase and that they dissociate rapidly following completion of the catalytic process, which differs from that of the avian uropygial gland in which the two enzyme associate to form a stable complex even in the absence of substrates.