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pubmed-article:2751995pubmed:abstractTextThe amino acid sequences associated with pyridoxal 5'-phosphate binding sites in chicken liver fatty acid synthase have been determined: a site whose modification causes selective inhibition of the enoyl reductase activity and a site (site I) that is not associated with enzymatic activity. The amino acid sequences of peptides obtained by trypsin hydrolysis of the pyridoxamine 5'-phosphate labeled enzyme were determined. For the site associated with enoyl reductase activity, the sequence similarities between chicken and goose are extensive and include the sequence Ser-X-X-Lys, a characteristic structural feature of pyridoxamine enzymes. In addition, the spatial relationships between the pyridoxal 5'-phosphate binding sites and reductase site(s) have been studied with fluorescence resonance energy-transfer techniques. The distances between site I and the enoyl reductase and beta-ketoacyl reductase sites are greater than 50 and 41-44 A, respectively. The distance between the two reductase sites is greater than 49 A.lld:pubmed
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pubmed-article:2751995pubmed:monthMaylld:pubmed
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pubmed-article:2751995pubmed:authorpubmed-author:HammesG GGGlld:pubmed
pubmed-article:2751995pubmed:authorpubmed-author:ChangS ISIlld:pubmed
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pubmed-article:2751995pubmed:pagination3781-8lld:pubmed
pubmed-article:2751995pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:2751995pubmed:year1989lld:pubmed
pubmed-article:2751995pubmed:articleTitleAmino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase.lld:pubmed
pubmed-article:2751995pubmed:affiliationDepartment of Chemistry, Cornell University, Ithaca, New York 14853-1301.lld:pubmed
pubmed-article:2751995pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2751995pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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