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pubmed-article:10328314pubmed:abstractTextA one-step enzymatic synthesis of the conformationally restrained tyrosine analog (2S,3R)-beta-methyltyrosine is reported. This synthesis extends the preparative chemistry associated with tyrosine phenol-lyase. This beta-methyltyrosine derivative was shown to be an efficient protein tyrosine kinase substrate, suggesting that conformational restraint may ultimately be used to enhance tyrosine kinase recognition of substrates.lld:pubmed
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pubmed-article:10328314pubmed:authorpubmed-author:KimKKlld:pubmed
pubmed-article:10328314pubmed:authorpubmed-author:ColeP APAlld:pubmed
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pubmed-article:10328314pubmed:pagination1205-8lld:pubmed
pubmed-article:10328314pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:10328314pubmed:articleTitleSynthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.lld:pubmed
pubmed-article:10328314pubmed:affiliationLaboratory of Bioorganic Chemistry, Rockefeller University, New York, NY 10021, USA.lld:pubmed
pubmed-article:10328314pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10328314pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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