10328314

Source:http://linkedlifedata.com/resource/pubmed/id/10328314

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0041493, umls-concept:C0220781, umls-concept:C0390759, umls-concept:C1883254
pubmed:issue	8
pubmed:dateCreated	1999-8-3
pubmed:abstractText	A 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.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9107377
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Methyltyrosines, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine Phenol-Lyase
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	0960-894X
pubmed:author	pubmed-author:ColeP APA, pubmed-author:KimKK
pubmed:issnType	Print
pubmed:day	19
pubmed:volume	9
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1205-8
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:10328314-Catalysis, pubmed-meshheading:10328314-Methyltyrosines, pubmed-meshheading:10328314-Tyrosine Phenol-Lyase
pubmed:year	1999
pubmed:articleTitle	Synthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.
pubmed:affiliation	Laboratory of Bioorganic Chemistry, Rockefeller University, New York, NY 10021, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't