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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
43
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pubmed:dateCreated |
2010-10-27
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pubmed:abstractText |
By replacing a single active-site residue Cys107 with Ser in phenylalanine aminomutase (PAM), the enzyme gained tyrosine aminomutase (TAM) activity while retaining PAM activity and high enantioselectivity. This engineered enantioselective TAM also catalyzed formation of ?-tyrosine from p-coumaric acid and may prove to be useful for the synthesis of enantiopure ?-tyrosine and its derivatives.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1364-548X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
21
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8157-9
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pubmed:meshHeading |
pubmed-meshheading:20924508-Amino Acid Sequence,
pubmed-meshheading:20924508-Amino Acid Substitution,
pubmed-meshheading:20924508-Ammonia-Lyases,
pubmed-meshheading:20924508-Catalytic Domain,
pubmed-meshheading:20924508-Intramolecular Transferases,
pubmed-meshheading:20924508-Kinetics,
pubmed-meshheading:20924508-Molecular Sequence Data,
pubmed-meshheading:20924508-Mutation,
pubmed-meshheading:20924508-Protein Engineering,
pubmed-meshheading:20924508-Protein Structure, Tertiary,
pubmed-meshheading:20924508-Sequence Alignment,
pubmed-meshheading:20924508-Stereoisomerism,
pubmed-meshheading:20924508-Tyrosine
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pubmed:year |
2010
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pubmed:articleTitle |
Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase.
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pubmed:affiliation |
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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