rdf:type |
|
lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2003-9-25
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pubmed:abstractText |
[reaction: see text] d-tert-Leucine was prepared with an enantiomeric excess of >99% by an enzyme-catalyzed oxidative resolution of the racemic mixture of dl-tert-leucine with use of leucine dehydrogenase. The l-amino acid was oxidized completely due to coupling of the primary reaction with a highly efficient irreversible NAD(+)-regenerating step by NADH oxidase.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-amino-3,3-dimethylbutanoic acid,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1523-7060
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3649-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14507195-Amino Acid Oxidoreductases,
pubmed-meshheading:14507195-Bacillus cereus,
pubmed-meshheading:14507195-Catalysis,
pubmed-meshheading:14507195-Kinetics,
pubmed-meshheading:14507195-Leucine,
pubmed-meshheading:14507195-Leucine Dehydrogenase,
pubmed-meshheading:14507195-Multienzyme Complexes,
pubmed-meshheading:14507195-NAD,
pubmed-meshheading:14507195-NADH, NADPH Oxidoreductases,
pubmed-meshheading:14507195-Oxidation-Reduction,
pubmed-meshheading:14507195-Stereoisomerism,
pubmed-meshheading:14507195-Valine
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pubmed:year |
2003
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pubmed:articleTitle |
An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine.
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pubmed:affiliation |
Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, im Forschungszentrum Jülich, 52426 Jülich, Germany. w.hummel@fz-juelich.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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