| A novel method of preparing totally alpha-deuterated amino acids for selective incorporation into proteins. Application to assignment of 1H resonances of valine residues in dihydrofolate reductase. | |
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MedLine Citation:
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PMID: 2121536 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The pyridoxal/2H2O exchange reaction of the alpha-CH of amino acids is known to be accompanied by racemisation: Thus by using a D-amino acid as the starting material any L-amino acid formed in the reaction will be essentially fully deuterated at its alpha-position. We have used this method to prepare alpha-deuterated L-valine and incorporated this biosynthetically into L. casei dihydrofolate reductase. A comparison of the alpha CH-NH fingerprint regions of COSY spectra of deuterated and normal DHFR complexes allows one to identify cross-peaks from 15 of the 16 valine residues. |
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Authors:
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J Feeney; B Birdsall; G Ostler; M D Carr; M Kairi |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: FEBS letters Volume: 272 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 1990 Oct |
Date Detail:
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Created Date: 1990-12-13 Completed Date: 1990-12-13 Revised Date: 2000-12-18 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 197-9 Citation Subset: IM |
Affiliation:
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Laboratory of Molecular Structure, National Institute for Medical Research, London, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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metabolism* Deuterium* Isotope Labeling / methods* Lactobacillus casei / enzymology Magnetic Resonance Spectroscopy* Tetrahydrofolate Dehydrogenase / biosynthesis*, chemistry Valine / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 7004-03-7/Valine; 7782-39-0/Deuterium; EC 1.5.1.3/Tetrahydrofolate Dehydrogenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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