Document Detail


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.
MedLine Citation:
PMID:  2121536     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
J Feeney; B Birdsall; G Ostler; M D Carr; M Kairi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  FEBS letters     Volume:  272     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1990 Oct 
Date Detail:
Created Date:  1990-12-13     Completed Date:  1990-12-13     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  197-9     Citation Subset:  IM    
Affiliation:
Laboratory of Molecular Structure, National Institute for Medical Research, London, UK.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism*
Deuterium*
Isotope Labeling / methods*
Lactobacillus casei / enzymology
Magnetic Resonance Spectroscopy*
Tetrahydrofolate Dehydrogenase / biosynthesis*,  chemistry
Valine / metabolism*
Chemical
Reg. No./Substance:
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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