Premium
A novel method of preparing totally α‐deuterated amino acids for selective incorporation into proteins
Author(s) -
Feeney J.,
Birdsall B.,
Ostler G.,
Carr M.D.,
Kairi M.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80483-y
Subject(s) - deuterium , valine , chemistry , amino acid , dihydrofolate reductase , stereochemistry , pyridoxal , hydrogen–deuterium exchange , alanine , alpha (finance) , phosphate , biochemistry , mass spectrometry , chromatography , enzyme , medicine , physics , construct validity , nursing , quantum mechanics , patient satisfaction
The pyridoxal/ 2 H 2 O exchange reaction of the α‐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 α‐position. We have used this method to prepare α‐deuterated L‐valine and incorporated this biosynthetically into L. casei dihydrofolate reductase. A comparison of the αCH‐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.