159680-32-7Relevant articles and documents
Enzymatic synthesis of specifically 2H-labelled L-glutamic acids and 2H-, 15N-, 13C-labelled L-glutamines on a preparative scale
Ogrel, A.,Vasilenko, I. A.,Lugtenburg, J.,Raap, J.
, p. 369 - 376 (1994)
In this paper we report the preparation od specifically 2H-labelled L-glutamic acids and 2H-, 15N-, 13C-labelled L-glutamines on the gram scale.The products obtained have high isotope enrichment (>98percent) and high optical purity.The synthetic schemes allow the specific isotope enrichment of every H, C, and N position or any combination of positions. (2-2H)-L-Glutamic acid was synthesized by enantioselective enzymatic conversion of 2-oxoglutaric acid using glutamate dehydrogenase (GDH, E.C. 1.4.1.3.), alcohol dehydrogenase (ADH, E.C. 1.1.1.1.) and (2H6)ethanol. (3,3-2H2)-L-Glutamic acid was prepared by enzymatic conversion of 2-oxo-3,3-dideuteroglutaric acid which was easily obtained from 2-oxoglutaric acid by an isotope exchange reaction in 2H2O at pH 13.0. (4,4-2H2)-L-Glutamic acid was obtained by chemical exchange in 20percent 2HCl.Four different isotopomers of L-glutamine were synthesized by the enantioselective conversion of isotopically labelled L-glutamic acids using glutamine synthetase (GS, E.C. 6.3.1.2.).The amide group of glutamine was labelled with 15N using 15NH4Cl in the enzymatic reaction.The labelled L-glutamic acids and L-glutamines were characterized by 1H-NMR, 13C-NMR and mass spectroscopy.
STABLE ISOTOPE-LABELED AMINO ACID, METHOD OF INTEGRATING THE SAME INTO TARGET PROTEIN, METHOD OF NMR STRUCTURAL ANALYSIS OF PROTEIN AND PROCESS FOR PRODUCING SITE-SELECTIVE STABLE ISOTOPE-LABELED FUMARIC ACID AND TARTARIC ACID
-
Page 14-15, (2010/02/08)
The present invention provides a stable isotope-labeled amino acid which is at least one of amino acids constituting a protein and which has at least one of the following labeling patterns:(a) hydrogen atoms except at least one hydrogen atom in one or more methylene groups are deuterated,(b) hydrogen atoms in one of prochiral gem-methyl groups are completely deuterated,(c) hydrogen atoms in prochiral methyl groups are partially deuterated, and(d) all hydrogen atoms except one of them in methyl group are deuterated and hydrogen atoms in the aromatic ring are partially deuterated. With the stable isotope-labeled amino acid, the deuteration of protein can be attained without damaging the NMR sensitivity of remaining hydrogen nucleus and, in addition, the rapid, accurate analysis of NMR spectrum of a high-molecular protein which is beyond the limitation in the prior art and the determination of the stereo-structure can be performed at the same time.