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Stereoselective synthesis of stable isotope‐labeled L‐α‐amino acids: Chemomicrobiological synthesis of 13 C‐ and 2 H‐labeled L‐cysteine
Author(s) -
Unkefer Clifford J.,
Hanners John L.,
Ehler Deborah S.
Publication year - 1991
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.2580291108
Subject(s) - chemistry , serine , cysteine , tryptophan synthase , stereochemistry , nucleophile , amino acid , biosynthesis , tryptophan , enzyme , biochemistry , catalysis
Tryptophan synthase catalyzes the nucleophilic replacement of the hydroxyl group at C‐3 of L‐serine. This enzyme can use benzyl mercaptan as a nucleophile in the conversion of serine to S‐benzyl‐L‐cysteine which is deblocked by treatment with sodium in liquid ammonia to yield L‐cysteine. A strain of E. coli engineered to overproduce tryptophan synthase was used in the conversion of L‐serine to L‐cysteine. Labeled serine was prepared biosynthetically as described previously.