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Stereoselective synthesis of stable isotope-labeled L-α-amino acids: Chemomicrobiological synthesis of 13C- and 2H-labeled L-cysteine

✍ Scribed by Clifford J. Unkefer; John L. Hanners; Deborah S. Ehler


Publisher
John Wiley and Sons
Year
1991
Tongue
French
Weight
284 KB
Volume
29
Category
Article
ISSN
0022-2135

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✦ Synopsis


Abstract

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.


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