## Abstract We have developed a stereospecific chemomicrobiological synthesis of labeled tryptophan. L‐[3‐^13^C]Serine, [1‐^15^N]‐ and [2‐^13^C]indole were used as precursors for the synthesis of L‐[β‐^13^C]‐, L‐[1′‐^15^N]‐, and L‐[2′‐^13^C]tryptophan, respectively. The labeled precursors were inco
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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