## 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
Stereoselective synthesis of stable isotope-labeled L-α-amino acids: Biosynthesis of 2H-, 13C-, and 15N-labeled L-serines
✍ Scribed by John Hanners; Rowena Gibson; Karen Velarde; Judy Hammer; Mark Alvarez; Janet Griego; Clifford J. Unkefer
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- French
- Weight
- 460 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0022-2135
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
We have developed a stereospecific biosynthesis of ^13^C‐ and ^15^N‐labeled L‐serine which involves the serine‐type methylotroph Methylobacterium extorquens AM1. In this biosynthesis, C‐3 of serine is derived from methanol while C‐2, C‐1 and the α‐amino group are derived from glycine. By starting with the appropriate labeling precursor, we can produce any of the ^2^H, ^13^C and/or ^15^N isotopomers of L‐serine. Using a 5‐L culture, 40–50 millimoles of L‐serine are produced; L‐serine and glycine are recovered from the growth medium and then separated chromatographically.
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