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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Review Article

Conformation of the α-aminoacrylate intermediate of o-acetylserine sulfhydrylase from salmonella typhimurium as inferred by 31p nmr spectroscopy

Author(s): Chia-Hui Tai, Paul F. Cook and Klaus D. Schnackerz

Volume 7, Issue 4, 2000

Page: [207 - 210] Pages: 4

DOI: 10.2174/092986650704221206151806

Price: $65

Abstract

31P NMR chemical shifts of the internal aldimine and the cx.-aminoacrylate intermediate of 0- acetylserine sulfhydrylase were determined and found to be 5.13 and 3.95 ppm, respectively. In addition, the line width decreases upon addition of OAS, suggesting a less restricted rotation around the CS'-0 bond of pyridoxal 5' -phosphate in the cx.-aminoacrylate intermediate The upfield shift of the cx.-aminoacrylate is similar to the behavior of the L-serine external Schiff base and may be interpreted as a loosening of the active site.

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