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

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

Volume: 7 Issue: 4

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

Affiliation:

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.

Cite this article as:

Tai Chia-Hui, Cook F. Paul and Schnackerz D. Klaus, Conformation of the α-aminoacrylate intermediate of o-acetylserine sulfhydrylase from salmonella typhimurium as inferred by 31p nmr spectroscopy, Protein & Peptide Letters 2000; 7 (4) . https://dx.doi.org/10.2174/092986650704221206151806