Stereochemical support for Serratia endonuclease active-site
geometry*
W. J. Stec**1, M. Koziolkiewicz1, and K. Taira2
1Department of Bioorganic
Chemistry, Centre of Molecular and Macromolecular Studies, Polish Academy
of Sciences, 90-363 Lódz, Poland; 2Department of Chemistry
and Biotechnology, Graduate School of Engineering, University of Tokyo,
Hongo, Tokyo 113-8656, Japan
Abstract: Earlier observation that stereoregular All-Rp-PS-oligonucleotides
in the presence of nonsequence-specific Serratia endonuclease
undergo nucleolytic degradation, confronted with recently published
results on the active-site architecture of this enzyme, strongly supports
an involvement of 3'-bridging and pro-Sp-nonbridging oxygen atoms
of scissile internucleotide bond in the interactions with hydrated magnesium
ion anchored by Asn-119 residue of this endonuclease.
*Lecture presented at the 13th International
Conference on Organic Synthesis (ICOS-13), Warsaw, Poland, 1-5 July
2000.
** Corresponding author
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