NDLI: The effect of divalent cations on the catalytic activity of the human plasma 3′-exonuclease

Content Provider	Springer Nature Link
Author	Wojcik, Marzena Stec, Wojciech J.
Copyright Year	2010
Abstract	The 3′-exonuclease from human plasma is a soluble form of nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) (EC 3.1.4.1/EC 3.6.1.9). Here, the possibility of divalent cation influence for the 3′-exonuclease activity was investigated using the phosphorothioate congener of oligonucleotide containing all phosphorothioate internucleotide linkages of the [RP]-configuration ([RP-PS]-d[T12]) as the substrate for this enzyme. It was found that the 3′-exonuclease is a metalloenzyme, i.e. its phosphodiesterase activity was completely abolished at 0.8 mM concentration EDTA and, in turn, it was restored in the presence of Mg2+ or Mn2+ ions. In addition, Mg2+ can be replaced effectively by Ca2+, Mn2+, or Co2+, but not by Ni2+ and Cd2+ during the hydrolysis of the phosphorothioate substrate in human plasma. In addition, the mechanism is postulated, by which a single internucleotide phosphorothioate bond of the SP-configuration at the 3′-end of unmodified phosphodiesters (PO-oligos), or their phosporothioate analogs (PS-oligos) protects these compounds against degradation in blood.
Starting Page	1113
Ending Page	1121
Page Count	9
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	23
Issue Number	6
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-06-30
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	The human plasma 3′-exonuclease NPP1 Catalysis Phosphorothioates Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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