Isoforms of Serratia marcescens nuclease. The role of Mg2+ in the hydrolysis mechanism. Academic Article

abstract

• Structural and functional differences between isoforms Sm1 and Sm2, a lack of influence of free Mg2+ on the isoform structures, formation of DNA-magnesium complex serving with great probability as a real substrate for the nuclease has been summarized on the basis of experimental data. Mg2+ forming a complex with phosphate groups of DNA are supposed to further increase the electrophilicity of the phosphorus atoms besides causing a conformational change of the substrate.

authors

• Benedik, Michael

published proceedings

• Biochemistry (Mosc)

author list (cited authors)

• Filimonova, M. N., Gubskaya, V. P., Nuretdinov, I. A., Benedik, M. J., Bogomolnaya, L. M., Andreeva, M. A., & Leshchinskaya, I. B.

citation count

• 5

complete list of authors

• Filimonova, MN||Gubskaya, VP||Nuretdinov, IA||Benedik, MJ||Bogomolnaya, LM||Andreeva, MA||Leshchinskaya, IB

publication date

• September 1997

published in

• Biochemistry (Moscow)  Journal

keywords

• Circular Dichroism
• DNA
• Endodeoxyribonucleases
• Endoribonucleases
• Hydrolysis
• Isoelectric Point
• Isoenzymes
• Kinetics
• Magnesium
• Protein Conformation
• Serratia Marcescens
• Structure-Activity Relationship

PubMed Central ID

• 9457762

start page

• 983

end page

• 988

volume

• 62

issue

• 9