Premium
On the catalytic mechanism of Eco RI and Eco RV A detailed proposal based on biochemical results, structural data and molecular modelling
Author(s) -
Jeltsch Albert,
Alves Jürgen,
Maass Günter,
Pingoud Alfred
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80576-3
Subject(s) - phosphodiester bond , scissile bond , chemistry , stereochemistry , molecule , dna , mechanism (biology) , protonation , cofactor , cleavage (geology) , active site , catalysis , enzyme , biochemistry , biology , rna , ion , paleontology , organic chemistry , fracture (geology) , gene , philosophy , epistemology
Eco RI and Eco RV have a very similar active site, as is apparent from a comparison of the structures of their respective protein‐DNA complexes. Based on structural and mechanistic data, as well as detailed molecular modelling presented here, a mechanism for the DNA cleavage by these enzymes is suggested in which the attacking water molecule is activated by the phosphate group 3′ to the scissile phosphodiester bond, and in which the leaving group is protonated by a water molecule associated with the essential cofactor, Mg 2+ . The mechanism proposed may also apply to other nucleases.