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PMID: 1618296 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

On the catalytic mechanism of EcoRI and EcoRV. A detailed proposal based on biochemical results, structural data and molecular modelling.

FEBS letters ·Vol. 304 ·No. 1 ·1992-06-08 ·Pages 4-8

Jeltsch A, Alves J, Maass G, Pingoud A

Abstract

EcoRI and EcoRV 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, Mg2+. The mechanism proposed may also apply to other nucleases.

MeSH Terms
Binding Sites DNA/metabolism Deoxyribonuclease EcoRI/chemistry,metabolism Deoxyribonucleases, Type II Site-Specific/chemistry,metabolism Models, Molecular
Chemicals
DNA Deoxyribonuclease EcoRI Deoxyribonucleases, Type II Site-Specific GATATC-specific type II deoxyribonucleases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jeltsch A
Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover, Germany.
Alves J
Maass G
Pingoud A
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1992-06-08
Pages
4-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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