Changing the hydrogen-bonding potential in the DNA binding site of EcoRI by site-directed mutagenesis drastically reduces the enzymic activity, not, however, the preference of this restriction endonuclease for cleavage within the site -GAATTC-

Biochemistry ◽  
1989 ◽  
Vol 28 (6) ◽  
pp. 2678-2684 ◽  
Author(s):  
Jurgen Alves ◽  
Thomas Rueter ◽  
Robert Geiger ◽  
Anja Fliess ◽  
Guenter Maass ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Dna Binding ◽  
Binding Site ◽  
Restriction Endonuclease ◽  
Enzymic Activity ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Dna Binding Site ◽  
Hydrogen Bonding Potential

How Does a DNA Interacting Enzyme Change Its Specificity during Molecular Evolution? A Site-Directed Mutagenesis Study at the DNA Binding Site of the DNA-(Adenine-N6)-methyltransferaseEcoRV†

Biochemistry ◽  
2001 ◽  
Vol 40 (37) ◽  
pp. 10956-10965 ◽  
Author(s):  
Carsten Beck ◽  
Susanne Cranz ◽  
Merdol Solmaz ◽  
Markus Roth ◽  
Albert Jeltsch
Keyword(s):  
Molecular Evolution ◽  
Dna Binding ◽  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Dna Binding Site ◽  
Enzyme Change ◽  
A Site ◽  
Mutagenesis Study

Probing the function of individual amino acid residues in the DNA binding site of the EcoRI restriction endonuclease by analysing the toxicity of genetically engineered mutants

Gene ◽  
1990 ◽  
Vol 89 (1) ◽  
pp. 19-27 ◽  
Author(s):  
Thomas Oelgeschläger ◽  
Robert Geiger ◽  
Thomas Rüter ◽  
Jürgen Alves ◽  
Anja Fliess ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Binding Site ◽  
Restriction Endonuclease ◽  
Genetically Engineered ◽  
Individual Amino Acid ◽  
Amino Acid Residues ◽  
Dna Binding Site ◽  
Ecori Restriction

scholarly journals Evidence for the presence of an essential arginine residue in photoreactivating enzyme from Streptomyces griseus

1985 ◽  
Vol 229 (2) ◽  
pp. 469-476 ◽  
Author(s):  
A P M Eker
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Streptomyces Griseus ◽  
Enzymic Activity ◽  
Borate Buffer ◽  
Arginine Residue ◽  
Dna Binding Site ◽  
Arginine Residues ◽  
Kinetics Of ◽  
Kinetics Of Inhibition

Butane-2,3-dione inhibits the enzymic activity of Streptomyces griseus photoreactivating enzyme (PRE). Some characteristics of the inhibition, notably the enhancement by borate buffer and the reversibility, indicate that arginine residues are modified. From the kinetics of inhibition it can be concluded that a single essential arginine residue is involved. U.v.-irradiated DNA, the substrate for PRE, protects the enzyme against inactivation by butane-2,3-dione. This suggests that the essential arginine residue is situated in or near the u.v.-irradiated-DNA-binding site. Non-irradiated DNA at higher concentrations also protects against inactivation, indicating that PRE can form non-specific complexes. From the ratio of complex constants obtained from protection experiments with non-irradiated and u.v.-irradiated DNA it appears that PRE preferably binds to dimer sites.

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