title: Sequence-specific endonuclease Bgl I. Modification of lysine and arginine residues of the homogeneous enzyme.
abstract: The sequence-specific endonuclease Bgl I from Bacillus globigii (RUB561) has been purified to homogeneity as determined by denaturing polyacrylamide gel analysis. The active form of the enzyme is a single polypeptide with a molecular weight of 32,000. The enzyme requires Mg2+ in the reaction mixture and displays a broad pH and monovalent cation requirement. Bgl I is not sensitive to sulfhydryl reagents but was affected by reagents that modify lysine and arginine residues. When lysine residues were modified by pyridoxal 5'-phosphate, both binding and catalysis were diminished while modification of arginine residues by 2,3-butanedione inhibited the enzyme activity but had no effect on its binding properties.
mesh_terms: D001120:Arginine; D001407:Bacillus / Q000201:enzymology*; D003851:Deoxyribonucleases / Q000302:isolation & purification*; D003931:Diacetyl / Q000494:pharmacology; D004720:Endonucleases / Q000302:isolation & purification*; D007700:Kinetics; D008239:Lysine; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D011732:Pyridoxal Phosphate / Q000494:pharmacology
chemical_list: D011732:Pyridoxal Phosphate; D001120:Arginine; D003851:Deoxyribonucleases; D004720:Endonucleases; D008274:Magnesium; D003931:Diacetyl; D008239:Lysine