Electrostatic suppression allows tyrosine site-specific recombination in the absence of a conserved catalytic arginine
PA Rowley, AH Kachroo, CH Ma, AD Maciaszek… - Journal of Biological …, 2010 - ASBMB
The active site of the tyrosine family site-specific recombinase Flp contains a conserved
catalytic pentad that includes two arginine residues, Arg-191 and Arg-308. Both arginines
are essential for the transesterification steps of strand cleavage and strand joining in DNA
substrates containing a phosphate group at the scissile position. During strand cleavage, the
active site tyrosine supplies the nucleophile to form a covalent 3′-phosphotyrosyl
intermediate. The 5′-hydroxyl group produced by cleavage provides the nucleophile to re …
catalytic pentad that includes two arginine residues, Arg-191 and Arg-308. Both arginines
are essential for the transesterification steps of strand cleavage and strand joining in DNA
substrates containing a phosphate group at the scissile position. During strand cleavage, the
active site tyrosine supplies the nucleophile to form a covalent 3′-phosphotyrosyl
intermediate. The 5′-hydroxyl group produced by cleavage provides the nucleophile to re …
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