ArticleThe Journal of biological chemistry2013
Arginine as a general acid catalyst in serine recombinase-mediated DNA cleavage.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
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- Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.The Journal of biological chemistry · 2017Article
- Structure and function of HWE/HisKA2-family sensor histidine kinases.Current opinion in microbiology · 2017Review
- Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Advances in protein chemistry and structural biology · 2017Article
- Nicked-site substrates for a serine recombinase reveal enzyme-DNA communications and an essential tethering role of covalent enzyme-DNA linkages.Nucleic acids research · 2015Article
- Mechanisms of DNA Transposition.Microbiology spectrum · 2015Review
- Serine Resolvases.Microbiology spectrum · 2015Review
- Expanding the zinc-finger recombinase repertoire: directed evolution and mutational analysis of serine recombinase specificity determinants.Nucleic acids research · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Members of the serine family of site-specific DNA recombinases use an unusual constellation of amino acids to catalyze the formation and resolution of a covalent protein-DNA intermediate. A recent high resolution structure of the catalytic domain of Sin, a particularly well characterized family member, provided a detailed view of the catalytic site. To determine how the enzyme might protonate and stabilize the 3'O leaving group in the strand cleavage reaction, we examined how replacing this oxygen with a sulfur affected the cleavage rate by WT and mutant enzymes. To facilitate direct comparison of the cleavage rates, key experiments used suicide substrates that prevented religation after cleavage. The catalytic defect associated with mutation of one of six highly conserved arginine residues, Arg-69 in Sin, was partially rescued by a 3' phosphorothiolate substrate. We conclude that Arg-69 has an important role in stabilizing the 3'O leaving group and is the prime candidate for the general acid that protonates the 3'O, in good agreement with the position it occupies in the high resolution structure of the active site of Sin.
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