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Literature summary for 3.1.30.2 extracted from

  • Koziolkiewicz, M.; Owczarek, A.; Domanski, K.; Nowak, M.; Guga, P.; Stec, W.J.
    Stereochemistry of cleavage of internucleotide bonds by Serratia marcescens endonuclease (2001), Bioorg. Med. Chem., 9, 2403-2409.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Serratia marcescens
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Reaction

Reaction Comment Organism Reaction ID
endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products one-step in line mechanism of enzymatic hydrolysis. The enzyme hydrolyzes internucleotide phosphothioate linkages of Rp configuration with inversion of configuration at the P-atom. The enzyme is stereoselective towards internucleotide phosphothioate linkages of Rp configuration. The involvement of a non-bridging oxygen in contact with a magnesium ion is a critical discriminatory factor for selectivity towards phosphothioate analogues Serratia marcescens