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Literature summary extracted from

  • Harijan, R.K.; Hoff, O.; Ducati, R.G.; Firestone, R.S.; Hirsch, B.M.; Evans, G.B.; Schramm, V.L.; Tyler, P.C.
    Selective inhibitors of Helicobacter pylori methylthioadenosine nucleosidase and human methylthioadenosine phosphorylase (2019), J. Med. Chem., 62, 3286-3296 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.9 structure in complex with transition state analogue inhibitors Helicobacter pylori

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.9 (4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(ethynylsulfanyl)methyl]pyrrolidin-3-ol transition-state analogue, shows significant overlap in specificity with human 5'-methylthioadenosine phosphorylase MTAP Helicobacter pylori
3.2.2.9 (4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(pent-4-yn-1-yl)sulfanyl]methyl]pyrrolidin-3-ol transition-state analogue, best binding inhibitor tested, shows significant overlap in specificity with human 5'-methylthioadenosine phosphorylase MTAP Helicobacter pylori

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.9 Helicobacter pylori A0A1W0VQJ9
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Synonyms

EC Number Synonyms Comment Organism
3.2.2.9 BW246_00770
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Helicobacter pylori