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 .
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 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.2.2.9 |
BW246_00770 |
- |
Helicobacter pylori |