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Literature summary for 2.5.1.16 extracted from

  • Dufe, V.T.; Qiu, W.; Mueller, I.B.; Hui, R.; Walter, R.D.; Al-Karadaghi, S.
    Crystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATO (2007), J. Mol. Biol., 373, 167-177.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in apo form, in complex with S-adenosylmethioninamine in complex with and two inhibitors, S-adenosyl-1,8-diamino-3-thio-octane and trans-4-methylcyclohexylamine. Binding of S-adenosylmethioninamine stabilizes the conformation of the flexible gatekeeper loop of the enzyme and affects the conformation of the active-site amino acid residues, preparing the protein for binding of the second substrate. Inhibitor S-adenosyl-1,8-diamino-3-thio-octane essentially fills the entire active-site pocket, inhibitor trans-4-methylcyclohexylamine only occupies part of it Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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