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Literature summary extracted from

  • Burger, P.B.; Birkholtz, L.M.; Joubert, F.; Haider, N.; Walter, R.D.; Louw, A.I.
    Structural and mechanistic insights into the action of Plasmodium falciparum spermidine synthase (2007), Bioorg. Med. Chem., 15, 1628-1637.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.16 drug development the enzyme is a drug target in the malaria parasite, Plasmodium falciparum, due to the vital role of spermidine in the activation of the eukaryotic translation initiation factor and cell proliferation Plasmodium falciparum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.16 construction of a crystal structure homology model, PDB ID: Q9FS5, for the Plasmodium falciparum enzyme from crystal structure 1JQ3 and 1XJ5, structure-function relationship Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.16 D196N site-directed mutagenesis, the mutant activity is reduced by 89% compared to the wild-type enzyme Plasmodium falciparum
2.5.1.16 S197A site-directed mutagenesis, the mutant activity is reduced by 24% compared to the wild-type enzyme Plasmodium falciparum
2.5.1.16 Y102A site-directed mutagenesis, the mutant activity is reduced by 91% compared to the wild-type enzyme Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.16 trans-4-Methylcyclohexylamine i.e. 4MCHA, binding structure Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.16 additional information
-
 additional information molecular dynamics Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.16 S-adenosylmethioninamine + putrescine Plasmodium falciparum spermidine plays an important role in the activation of the eukaryotic translation initiation factor and cell proliferation 5'-S-methyl-5'-thioadenosine + spermidine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.16 Plasmodium falciparum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.16 S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine reaction mechanism involving a gate-keeping loop, active site and substrate binding structures and involved residues, structure-function relationship analysis by molecular dynamics simulations of a homology model Plasmodium falciparum
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.16 S-adenosylmethioninamine + putrescine
-
 Plasmodium falciparum 5'-S-methyl-5'-thioadenosine + spermidine
-
 ?
2.5.1.16 S-adenosylmethioninamine + putrescine spermidine plays an important role in the activation of the eukaryotic translation initiation factor and cell proliferation Plasmodium falciparum 5'-S-methyl-5'-thioadenosine + spermidine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.16 More structure-function relationship, overview Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.5.1.16 SPDSYN
-
 Plasmodium falciparum