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Literature summary for 2.5.1.16 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

Application Comment Organism
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)

Crystallization (Comment) Organism
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

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

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosylmethioninamine + putrescine
-
Plasmodium falciparum 5'-S-methyl-5'-thioadenosine + spermidine
-
?
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

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

Synonyms

Synonyms Comment Organism
SPDSYN
-
Plasmodium falciparum