Literature summary for 4.1.1.17 extracted from

Birkholtz, L.M.; Wrenger, C.; Joubert, F.; Wells, G.A.; Walter, R.D.; Louw, A.I.
Parasite-specific inserts in the bifunctional S-adenosylmethionine decarboxylase/ornithine decarboxylase of Plasmodium falciparum modulate catalytic activities and domain interactions (2004), Biochem. J., 377, 439-448.

Search for more literature for 4.1.1.17

Protein Variants

Protein Variants	Comment	Organism
additional information	enzyme activity is reduced up to 95% when the deletion of a parasite-specific insert occurs within the respective domain. Inserts mediate specific physical interactions between the two domains of the bifunctional enzyme that are essential for both S-adenosylmethionine decarboxylase and ornithine decarboxylase activities	Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
330000	-	gel filtration	Plasmodium falciparum

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q9U8D4	bifunctional S-adenosylmethionine decarboxylase/ornithine decarboxylase	-

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Release 2023.1 (January 2023)