Literature summary for 4.1.1.50 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.

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Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of parasite-specific regions, analysis of influence on catalytic activities and domain interactions, co-incubation of monofunctional heterotetrameric S-adenosyl-L-methionine decarboxylase domain with monofunctional, homodimeric ornithine decarboxylase domain produces an active hybrid complex of 330,000 Da	Plasmodium falciparum

Organism

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

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Release 2023.1 (January 2023)