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Article

Novel properties of malarial S-adenosylmethionine decarboxylase as revealed by structural modelling.

Journal of molecular graphics & modelling - 1 Jan 2006

Wells Gordon A, Birkholtz Lyn-Marie, Joubert Fourie, Walter Rolf D, Louw Abraham I

Abstract excerpt

In the malaria parasite, the two main regulatory activities of polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) occur in a single bifunctional protein. The AdoMetDC domain was modeled using the human and potato X-ray crystal structures as templates. Three parasite-specific inserts and the core active site region was identified using a structure-based...

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Identifiers

PMID: 16257247
DOI: 10.1016/j.jmgm.2005.09.011

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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