Download MendeleyThe crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold.
Ekstrom, J.L., Mathews, I.I., Stanley, B.A., Pegg, A.E., Ealick, S.E.(1999) Structure 7: 583-595
- PubMed: 10378277
- DOI: https://doi.org/10.1016/s0969-2126(99)80074-4
- Primary Citation of Related Structures:
1JEN - PubMed Abstract:
S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine synthetic pathway, and a well-studied drug target. The AdoMetDC decarboxylation reaction depends upon a pyruvoyl cofactor generated via an intramolecular proenzyme self-cleavage reaction. Both the proenzyme-processing and substrate-decarboxylation reactions are allosterically enhanced by putrescine. Structural elucidation of this enzyme is necessary to fully interpret the existing mutational and inhibitor-binding data, and to suggest further experimental studies.
Organizational Affiliation:
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
