Ontology highlight
ABSTRACT:
SUBMITTER: Bale S
PROVIDER: S-EPMC2815669 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
Bale Shridhar S Baba Kavita K McCloskey Diane E DE Pegg Anthony E AE Ealick Steven E SE
Acta crystallographica. Section D, Biological crystallography 20100122 Pt 2
The polyamines putrescine, spermidine and spermine are ubiquitous aliphatic cations and are essential for cellular growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. The crystal structures of AdoMetDC from humans and plants and of the AdoMetDC proenzyme from Thermotoga maritima have been obtained previously. Here, the crystal structures of activated T. maritima AdoMetDC (TmAdoMetDC) and of its c ...[more]