Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme.
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Patel CN, Adcock RS, Sell KG, Oliveira MA
Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme.
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2396-8. Epub 2004 Nov 26.
- PubMed ID
- 15583399 [ View in PubMed]
- Abstract
Arginine decarboxylase (ADC) is a 70 kDa pyridoxal-5'-phosphate (PLP) dependent enzyme that controls an alternative step in the biosynthesis of polyamines in some bacteria and plants. Crystals of ADC were flash-cooled and diffracted to 3.0 A resolution using a synchrotron-radiation source. Crystals of ADC are monoclinic, with four monomers in the asymmetric unit. Light-scattering data reveals that the enzyme forms dimers in solution. The rotation function suggests the presence of two dimers in the asymmetric unit. Heavy-atom searches have identified PCMBS as forming a mercury derivative.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Pyridoxal phosphate Arginine decarboxylase Protein Humans UnknownCofactorDetails