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Crystallization of a mammalian ornithine decarboxylase
A Kern1, M A Oliveira, N L Chang
1Department of Chemistry and Biochemistry, University of Texas at Austin 78712, USA.
Proteins
|February 1, 1996
Abstract:
Crystals of truncated (delta425-461) pyridoxal-5'-phosphate (PLP)-dependent mouse ornithine decarboxylase (mOrnDC') have been obtained that diffract to 2.2 angstroms resolution (P2(1)2(1)2, a = 119.5 angstroms, b = 74.3 angstroms, c = 46.1 angstroms). OrnDC produces putrescine, which is the precursor for the synthesis of polyamines in eukaryotes. Regulation of activity and understanding of the mechanism of action of this enzyme may aid in the development of compounds against cancer. mOrnDC is a member of group IV PLP-dependent decarboxylases, for which there are no known representative structures.