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Crystallization of a mammalian ornithine decarboxylase

✍ Scribed by Kern, Andrew; Oliveira, Marcos A.; Chang, Ning-Leh; Ernst, Stephen R.; Carroll, Donald W.; Momany, Cory; Minard, Karyl; Coffino, Philip; Hackert, Marvin L.

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
293 KB
Volume
24
Category
Article
ISSN
0887-3585

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✦ Synopsis

Crystals of truncated (A425-461) pyridoxal-5'-phosphate (PLP)-dependent mouse ornithine decarboxylase (mOrnDC') have been obtained that diffract to 2.2 resolution (P2,2,2, a = 119.5 A, b = 74.3 A, c = 46.1 A). 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.

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