Crystallization of a mammalian ornithine decarboxylase
Crystals of truncated (Δ425‐461) pyridoxal‐5′‐phosphate (PLP)‐dependent mouse ornithine decarboxylase (mOrnDC′) have been obtained that diffract to 2.2 Å resolution (P21212, a = 119.5 Å, b = 74.3 Å, c = 46.1 Å). OrnDC produces putrescine, which is the precursor for the synthesis of polyamines in euk...
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Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1996-02, Vol.24 (2), p.266-268 |
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Hauptverfasser: | , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Crystals of truncated (Δ425‐461) pyridoxal‐5′‐phosphate (PLP)‐dependent mouse ornithine decarboxylase (mOrnDC′) have been obtained that diffract to 2.2 Å resolution (P21212, a = 119.5 Å, b = 74.3 Å, c = 46.1 Å). 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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ISSN: | 0887-3585 1097-0134 |
DOI: | 10.1002/(SICI)1097-0134(199602)24:2<266::AID-PROT15>3.0.CO;2-L |