Ornithine aminotransferase (OAT): a target for anticancer drugs

Details Ornithine aminotransferase (OAT): a target for anticancer drugs Ornithine aminotransferase (OAT): a target for anticancer drugs

2006-06-12

2009-11-24

Pak, Yong D (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Transferase other than ribonuclease

C435S004000, C435S007100, C435S015000, C435S069100, C435S071100, C435S440000, C514S789000, C424S094500

Reexamination Certificate

active

07622289

ABSTRACT:
Ornithine δ-aminotransferase (OAT) facilitates microtubule assembly in addition to its aminotransferase activity in mitochondria. An N-terminal proteolysis of the first 17 amino acids of OAT block its transport to the mitochondria. The resultant truncated protein (OATC) forms specific complexes with mitotic spindle promoting proteins such as Eg5 and takes on a Ran-dependent spindle-assembly activity. Methods and compositions for inhibiting mitotic spindle assembly in a cell by specifically inhibiting OAT, and methods for screening for inhibitors of (1) the spindle-assembly function of OAT, (2) the protease that N-truncates OAT, (3) the OAT/RanGTP association and (4) the OAT/Eg5 association are disclosed.

REFERENCES:
Branden et al. Introduction to Protein Structure, Garland Publishing Inc., New York, p. 247, 1991.
Williams et al. Therapeutic anticancer efficacy of a synthetic diazonamide analog in the absence of overt toxicity. Proc Natl Acad Sci U S A. Feb. 13, 2007;104(7):2074-9. Epub Feb. 7, 2007.
Wang et al. Diazonamide toxins reveal an unexpected function for ornithine delta-amino transferase in mitotic cell division. Proc Natl Acad Sci U S A. Feb. 13, 2007;104(7):2068-73. Epub Feb. 7, 2007.

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