Purification and characterization of ornithine acetyltransferase from saccharomyces-erevisiae

Liu, Yongshu, Van Heeswijck, Robyn, Høj, Peter and Hoogenraad, Nicholas (1995) Purification and characterization of ornithine acetyltransferase from saccharomyces-erevisiae. European Journal of Biochemistry, 228 2: 291-296. doi:10.1111/j.1432-1033.1995.0291n.x

Author Liu, Yongshu
Van Heeswijck, Robyn
Høj, Peter
Hoogenraad, Nicholas
Title Purification and characterization of ornithine acetyltransferase from saccharomyces-erevisiae
Journal name European Journal of Biochemistry   Check publisher's open access policy
ISSN 0014-2956
Publication date 1995-03
Sub-type Article (original research)
DOI 10.1111/j.1432-1033.1995.0291n.x
Volume 228
Issue 2
Start page 291
End page 296
Total pages 6
Place of publication Chichester, West Sussex, United Kingdom
Publisher Wiley-Blackwell Publishing
Language eng
Abstract Ornithine acetyltransferase has been purified 4000-fold to homogeneity from Saccharomyces cerevisiae. The enzyme catalyses the freely reversible interchange of an acetyl group between N-acetylornithine and glutamate and has a specific activity of 22 μmol · min−1· mg−1 at 37°C and pH 7.5. The Km values were determined for the substrates of the forward and reverse directions to be 1.0 mM for N-acetylornithine, 7.2 mM for glutamate, 1.5 mM for ornithine and 17.1 mM for N-acetylglutamate. The enzyme was localised to the mitochondrial matrix and was found to be a 57-kDa heterodimer consisting of subunits of 31 kDa and 26 kDa. Antibodies raised against the small subunit immunoprecipitated a single in vitro translation product of approximately 57 kDa suggesting that the subunits are processed from a single precursor protein. This is supported by N-terminal sequence analysis which shows that the 26-kDa subunit exhibits 40% sequence identity (8 out of 20) with the N-terminus of ornithine acetyltransferase from Neisseria gonorrhoeae whereas the N-terminus of the 31-kDa subunit exhibits 45% identity (9 out of 20) with a sequence located in the middle of the 60-kDa N. gonorrhoeae enzyme. The N-terminal sequence of the small subunit has the potential to form an amphiphilic helix, further suggesting that the precursor protein with the small subunit at its N-terminus could be targeted to mitochondria and processed into two subunits.
Keyword Arginine
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Office of the Vice-Chancellor
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