Abstract
d-Amino acid N-acetyltransferase is a unique enzyme of Saccharomyces cerevisiae acting specifically on d-amino acids. The enzyme was found to be encoded by HPA3, a putative histone/protein acetyltransferase gene, and we purified its gene product, Hpa3p, from recombinant Escherichia coli cells. Hpa3p shares 49% sequence identity and 81% sequence similarity with a histone acetyltransferase, Hpa2p, of S. cerevisiae. Hpa3p acts on a wide range of d-amino acids but shows extremely low activity toward histone. However, Hpa2p does not act on any of the free amino acids except l-lysine and d-lysine. Kinetic analyses suggest that Hpa3p catalyzes the N-acetylation of d-amino acids through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated.
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Acknowledgements
This work was supported in part by Grants-in-Aid for Scientific Research (14560064 to T.Y., 09460049 to N.E.) and a Grant-in-Aid for Scientific Research on Priority Areas (B) (13125203 to N.E.) from the Ministry of Education, Culture, Sports, Science, and Technology; and by the Pioneering Research Project in Biotechnology of the Ministry of Agriculture, Forestry, and Fisheries (T.Y.).
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Yow, GY., Uo, T., Yoshimura, T. et al. d-Amino acid-N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free d-amino acids. Arch Microbiol 182, 396–403 (2004). https://doi.org/10.1007/s00203-004-0724-y
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DOI: https://doi.org/10.1007/s00203-004-0724-y