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Pure and Applied Chemistry

The Scientific Journal of IUPAC

Ed. by Burrows, Hugh / Weir, Ron / Stohner, Jürgen

12 Issues per year


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Online
ISSN
1365-3075
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Volume 77, Issue 1 (Jan 2005)

Issues

Acetoxy drug: protein transacetylase: A novel enzyme-mediating protein acetylation by polyphenolic peracetates

Hanumantharao G. Raj
  • Corresponding author
  • Biochemistry Department, V. P. Chest Institute, University of Delhi, Delhi 110 007, India
/ Brajendra K. Singh
  • Corresponding author
  • Bioorganic Laboratory, Department of Chemistry, University of Delhi, Delhi 110 007, India
/ Ekta Kohli
  • Corresponding author
  • Biochemistry Department, V. P. Chest Institute, University of Delhi, Delhi 110 007, India
/ Bilikere S. Dwarkanath
  • Corresponding author
  • Institute of Nuclear Medicine and Allied Sciences, Lucknow Road, Delhi 110 054, India
/ Subhash C. Jain
  • Corresponding author
  • Bioorganic Laboratory, Department of Chemistry, University of Delhi, Delhi 110 007, India
/ Ramesh C. Rastogi
  • Corresponding author
  • Bioorganic Laboratory, Department of Chemistry, University of Delhi, Delhi 110 007, India
/ Ajit Kumar
  • Corresponding author
  • Biochemistry Department, V. P. Chest Institute, University of Delhi, Delhi 110 007, India
/ J. S. Adhikari
  • Corresponding author
  • Institute of Nuclear Medicine and Allied Sciences, Lucknow Road, Delhi 110 054, India
/ Arthur C. Watterson
  • Corresponding author
  • INSET, Department of Chemistry, University of Massachusetts, Lowell, MA 01854, USA
/ Carl E. Olsen
  • Corresponding author
  • Department of Chemistry, Royal Veterinary and Agricultural University, DK-1871 Frederiksburg C, Copenhagen, Denmark
/ Virinder S. Parmar
  • Corresponding author
  • Bioorganic Laboratory, Department of Chemistry, University of Delhi, Delhi 110 007, India
Published Online: 2009-01-01 | DOI: https://doi.org/10.1351/pac200577010245

The acetylation of proteins in biological systems is largely catalyzed by specific acetyl transferases utilizing acetyl CoA as the acetyl donor. The enzymatic acetylation of proteins independent of acetyl CoA was unknown until we discovered a unique membrane-bound enzyme in mammalian cells catalyzing the transfer of acetyl groups from polyphenolic peracetates (PAs) to certain enzyme proteins, resulting in the modulation of their catalytic activities. Since for the enzyme, acetyl derivatives of several classes of polyphenols such as coumarins, flavones, chromones, and xanthones were found to be acetyl donors, the enzyme was termed as acetoxy drug: protein transacetylase (TAase). TAase was found to be ubiquitously present in tissues of several animal species and a variety of animal cells. Liver microsomal cytochrome P-450 (CYP), NADPH-cytochrome c reductase and cytosolic glutathione S-transferase (GST) were found to be the targets for TAase-catalyzed acetylation by the model acetoxy drug 7,8-diacetoxy-4-methylcoumarin (DAMC). Accordingly, the catalytic activities of CYP-linked, mixed function oxidases (MFOs) and GST were irreversibly inhibited while the reductase was remarkably activated. In this report, we have reviewed the details concerning purification and characterization of TAase and the protein acetylation by DAMC. Quantitative structure–activity relationship (QSAR) studies concerning the specificities of various PAs to liver microsomal TAase and TAase-related biological effects have also been reviewed.

Keywords: acetoxy drug; enzyme-mediating protein acetylation; glutathione S-transferase; nitric oxide synthase; polyphenolic peracetates; protein transacetylase

Conference

International Symposium on the Chemistry of Natural Products and the 4th International Congress on Biodiversity, International Conference on Biodiversity, International Symposium on the Chemistry of Natural Products, ICOB, ISCNP, Biodiversity, Natural Products, 24th, Delhi, India, 2004-01-26–2004-01-31

About the article

Published Online: 2009-01-01

Published in Print: 2005-01-01


Citation Information: Pure and Applied Chemistry, ISSN (Online) 1365-3075, ISSN (Print) 0033-4545, DOI: https://doi.org/10.1351/pac200577010245. Export Citation

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