Rat liver nuclear N-acetyltransferases: Separation of two enzymes with both histone and spermidine acetyltransferase activity
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Spermidine is acetylated at N8 by an N-acetyltransferase in the nucleus and then exported to the cytosol, where it is deacetylated by a metal-dependent N8-acetylspermidine deacetylase (PDAC).
“Spermidine is acetylated at the N8 position by an N-acetyltransferase in the cell nucleus7 and then exported to the cytosol, where it is deacetylated by a metal-dependent N8-acetylspermidine deacetylase, also known as polyamine deacetylase (PDAC)89.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [7]
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- Authors
- Libby, P. R.
- Affiliations
- Roswell Park Comprehensive Cancer Center (US)
- Corresponding author
- Libby, Paul R.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1980-08
- Volume
- 203
- Issue
- 1
- Pages
- 384-389
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W1978504375
- Cited by
- 67
- References
- 23
- Citations by year
- 2025: 1 · 2024: 1 · 2022: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 1
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- histone acetyltransferase, N-acetyltransferase, histone H3 acetylation, enzyme purification, Michaelis constant, acetyl-CoA
- MeSH terms
- Acetylation, Acetyltransferases, Animals, Cell Nucleus, DNA, Female, Histones, Kinetics, Liver, Spermine, Substrate Specificity, Rats
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