N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase
Abstract
The specificity of N-acetylspermidine deacetylase from rat liver for the two naturally occurring forms of monoacetylated spermidine was studied. N8-Acetylspermidine is the preferred substrate in vitro for this enzyme, and, in fact, N1-acetylspermidine did not undergo deacetylation under the conditions used in this study. Thus N8-acetylspermidine is the more appropriate substrate for assaying N-acetylspermidine deacetylase activity.
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Substrate specificity trends observed for zHDAC10 and hHDAC10 matched those of previously reported mammalian N8-acetylspermidine deacetylase activity.
“Substrate specificity trends observed for zHDAC10 and hHDAC10 matched those of the previously reported mammalian N8-acetylspermidine deacetylase activity91011.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [10]
These properties match the tissue distribution, subcellular localization and inhibitor sensitivity of mammalian PDAC.
“These properties match the tissue distribution, subcellular localization and inhibitor sensitivity of mammalian PDAC8910111213.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [10]
PDAC substrate specificity is very strict; it does not deacetylate cytosolic N1-acetylspermidine or N1-acetylspermine.
“The substrate specificity of PDAC is very strict, as it does not deacetylate cytosolic N1-acetylspermidine or N1-acetylspermine10.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [10]
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- Authors
- Marchant, P., Manneh, V. A., & Blankenship, J.
- Affiliations
- University of the Pacific (US)
- Corresponding author
- Blankenship, Jim
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 1986-04
- Volume
- 881
- Issue
- 2
- Pages
- 297-299
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2030105645
- Cited by
- 13
- References
- 10
- Citations by year
- 2025: 2 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 1 · 2015: 1 · 2013: 1
- FWCI
- 0.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- N1-acetylspermidine, N8-acetylspermidine, enzyme substrate specificity, polyamine metabolism, rat liver
- MeSH terms
- Amidohydrolases, Animals, Chromatography, High Pressure Liquid, Liver, Male, Rats, Inbred Strains, Spermidine, Structure-Activity Relationship, Substrate Specificity, Rats
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