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PMID: 3955076 Published · ppublish English Journal Article

N1-acetylspermidine is not a substrate for N-acetylspermidine deacetylase.

Biochimica et biophysica acta ·Vol. 881 ·No. 2 ·1986-04-11 ·Pages 297-9

Marchant P, Manneh VA, Blankenship J

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.

MeSH Terms
Amidohydrolases/metabolism Animals Chromatography, High Pressure Liquid Liver/enzymology Male Rats Rats, Inbred Strains Spermidine/analogs & derivatives,metabolism Structure-Activity Relationship Substrate Specificity
Chemicals
N(1)-acetylspermidine Amidohydrolases acetylspermidine deacetylase Spermidine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Marchant P
Manneh V A
Blankenship J
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1986-04-11
Pages
297-9
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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