title: 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.
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D008099:Liver / Q000201:enzymology; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013095:Spermidine / Q000031:analogs & derivatives* / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: C017988:N(1)-acetylspermidine; D000581:Amidohydrolases; C018738:acetylspermidine deacetylase; D013095:Spermidine