Acetylspermidine deacetylase

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In enzymology, an acetylspermidine deacetylase (EC 3.5.1.48) is an enzyme that catalyzes the chemical reaction

N₈-acetylspermidine + H₂O $\rightleftharpoons$ acetate + spermidine

Thus, the two substrates of this enzyme are N8-acetylspermidine and H₂O, whereas its two products are acetate and spermidine.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N8-acetylspermidine amidohydrolase. Other names in common use include N8-monoacetylspermidine deacetylase, N8-acetylspermidine deacetylase, N-acetylspermidine deacetylase, N1-acetylspermidine amidohydrolase (incorrect), and 8-N-acetylspermidine amidohydrolase.

[edit] References

IUBMB entry for 3.5.1.48
BRENDA references for 3.5.1.48 (Recommended.)
PubMed references for 3.5.1.48
PubMed Central references for 3.5.1.48
Google Scholar references for 3.5.1.48
Libby PR (1978). "Properties of an acetylspermidine deacetylase from rat liver". Arch. Biochem. Biophys. 188: 360–3. doi:10.1016/S0003-9861(78)80020-4. PMID 28089.
Blankenship J (1978). "Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue". Arch. Biochem. Biophys. 189: 20–7. doi:10.1016/0003-9861(78)90109-1. PMID 708044.
Marchant P, Manneh VA, Blankenship J (1986). "N1-acetylspermidine is not a substrate for N-acetylspermidine deacetylase". Biochim. Biophys. Acta. 881: 297–9. PMID 3955076.