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Literature summary for 3.5.1.48 extracted from

  • Libby, P.R.
    Properties of an acetylspermidine deacetylase from rat liver (1978), Arch. Biochem. Biophys., 188, 360-363.
    View publication on PubMed
Search for more literature for 3.5.1.48

Inhibitors

Inhibitors Comment Organism Structure
1,4-diaminobutane competitive inhibition, Ki: 0.25 mM Rattus sp.
spermidine competitive inhibition, Ki: 0.055 mM Rattus sp.
spermine competitive inhibition, Ki: 0.036 mM Rattus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 N1-acetylspermidine
-
 Rattus sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus sp. 5829
-

Organism

Organism UniProt Comment Textmining
Rattus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Rattus sp.

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.54
-
-
 Rattus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N1-acetylspermidine + H2O
-
 Rattus sp. acetate + spermidine
-
 ?
N1-acetylspermine + H2O
-
 Rattus sp. spermine + acetate
-
 ?
N8-acetylspermidine + H2O
-
 Rattus sp. acetate + spermidine
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 stable up to 30 min Rattus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10.4
-
-
 Rattus sp.