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Literature summary extracted from

  • Montemayor, E.J.; Hoffman, D.W.
    The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis (2008), Biochemistry, 47, 9145-9153.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.57 expression of His-tagged SSAt in Escherichia coli strain BL21(DE3) Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.57 SSAT in complex with coenzyme A, with and without bound spermine, hanging drop vapor diffusion method at 4°C, crystals of the binary complex between SSAT and CoA are obtained in 20% PEG 8000, 80 mM sodium acetate, 15% glycerol, 2 mM spermine, 1 mM CoA, and 85 mM sodium cacodylate, pH 6.0, 0.001 ml of the protein solution is mixed with 0.01 ml of precipitant solution containing 20% PEG 8000, 50 mM NaCl, 2 mM spermine, 1 mM coenzyme A, 15% glycerol, and 100 mM bicine buffer, pH 9.0. Crystals are obtained at pH 5.0-6.5 over a broad range of precipitant and salt concentrations. Introduction of spermine results in displacement of CoA from the enzyme active site. X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.57 D93N site-directed mutagenesis, the mutation affects both substrate binding and catalysis without changing the pH dependence of the enzyme Mus musculus
2.3.1.57 E92Q site-directed mutagenesis, the mutation has a detrimental effect on both substrate binding and catalysis and shifts the optimal pH for enzyme activity further into alkaline solution conditions Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.57 acetyl-CoA + 1,3-diaminopropane Mus musculus
-
 CoA + ?
-
 ?
2.3.1.57 acetyl-CoA + diethylenetriamine Mus musculus
-
 CoA + ?
-
 ?
2.3.1.57 acetyl-CoA + N1-acetylspermine Mus musculus
-
 CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + N1-methyl-1,3-diaminopropane Mus musculus
-
 CoA + ?
-
 ?
2.3.1.57 acetyl-CoA + spermidine Mus musculus
-
 CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermine Mus musculus
-
 CoA + N1-acetylspermine
-
 ?
2.3.1.57 additional information Mus musculus SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway. No activity with putrescine, cadaverine, lysine, thialysine, amantadine, substrate specificity, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.57 Mus musculus P48026
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.57 acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine Glu92 functions as a catalytic base to drive an otherwise unfavorable deprotonation step at physiological pH. Spermine and the enzyme and form a proton wire between the side chain of Glu92 and the N1 amine of spermine, a single water molecule forms hydrogen bonds with the side chains of Glu92, Asp93, and the N4 amine of spermine, substrate binding structure, overview Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.57 acetyl-CoA + 1,3-diaminopropane
-
 Mus musculus CoA + ?
-
 ?
2.3.1.57 acetyl-CoA + diethylenetriamine
-
 Mus musculus CoA + ?
-
 ?
2.3.1.57 acetyl-CoA + N1-acetylspermine
-
 Mus musculus CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + N1-methyl-1,3-diaminopropane
-
 Mus musculus CoA + ?
-
 ?
2.3.1.57 acetyl-CoA + spermidine
-
 Mus musculus CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermine
-
 Mus musculus CoA + N1-acetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermine spermine and the enzyme and form a proton wire between the side chain of Glu92 and the N1 amine of spermine, a single water molecule forms hydrogen bonds with the side chains of Glu92, Asp93, and the N4 amine of spermine, substrate binding structure, overview Mus musculus CoA + N1-acetylspermine
-
 ?
2.3.1.57 additional information SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway. No activity with putrescine, cadaverine, lysine, thialysine, amantadine, substrate specificity, overview Mus musculus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.57 More SSAT belongs to the GCN5-related N-acetyltransferase, GNAT, superfamily of acetyltransferases Mus musculus
2.3.1.57 spermidine/spermine N1-acetyltransferase
-
 Mus musculus
2.3.1.57 SSAT
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.57 25
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.57 8.5
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.57 acetyl-CoA
-
 Mus musculus

General Information

EC Number General Information Comment Organism
2.3.1.57 metabolism SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway Mus musculus