EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.57 | expression of His-tagged SSAt in Escherichia coli strain BL21(DE3) | Mus musculus |
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 |
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 |
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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.57 | Mus musculus | P48026 | - |
- |
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 |
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 | ? | - |
? |
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 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.57 | 25 | - |
assay at | Mus musculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.57 | 8.5 | - |
assay at | Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.57 | acetyl-CoA | - |
Mus musculus |
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 |