EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.57 | purified enzyme, dodecameric structure in a ligand-free form in three different conformational states, open, intermediate and closed, sitting drop vapor diffusion method, for open state crystals: mixing of 400 nl of 10 mg/ml protein in 100 mM sodium chloride, 10 mM HEPES, pH 7.5, with 400 nl of reservoir solution containing 8% isopropanol and 0.1 M Tris-HCl, pH 8.5, for closed state crystals: mixing of 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, with 0.001 ml of reservoir solution that contains 0.05 M ammonium sulfate, 0.1 M tri-sodium citrate and 15% polyethylene glycol 8000, and for intermediate state crystals: 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, and 0.001 ml of reservoir solution containing 0.01 M calcium chloride, 20% methanol, and 0.1 M Tris-HCl, pH 8.5, 19°C, X-ray diffraction structure determination and analysis at 2.38-2.88 A reolution, molecular replacement. All structures are crystallized in C2 space group symmetry and contain six monomers in the asymmetric unit cell. Two hexamers related by crystallographic 2fold symmetry form the SpeG dodecamer. The open and intermediate states have a unique open dodecameric ring | Vibrio cholerae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.57 | additional information | - |
additional information | allosteric substrate binding, bireactant random steady-state kinetic mechanism | Vibrio cholerae |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.57 | 220000 | 230000 | ligand-free enzyme, gel filtration and small-angle X-ray scattering analysis | Vibrio cholerae |
2.3.1.57 | 250000 | - |
polyamine-bound enzyme, gel filtration and small-angle X-ray scattering analysis | Vibrio cholerae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.57 | 3 acetyl-CoA + 2 spermine | Vibrio cholerae | - |
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine | - |
? | |
2.3.1.57 | 3 acetyl-CoA + 2 spermine | Vibrio cholerae N16961 | - |
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine | - |
? | |
2.3.1.57 | 3 acetyl-CoA + spermidine | Vibrio cholerae | - |
3 CoA + N1,N4,N8-triacetylspermidine | - |
? | |
2.3.1.57 | 3 acetyl-CoA + spermidine | Vibrio cholerae N16961 | - |
3 CoA + N1,N4,N8-triacetylspermidine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.57 | Vibrio cholerae | Q9KL03 | serotype O1, gene speG | - |
2.3.1.57 | Vibrio cholerae N16961 | Q9KL03 | serotype O1, gene speG | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.57 | 3 acetyl-CoA + 2 spermine | - |
Vibrio cholerae | 3 CoA + N1-acetylspermine + N1,N12-diacetylspermine | - |
? | |
2.3.1.57 | 3 acetyl-CoA + 2 spermine | - |
Vibrio cholerae N16961 | 3 CoA + N1-acetylspermine + N1,N12-diacetylspermine | - |
? | |
2.3.1.57 | 3 acetyl-CoA + spermidine | - |
Vibrio cholerae | 3 CoA + N1,N4,N8-triacetylspermidine | - |
? | |
2.3.1.57 | 3 acetyl-CoA + spermidine | - |
Vibrio cholerae N16961 | 3 CoA + N1,N4,N8-triacetylspermidine | - |
? | |
2.3.1.57 | additional information | substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview | Vibrio cholerae | ? | - |
? | |
2.3.1.57 | additional information | substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview | Vibrio cholerae N16961 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.57 | dodecamer | substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview. The enzyme possesses unique open dodecameric state exists in solution | Vibrio cholerae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.57 | SpeG | - |
Vibrio cholerae |
2.3.1.57 | spermidine N-acetyltransferase | - |
Vibrio cholerae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.57 | acetyl-CoA | - |
Vibrio cholerae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.57 | evolution | the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily. The open and intermediate states of ligand-free enzyme have a unique open dodecameric ring. The SpeG dodecamer is asymmetric except for the one 2fold axis and is unlike any known dodecameric structure. The SpeG dodecamer is conserved in different bacterial species, structure analysis and comparisons, overview | Vibrio cholerae |
2.3.1.57 | physiological function | enzyme SpeG has an allosteric polyamine-binding site and acetylating polyamines regulate their intracellular concentrations | Vibrio cholerae |