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Literature summary extracted from

  • Filippova, E.V.; Weigand, S.; Osipiuk, J.; Kiryukhina, O.; Joachimiak, A.; Anderson, W.F.
    Substrate-induced allosteric change in the quaternary structure of the spermidine N-acetyltransferase SpeG (2015), J. Mol. Biol., 427, 3538-3553.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-

Substrates and Products (Substrate)

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 ?
-
?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.3.1.57 SpeG
-
Vibrio cholerae
2.3.1.57 spermidine N-acetyltransferase
-
Vibrio cholerae

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.57 acetyl-CoA
-
Vibrio cholerae

General Information

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