Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.57 extracted from

  • Filippova, E.V.; Kuhn, M.L.; Osipiuk, J.; Kiryukhina, O.; Joachimiak, A.; Ballicora, M.A.; Anderson, W.F.
    A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed by its dodecameric structure (2015), J. Mol. Biol., 427, 1316-1334.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in ligand-free form or complxed with spermine or spermidine, and/or acetyl-CoA, X-ray diffraction structure determination and analysis at 1.85-2.83 A resolution, the enzyme occurs in open and closed conformations Vibrio cholerae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information allosteric substrate binding, polyamine allosteric site structure, complex enzyme behavior, it exhibits sigmoidal curves and substrate inhibition, bireactant random steady-state kinetic mechanism, detailed non-linear regression kinetic analysis, overview Vibrio cholerae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
270000
-
polyamine-bound enzyme, gel filtration and small-angle X-ray scattering analysis Vibrio cholerae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3 acetyl-CoA + 2 spermine Vibrio cholerae
-
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
?
3 acetyl-CoA + 2 spermine Vibrio cholerae N16961
-
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
?
3 acetyl-CoA + spermidine Vibrio cholerae
-
3 CoA + N1,N4,N8-triacetylspermidine
-
?
3 acetyl-CoA + spermidine Vibrio cholerae N16961
-
3 CoA + N1,N4,N8-triacetylspermidine
-
?

Organism

Organism UniProt Comment Textmining
Vibrio cholerae Q9KL03 serotype O1, gene speG or VCA0947
-
Vibrio cholerae N16961 Q9KL03 serotype O1, gene speG or VCA0947
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 acetyl-CoA + 2 spermine
-
Vibrio cholerae 3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
?
3 acetyl-CoA + 2 spermine
-
Vibrio cholerae N16961 3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
?
3 acetyl-CoA + spermidine
-
Vibrio cholerae 3 CoA + N1,N4,N8-triacetylspermidine
-
?
3 acetyl-CoA + spermidine
-
Vibrio cholerae N16961 3 CoA + N1,N4,N8-triacetylspermidine
-
?
additional information spermine and spermidine are the preferential substrates, no activity with cadaverine. Conformational differences between enzyme SpeG ligand-free and liganded structures, allosteric substrate binding site structure, overview Vibrio cholerae ?
-
?
additional information spermine and spermidine are the preferential substrates, no activity with cadaverine. Conformational differences between enzyme SpeG ligand-free and liganded structures, allosteric substrate binding site structure, overview Vibrio cholerae N16961 ?
-
?

Subunits

Subunits Comment Organism
dodecamer three-dimensional structure in several ligand-free and ligand-bound structures, overview. The enzyme monomer has a mixed alpha/beta architecture Vibrio cholerae
More the enzyme occurs in open and closed conformations Vibrio cholerae

Synonyms

Synonyms Comment Organism
SpeG
-
Vibrio cholerae
spermidine N-acetyltransferase
-
Vibrio cholerae
VCA0947
-
Vibrio cholerae

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA cofactor-binding site structure, overview. The beta-bulge formed by the beta4 and beta5 parallel strands is where the pantotheine moiety of AcCoA is located in the active site, characteristic for members of the GNAT superfamily. The pantothenate moiety forms hydrogen bonds with two conserved residues Ile87 and Ile89 Vibrio cholerae

General Information

General Information Comment Organism
evolution the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily Vibrio cholerae
metabolism the enzyme is involved in regulation of polyamine levels in bacteria during pathogenesis Vibrio cholerae
additional information enzyme SpeG forms dodecamers in solution and in crystals, three-dimensional structure in several ligand-free and liganded structures, the enzyme occurs in open and closed conformations, overview. Conserved residue Tyr134 is proposed to function as the general acid to protonate the thiolate anion of CoA after transfer of the acetyl group to the substrate Vibrio cholerae
physiological function the enzyme catalyzes the initial step in the degradation of polyamines and is a critical enzyme for determining the polyamine concentrations in bacteria Vibrio cholerae