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Literature summary for 2.3.1.136 extracted from

  • Schulz, E.C.; Bergfeld, A.K.; Ficner, R.; Muehlenhoff, M.
    Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO (2011), PLoS ONE, 6, e17403.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.136

Cloned(Commentary)

Cloned (Comment) Organism
expression of the engineered C-terminally His6-tagged NeuO mutant in Escherichia coli strain BL21 gold (DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified engineered apo-NeuO, a protein variant with four N-terminal RLKTQDS heptads, sitting drop vapour diffusion, 6.3 mg/ml protein in 10 mM Tris-HCl pH 7.5 and 150 mM NaCl, mixed with precipitant solution containing 0.1 M Tris, pH 7.2, 0.45 M glycine, 0.2 M NH4NO3, 7% PEG 4000 w/v, 1 week, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information engineering of a neuO gene that allows phase-stable expression of NeuO with four N-terminal heptads Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant engineered C-terminally His6-tagged NeuO mutant from Escherichia coli strain BL21 gold (DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9 identification of highly conserved active site residues and catalytic mechanism, residues His147, Trp171, His119, and Trp143 are important, overview Escherichia coli
a

Subunits

Subunits Comment Organism
homotrimer the enzyme belongs to the left-handed beta-helix family of acyltransferases and is characterized by an unusual funnel-shaped outline. NeuO displays an unusual quaternary structure arrangement presumably is an adaptation to accommodate the exceptionally long polySia acceptor Escherichia coli
More domain structures, and three-dimensional structure of NeuO, modelling, overview Escherichia coli

Synonyms

Synonyms Comment Organism
NeuO
-
 Escherichia coli
polySia specific O-acetyltransferase
-
 Escherichia coli
polysialic acid specific O-acetyltransferase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Escherichia coli

General Information

General Information Comment Organism
evolution the homotrimeric enzyme belongs to the left-handed beta-helix family of acyltransferases and is characterized by an unusual funnel-shaped outline Escherichia coli
additional information the enzymatic activity linearly increases with the length of the N-terminal poly-psi-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad, the poly-psi-domain is not resolved in the crystal structure Escherichia coli
physiological function K1 capsule O-acetylation undergoes highfrequency phase-variation involving also the polysialic acid specific O-acetyltransferase Escherichia coli