2.3.1.136: polysialic-acid O-acetyltransferase

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For detailed information about polysialic-acid O-acetyltransferase, go to the full flat file.

Reaction

Synonyms

lecithin:retinol acyltransferase, LRAT, NeuO, OatC, OatWY, polySia specific O-acetyltransferase, polysialic acid O-acetyltransferase, polysialic acid O-AcTase, polysialic acid specific O-acetyltransferase, polysialic acid-specific O-acetyltransferase, polysialic-acid O-acetyltransferase

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.136 polysialic-acid O-acetyltransferase

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Results	in table
32	AA Sequence
1	CAS Registry Number
5	Cloned(Commentary)
1	Cofactor
2	Crystallization (Commentary)
3	General Information
3	General Stability
1	Inhibitors
2	kcat/KM [mM/s]
12	KM Value [mM]
1	Localization
1	Metals/Ions
4	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
17	Organism
3	PDB ID
5	pH Optimum
28	Protein Variants
5	Purification (Commentary)
2	Reaction
1	Reaction Type
10	Reference
1	Specific Activity [micromol/min/mg]
1	Storage Stability
24	Substrates and Products (Substrate)
7	Subunits
17	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Stability [°C]
11	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.136 - polysialic-acid O-acetyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

-

720818

OatWY is crystalised with bound substrate acetyl-CoA and its analogs (CoA, S-(2-oxopropyl)-CoA) using the hanging drop vapor diffusion technique. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. A significant movement of Tyr-171 blocks the active site of the enzyme in its native form

Neisseria meningitidis

O33391

704530