Literature summary extracted from

  • Hung, M.N.; Rangarajan, E.; Munger, C.; Nadeau, G.; Sulea, T.; Matte, A.
    Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis (2006), J. Bacteriol., 188, 5606-5617.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.210 gene wecD, expression of N-terminal fusion protein with a noncleavable His6-tag in Escherichia coli strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.210 purified recombinant N-terminally His6-tagged WecD free and in complex with acetyl-CoA, hanging drop vapour diffusion method, mixing of 0.001 ml of 7.1 mg/ml protein in a 20 mM Tris-Cl, pH 8.0, 450 mM NaCl, and 5 mM DTT, with 0.001 ml reservoir solution aontaining 100 mM Na-acetate, pH 4.5, 10 mM ZnSO4, 20°C, 1 day, X-ray diffraction structure determination and analysis at 1.66-1.95 A resolution Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.210 acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose Escherichia coli
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CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
-
?
2.3.1.210 acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose Escherichia coli CFT073
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CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.210 Escherichia coli Q8FBQ3 gene wecD
-
2.3.1.210 Escherichia coli CFT073 Q8FBQ3 gene wecD
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.210 recombinant N-terminally His6-tagged WecD from Escherichia coli strain BL21(DE3) Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.210 acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
-
Escherichia coli CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
-
?
2.3.1.210 acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose acetyl-CoA binding site structure, overview Escherichia coli CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
-
?
2.3.1.210 acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
-
Escherichia coli CFT073 CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
-
?
2.3.1.210 acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose acetyl-CoA binding site structure, overview Escherichia coli CFT073 CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.210 dimer WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, gel filtration and dynamic light scattering, three-dimensional structure comparison, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.210 TDP-fucosamine acetyltransferase
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Escherichia coli
2.3.1.210 WecD
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Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.210 acetyl-CoA
-
Escherichia coli

General Information

EC Number General Information Comment Organism
2.3.1.210 physiological function the enzyme is involved in biosynthesis of enterobacterial common antigen, ECA, a polysaccharide found on the outer membrane of virtually all Gram-negative enteric bacteria, that consists of three sugars, N-acetyl-D-glucosamine, N-acetyl-D-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-D-galactose, organized into trisaccharide repeating units having the sequence ->3)-alpha-D-Fuc4NAc-(1->4)-beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-(1-> Escherichia coli
2.3.1.210 evolution WecD is a GNAT family member. The GNAT N-acetyltransferase fold is common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars Escherichia coli
2.3.1.210 additional information usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom Escherichia coli