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Literature summary for 2.3.1.201 extracted from

  • Thoden, J.B.; Holden, H.M.
    Molecular structure of WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid (2010), Biochemistry, 49, 4644-4653.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta(DE3) cells Bordetella petrii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method. The enzyme complexed with acetyl-CoA and UDP is crystallized at pH 8.0 in the presence of 100 mM HEPPS, 16-20% (w/v) poly(ethylene glycol) 3400 and 210 mM tetramethylammonium chloride. The enzyme bound to CoA and UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate is crystallized using 17% (w/v) poly(ethylene glycol) 3400, 300 mM NaCl, 100 mM HEPPS (pH 8.0), 210 mM tetramethylammonium chloride Bordetella petrii

Organism

Organism UniProt Comment Textmining
Bordetella petrii A9IH93
-
-
Bordetella petrii ATCC BAA-461 A9IH93
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Bordetella petrii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
Bordetella petrii CoA + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate
-
?
acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
Bordetella petrii ATCC BAA-461 CoA + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate
-
?

Subunits

Subunits Comment Organism
trimer x-ray crystallography Bordetella petrii

Synonyms

Synonyms Comment Organism
WlbB
-
Bordetella petrii