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Literature summary for 2.3.1.202 extracted from

  • Song, W.S.; Nam, M.S.; Namgung, B.; Yoon, S.I.
    Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation (2015), Biochem. Biophys. Res. Commun., 458, 843-848.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
PseH alone and in complex with AcCoA, to 1.95 A resolution. PseH folds into a single-domain structure of a central beta-sheet decorated by four alpha-helices with two continuously connected grooves. A deep groove accommodates the AcCoA molecule. The acetyl end of AcCoA points toward an open space in a neighboring shallow groove, which is occupied by extra electron density that potentially serves as a pseudosubstrate. PseH may utilize a catalytic mechanism of acetylation different from other glycosylation-associated acetyltransferases Campylobacter jejuni

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni A0A0J9X276 subsp. jejuni
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Campylobacter jejuni PT14 A0A0J9X276 subsp. jejuni
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
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Campylobacter jejuni CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
-
?
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
-
Campylobacter jejuni PT14 CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
-
?

Synonyms

Synonyms Comment Organism
A911_06385
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Campylobacter jejuni