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Literature summary extracted from

  • Ud-Din, A.I.; Liu, Y.C.; Roujeinikova, A.
    Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N-acetyltransferase PseH: implications for substrate specificity and catalysis (2015), PLoS ONE, 10, e0115634.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.202 in complex with cofactor acetyl-CoA, to 2.3 A resolution. PseH is a homodimer in the crystal, each subunit of which has a central twisted beta-sheet flanked by five alpha-helices. The cofactor-binding site is located between the splayed strands beta4 and beta5. The catalytic mechanism involves direct acetyl transfer from AcCoA without an acetylated enzyme intermediate. Modeling of the Michaelis complex suggests that the nucleotide- and 4-amino-4,6-dideoxy-beta-L-AltNAc-binding pockets form extensive interactions with the substrate and are thus the most significant determinants of substrate specificity. A hydrophobic pocket accommodating the 6'-methyl group of the altrose dictates preference to the methyl over the hydroxyl group Helicobacter pylori

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.202 Helicobacter pylori O25094
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2.3.1.202 Helicobacter pylori ATCC 700392 O25094
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Synonyms

EC Number Synonyms Comment Organism
2.3.1.202 PsEH
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 Helicobacter pylori