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Literature summary extracted from

  • Ishiyama, N.; Creuzenet, C.; Miller, W.L.; Demendi, M.; Anderson, E.M.; Harauz, G.; Lam, J.S.; Berghuis, A.M.
    Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism for inverting 4,6-dehydratase activity (2006), J. Biol. Chem., 281, 24489-24495.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.115 FlaA1-NADP+-UDP-GlcNAc and FlaA1-NADP+-UDPGlc ternary complexes, at room temperature by hanging-drop vapor diffusion in presence of NAD+, using as reservoir solution 10% v/v polyethylene glycol-200, 100 mM MES, pH 6.0, 5% v/w PEG 3000, and 4% acetone, and providing 10 mM excess of substrate, X-ray diffraction structure determination and analysis Helicobacter pylori

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.115 K133E site-directed mutagenesis, inactive mutant Helicobacter pylori
4.2.1.115 K133M site-directed mutagenesis, inactive mutant Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.115 UDP-N-acetylglucosamine Helicobacter pylori the enzyme catalyzes the first step in the biosynthetic pathway of a pseudaminic acid derivative, which is implicated in protein glycosylation UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.115 Helicobacter pylori
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.115 UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O reaction mechanism, FlaA1 is a UDP-GlcNAc 4,6-dehydratase that additionally inverts the chirality at the C-5 position Helicobacter pylori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.115 UDP-N-acetylglucosamine the enzyme catalyzes the first step in the biosynthetic pathway of a pseudaminic acid derivative, which is implicated in protein glycosylation Helicobacter pylori UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
?
4.2.1.115 UDP-N-acetylglucosamine NMR reaction analysis, a possible three-step reaction mechanism that involves Lys133 functioning as both a catalytic acid and base Helicobacter pylori UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
?

Subunits

EC Number Subunits Comment Organism
4.2.1.115 hexamer the enzyme possesses a hexameric doughnut-shaped quaternary structure, crystal stucture analysis Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
4.2.1.115 FlaA1
-
Helicobacter pylori
4.2.1.115 inverting 4,6-dehydratase
-
Helicobacter pylori
4.2.1.115 More the enzyme belongs to the SDR superfamily Helicobacter pylori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.115 25
-
assay at Helicobacter pylori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.115 7.2
-
assay at Helicobacter pylori

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.115 NADP+ NADP+/NADPH is tightly bound to FlaA1 Helicobacter pylori