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.
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 |
|