EC Number   |
General Information |
Reference  |
|---|
    2.5.1.55 | metabolism |
catalyzes the formation of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P), a key precursor in the biosynthesis of the endotoxin of Gram-negative bacteria |
707492 |
| 2.5.1.55 | more |
active site structure, overview |
737364 |
| 2.5.1.55 | physiological function |
the enzyme catalyzes a key step in the synthesis of the lipopolysaccharide of most Gram-negative bacteria, it catalyzes the condensation reaction between phosphoenolpyruvate and arabinose 5-phosphate to produce 3-deoxy-D-manno-octulosonate 8-phosphate. The enzyme is vital for for proper synthesis and assembly of lipoplysaccharides and the survival and virulence of Pseudomonas aeruginosa |
737364 |
| 2.5.1.55 | evolution |
KDO8PS is evolutionarily and structurally related to the first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS, EC 2.5.1.54), which uses erythrose 4-phosphate in place of arabinose 5-phosphate. Both KDO8PS and type Ibeta DAH7PS enzymes adopt similar homotetrameric associations with their active sites close to one of the interfaces |
737680 |
| 2.5.1.55 | physiological function |
the enzyme catalyzes the reaction between phosphoenolpyruvate and arabinose 5-phosphate in the first committed step in the pathway to 3-deoxy-D-manno-octulosonate, a component in the cell wall of Gram-negative bacteria |
737680 |
| 2.5.1.55 | physiological function |
the enzyme synthesizes 3-deoxy-D-manno-octulosonic acid, that is an important component of the nonrepeating core oligosaccharide part of bacterial lipopolysaccharides and in capsular polysaccharides of many bacteria |
737828 |
| 2.5.1.55 | malfunction |
Arabidopsis thaliana kdsA male gametophyte with lethal phenotype |
737981 |
| 2.5.1.55 | malfunction |
while single T-DNA mutants of either gene display no visible phenotypes, generation of a double knockout mutant has not been possible due to a failure of haploid pollen tube elongation |
737981 |
| 2.5.1.55 | more |
in the substrate-bound structure, water molecules play a key role in fixing residues in the proper configuration to achieve a compact structure. The active site is formed by residues the active site Lys52, Asn54, Arg55, Gln133, Asp252, and Asn255 |
738157 |
