Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.55 extracted from

  • Duewel, H.S.; Radaev, S.; Wang, J.; Woodard, R.W.; Gatti, D.L.
    Substrate and metal complexes of 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Aquifex aeolicus at 1.9-A resolution. Implications for the condensation mechanism (2001), J. Biol. Chem., 276, 8393-8402.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the metal-free and Cd2+ forms of the enzyme are determined in the uncomplexed state and in complex with various combinations of phosphoenolpyruvate, arabinose 5-phosphate and erythrose 4-phosphate Aquifex aeolicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-arabinose 5-phosphate
-
Aquifex aeolicus 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
?