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Literature summary extracted from

  • Radaev, S.; Dastidar, P.; Patel, M.; Woodard, R.W.; Gatti, D.L.
    Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase (2000), J. Biol. Chem., 275, 9476-9484.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.55 crystallization is performed by vapor diffusion in hanging drops Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.54 additional information Escherichia coli structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy ?
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose-5-phosphate + H2O Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the liposaccharide of gram-negative bacteria 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.54 Escherichia coli
-
-
-
2.5.1.55 Escherichia coli P0A715
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.55
-
 Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate mechanism Escherichia coli
a
2.5.1.55 phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate the synthesis of 2-dehydro-3-deoxy-D-octonate 8-phosphate proceeds through the formation of a linear rather than a cyclic intermediate Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.54 additional information structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy Escherichia coli ?
-
 ?
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
-
 Escherichia coli 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose 5-phosphate
-
 Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose-5-phosphate + H2O 2-dehydro-3-deoxy-D-octonate 8-phosphate is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the liposaccharide of gram-negative bacteria Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.54 More active site structure Escherichia coli
2.5.1.55 tetramer the enzyme is a homotetramer in which each monomer has the fold of a (beta/alpha)8 barrel Escherichia coli