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Literature summary extracted from

  • Li, Z.; Sau, A.
    Probing the subunit-subunit interaction of the tetramer of E. coli KDO8P synthase by electrospray ionization mass spectrometry (2009), Chin. J. Chem., 27, 111-116.
No PubMed abstract available

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.55 30845
-
 1 * 30845, ESI-MS, unbound enzyme with substrate phosphoenolpyruvate or product phosphate favors the formation of monomers, phosphoenolpyruvate-bound and unbound enzyme exists as monomer Escherichia coli
2.5.1.55 30845
-
 2 * 30845, ESI-MS, predominant in unbound enzyme in complex with substrate D-arabinose 5-phosphate or product 3-deoxy-D-manno-octulosonate 8-phosphate, phosphoenolpyruvate-bound and unbound enzyme exists as dimer Escherichia coli
2.5.1.55 30845
-
 4 * 30845, ESI-MS, phosphoenolpyruvate-bound enzyme exists as tetramer to a low extent, unbound enzyme does not exist in tetrameric state, phosphoenolpyrovate stabilizes the tetrameric structure and may bind at the same position as phosphate Escherichia coli
2.5.1.55 30850
-
 monomer, ESI-MS Escherichia coli
2.5.1.55 62680
-
 dimer, ESI-MS Escherichia coli
2.5.1.55 123400
-
 tetramer, ESI-MS Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.55 phosphoenolpyruvate + D-arabinose 5-phosphate + H2O Escherichia coli
-
 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.55 overnight dialysis against 50 mM ammonium acetate, pH 7.8, 4°C, reconstitution with substrates and products Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.55 phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
-
 Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.55 dimer 2 * 30845, ESI-MS, predominant in unbound enzyme in complex with substrate D-arabinose 5-phosphate or product 3-deoxy-D-manno-octulosonate 8-phosphate, phosphoenolpyruvate-bound and unbound enzyme exists as dimer Escherichia coli
2.5.1.55 monomer 1 * 30845, ESI-MS, unbound enzyme with substrate phosphoenolpyruvate or product phosphate favors the formation of monomers, phosphoenolpyruvate-bound and unbound enzyme exists as monomer Escherichia coli
2.5.1.55 tetramer 4 * 30845, ESI-MS, phosphoenolpyruvate-bound enzyme exists as tetramer to a low extent, unbound enzyme does not exist in tetrameric state, phosphoenolpyrovate stabilizes the tetrameric structure and may bind at the same position as phosphate Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.5.1.55 3-deoxy-D-manno-octulosonate 8-phosphate synthase
-
 Escherichia coli
2.5.1.55 Kdo8P synthase
-
 Escherichia coli