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Literature summary for 2.5.1.55 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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
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
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
30850
-
monomer, ESI-MS Escherichia coli
62680
-
dimer, ESI-MS Escherichia coli
123400
-
tetramer, ESI-MS Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A715
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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
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

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