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Literature summary extracted from

  • Ray, P.H.
    3-Deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase (1982), Methods Enzymol., 83, 525-530.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.5.1.55 repeated freezing and thawing causes loss of activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.55 2-Deoxy-2-fluoro-D-arabinoate-5-phosphate
-
 Escherichia coli
2.5.1.55 Cd2+ 1 mM Escherichia coli
2.5.1.55 Cu2+ 1 mM Escherichia coli
2.5.1.55 D-ribose 5-phosphate
-
 Escherichia coli
2.5.1.55 Hg2+ 1 mM Escherichia coli
2.5.1.55 phosphate
-
 Escherichia coli
2.5.1.55 Zn2+ 1 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.55 0.006
-
 phosphoenolpyruvate
-
 Escherichia coli
2.5.1.55 0.02
-
 D-arabinose 5-phosphate
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.55 additional information no metal requirement Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.55 32000
-
 3 * 32000, SDS-PAGE Escherichia coli
2.5.1.55 90000
-
 gel filtration, non-denaturing PAGE 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 the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose-5-phosphate + H2O Escherichia coli B / ATCC 11303 the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.55 Escherichia coli
-
-
-
2.5.1.55 Escherichia coli B / ATCC 11303
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.55 3.7
-
-
 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
2.5.1.55 -20°C, 50% loss of activity after 14 days Escherichia coli
2.5.1.55 -90°C, 0.1 M potassium phosphate buffer, pH 7.2, stable for up to 1 year 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
-
 Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose 5-phosphate
-
 Escherichia coli B / ATCC 11303 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose-5-phosphate + H2O the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
2.5.1.55 phosphoenolpyruvate + D-arabinose-5-phosphate + H2O the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor Escherichia coli B / ATCC 11303 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.55 trimer 3 * 32000, SDS-PAGE Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.55 4 6 and a second optimum at pH 9.0 Escherichia coli
2.5.1.55 9
-
 and a second optimum at pH 4.0-6.0 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.55 1
-
 D-ribose 5-phosphate pH 7.3, 37°C Escherichia coli