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Literature summary for 2.5.1.55 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
Search for more literature for 2.5.1.55

General Stability

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli B / ATCC 11303
-
-
-

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
-20°C, 50% loss of activity after 14 days Escherichia coli
-90°C, 0.1 M potassium phosphate buffer, pH 7.2, stable for up to 1 year Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-arabinose 5-phosphate
-
 Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
phosphoenolpyruvate + D-arabinose 5-phosphate
-
 Escherichia coli B / ATCC 11303 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
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
-
 ?
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

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

pH Optimum

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

Ki Value [mM]

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