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Literature summary for 2.5.1.132 extracted from

  • Angata, T.; Nakata, D.; Matsuda, T.; Kitajima, K.; Troy, F.A.
    Biosynthesis of KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid). Identification and characterization of a KDN-9-phosphate synthetase activity from trout testis (1999), J. Biol. Chem., 274, 22949-22956.
    View publication on PubMed
Search for more literature for 2.5.1.132

Inhibitors

Inhibitors Comment Organism Structure
EDTA the enzyme is active in the absence of exogenously added divalent cations but lost all activity when incubated before assay with 5 mM EDTA. The lost enzyme activity is restored to 2.4–3 times higher levels of the original one by the addition of 1 mM MnCl2, CoCl2, or NiCl2 and to one-third the original activity by 1 mM MgCl2. The other cations (Ca2+, Fe2+, Cu2+, and Zn2+) do not restore enzyme activity Oncorhynchus mykiss
NaCl activity is reduced by about 50% in the presence of 150 mM NaCl compared with the activity without added NaCl Oncorhynchus mykiss

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.66
-
 D-mannose 6-phosphate pH 7.0, 25°C Oncorhynchus mykiss

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ maximal activity in presence of Mn2+ Oncorhynchus mykiss

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 gel filtration Oncorhynchus mykiss

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphoenolpyruvate + D-mannose 6-phosphate + H2O Oncorhynchus mykiss the enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Oncorhynchus mykiss
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Oncorhynchus mykiss

Source Tissue

Source Tissue Comment Organism Textmining
liver specific activity is 33fold lower than in testis Oncorhynchus mykiss
-
testis
-
 Oncorhynchus mykiss
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0009
-
 pH 7.0, 25°C, the 50fold purified enzyme from testis is unstable, preventing further purification of this enzyme activity Oncorhynchus mykiss

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-mannose 6-phosphate + H2O the enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate Oncorhynchus mykiss 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate
-
 ?
phosphoenolpyruvate + D-mannose 6-phosphate + H2O phosphoenolpyruvate i.e. 2-(phosphonooxy)-2-propenoate Oncorhynchus mykiss 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase
-
 Oncorhynchus mykiss
KDN-9-phosphate synthetase
-
 Oncorhynchus mykiss

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
 Oncorhynchus mykiss