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Literature summary for 5.1.3.14 extracted from

  • Hinderlich, S.; Stäsche, R.; Zeitler, R.; Reutter, W.
    A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (1997), J. Biol. Chem., 272, 24313-24318.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
CMP-N-acetylneuraminic acid
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
 UDP-N-acetyl-D-glucosamine bifunctional enzyme EC5.1.3.14/EC2.7.1.60 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus norvegicus 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
450000
-
 gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 bifunctional enzyme EC 5.1.3.14/EC 2.7.1.60
-

Purification (Commentary)

Purification (Comment) Organism
bifunctional enzyme EC 5.1.3.14/EC 2.7.1.60 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.878
-
-
 Rattus norvegicus

Storage Stability

Storage Stability Organism
-70°C, stable for several months Rattus norvegicus

Subunits

Subunits Comment Organism
hexamer bifunctional enzyme EC 5.1.3.14/EC 2.7.1.60, SDS-PAGE Rattus norvegicus