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Literature summary for 5.1.3.14 extracted from

  • Effertz, K.; Hinderlich, S.; Reutter, W.
    Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments (1999), J. Biol. Chem., 274, 28771-28778.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
high level overexpression of the active enzyme is established by using the baculovirus/Sf9 system Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D413K enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity Rattus norvegicus
D413N enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity Rattus norvegicus
H110A mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme,loss of epimerase activity can largely by attributed to incorrect protein folding Rattus norvegicus
H132A mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme, loss of epimerase activity can largely by attributed to incorrect protein folding Rattus norvegicus
H155A mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer Rattus norvegicus
H155A mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding Rattus norvegicus
H157A mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer Rattus norvegicus
H157A mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding Rattus norvegicus
H45A mutant enzyme shows a drastic loss of epimerase activity Rattus norvegicus
R420M enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
CMP-N-acetylneuraminic acid feedback inhibitor 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
75000
-
6 * 75000, SDS-PAGE Rattus norvegicus
450000
-
gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus key enzyme of N-acetylneuraminic acid biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Rattus norvegicus ?
-
?
additional information key enzyme of N-acetylneuraminic acid biosynthesis Rattus norvegicus ?
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 75000, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
More bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Rattus norvegicus