Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.60 D413K loss of kinase activity Rattus norvegicus
2.7.1.60 D413L loss of kinase activity Rattus norvegicus
2.7.1.60 D413N loss of kinase activity Rattus norvegicus
2.7.1.60 H110A loss of epimerase activity Rattus norvegicus
2.7.1.60 H132A loss of epimerase activity Rattus norvegicus
2.7.1.60 H155A loss of epimerase activity Rattus norvegicus
2.7.1.60 H157A loss of epimerase activity Rattus norvegicus
2.7.1.60 H45A loss of epimerase activity Rattus norvegicus
2.7.1.60 R420M loss of kinase activity Rattus norvegicus
5.1.3.14 D413K enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity Rattus norvegicus
5.1.3.14 D413N enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity Rattus norvegicus
5.1.3.14 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
5.1.3.14 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
5.1.3.14 H155A mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer Rattus norvegicus
5.1.3.14 H155A mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding Rattus norvegicus
5.1.3.14 H157A mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer Rattus norvegicus
5.1.3.14 H157A mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding Rattus norvegicus
5.1.3.14 H45A mutant enzyme shows a drastic loss of epimerase activity Rattus norvegicus
5.1.3.14 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

EC Number Inhibitors Comment Organism Structure
5.1.3.14 CMP-N-acetylneuraminic acid feedback inhibitor Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.60 cytosol
-
Rattus norvegicus 5829
-
5.1.3.14 cytosol
-
Rattus norvegicus 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.60 75000
-
gel filtration, SDS-PAGE Rattus norvegicus
2.7.1.60 450000
-
gel filtration Rattus norvegicus
5.1.3.14 75000
-
6 * 75000, SDS-PAGE Rattus norvegicus
5.1.3.14 450000
-
gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.60 ATP + N-acetyl-D-mannosamine Rattus norvegicus involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis ADP + N-acetyl-D-mannosamine 6-phosphate
-
?
5.1.3.14 additional information Rattus norvegicus key enzyme of N-acetylneuraminic acid biosynthesis ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.60 Rattus norvegicus
-
-
-
5.1.3.14 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.60 liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.60 0.84
-
recombinant enzyme Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.60 ATP + N-acetyl-D-mannosamine involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis Rattus norvegicus ADP + N-acetyl-D-mannosamine 6-phosphate
-
?
2.7.1.60 ATP + N-acetyl-D-mannosamine
-
Rattus norvegicus ADP + N-acetyl-D-mannosamine-6-phosphate
-
?
5.1.3.14 additional information bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Rattus norvegicus ?
-
?
5.1.3.14 additional information key enzyme of N-acetylneuraminic acid biosynthesis Rattus norvegicus ?
-
?

Subunits

EC Number Subunits Comment Organism
2.7.1.60 dimer 2 * 75000, self associates as a dimer, gel filtration, SDS-PAGE, catalyzes only phosphorylation of N-acetylmannosamine, incubation with UDP-N-acetylglucosamine leads to reassembly of the fully active hexamer Rattus norvegicus
2.7.1.60 hexamer
-
Rattus norvegicus
5.1.3.14 hexamer 6 * 75000, SDS-PAGE Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.60 EC 5.1.3.14/EC 2.7.1.60
-
Rattus norvegicus
2.7.1.60 UDP-GlcNAc-epimerase/ManNAc kinase
-
Rattus norvegicus
5.1.3.14 More bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Rattus norvegicus