Crystallization (Comment) | Organism |
---|---|
ManNAc kinase in complex with its substrate ManNAc, its product ManNAc 6-phosphate, with or without ADP, vapor diffusion at 18°C, mixing 0.002 ml of 15 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 2 mM ManNAc, with 0.002 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodiumcacodylate, pH 6.5, and 40% PEG 300, 5 days, X-ray diffraction structure determination and analysis at 1.64-2.10 A resolution. No crystals by co-crystallization of hMNK with ManNAc and ADP, ATP, AMPPCP, or AMPPNP, but ternary complexes are obtained by soaking crystals of the binary hMNK-ManNAc complex replacing stepwise their mother liquor with solutions containing 0.1 M sodium cacodylate, pH 6.5, 50% PEG 300, and 20 mM ADPor ATP or nonhydrolyzable ATP derivatives | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D517A | site-directed mutagenesis, inactive mutant | Homo sapiens |
D517N | site-directed mutagenesis, inactive mutant | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-O-methyl-N-acetylglucosamine | - |
Homo sapiens | |
6-O-acetyl-N-acetylmannosamine | - |
Homo sapiens | |
N-propanoylglucosamine | - |
Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.127 | - |
N-acyl-D-mannosamine | pH 8.1, 37°C, recombinant enzyme | Homo sapiens | |
4.4 | - |
ATP | pH 8.1, 37°C, recombinant enzyme | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Homo sapiens | 5737 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, Mg2+ is octahedrically coordinated with the beta-phosphate-O3 atom and Asp-413-Odelta2 in the axial positions, whereas four water molecules occupy the equatorial sites | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + N-acyl-D-mannosamine | Homo sapiens | - |
ADP + N-acyl-D-mannosamine 6-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9Y223 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2.6 | - |
pH 8.1, 37°C, recombinant enzyme | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + N-acyl-D-mannosamine | - |
Homo sapiens | ADP + N-acyl-D-mannosamine 6-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MNK | - |
Homo sapiens |
UDP-GlcNAc-2 epimerase/ManNAc kinase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.1 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | binding structure, overview | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | active site structure of the N-acetylmannosamine kinase domain, ligand binding and reaction mechanism, catalytic role of Asp517, overview. The side chain of Asp-413 does not directly bind one of the oxygens of the beta-phosphate but is necessary for Mg2+ coordination and consequently crucial for ATP binding | Clostridium acetobutylicum |
physiological function | the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase transforms UDP-N-acetylglucosamine to N-acetylmannosamine followed by its phosphorylation to ManNAc 6-phosphate and has a direct impact on the sialylation of cell surface components | Clostridium acetobutylicum |