Application | Comment | Organism |
---|---|---|
analysis | the kinase is applied for high-sensitive detection of the amino sugars in cell wall preparations by radioactive phosphorylation | Clostridium acetobutylicum |
Cloned (Comment) | Organism |
---|---|
expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Clostridium acetobutylicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | a 3fold excess of EDTA compared to the Mg2+ concentration strongly represses the MurK activity. Addition of 2 mM MgCl2 to the reaction mixture partially restores MurK activity | Clostridium acetobutylicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.127 | - |
N-acetyl-D-glucosamine | pH 7.5, 37°C | Clostridium acetobutylicum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell wall | - |
Clostridium acetobutylicum | 5618 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Clostridium acetobutylicum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
34329 | - |
x * 34329, sequence calculation | Clostridium acetobutylicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + N-acetyl-D-glucosamine | Clostridium acetobutylicum | - |
ADP + N-acetyl-D-glucosamine 6-phosphate | - |
? | |
additional information | Clostridium acetobutylicum | the enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid and N-acetylglucosamine, which are phosphorylated at the 6-hydroxyl group, see also EC 2.7.1.170, the kcat value is 1.5fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. Product identificsation by nonradioactive and radioactive TLC | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium acetobutylicum | - |
gene murK | - |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Clostridium acetobutylicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + N-acetyl-D-glucosamine | - |
Clostridium acetobutylicum | ADP + N-acetyl-D-glucosamine 6-phosphate | - |
? | |
additional information | the enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid and N-acetylglucosamine, which are phosphorylated at the 6-hydroxyl group, see also EC 2.7.1.170, the kcat value is 1.5fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. Product identificsation by nonradioactive and radioactive TLC | Clostridium acetobutylicum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 34329, sequence calculation | Clostridium acetobutylicum |
Synonyms | Comment | Organism |
---|---|---|
GlcNAc kinase | - |
Clostridium acetobutylicum |
MurK | - |
Clostridium acetobutylicum |
N-acetylmuramic acid/N-acetylglucosamine kinase | - |
Clostridium acetobutylicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Clostridium acetobutylicum |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
at 30°C, the purified protein loses activity within hours of incubation, regardless of the addition of protease inhibitors | Clostridium acetobutylicum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
65 | - |
N-acetyl-D-glucosamine | pH 7.5, 37°C | Clostridium acetobutylicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 9 | - |
Clostridium acetobutylicum |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 10.5 | half maximal activity at about pH 6.5 and pH 10.5, inactive at pH 5.0 and below | Clostridium acetobutylicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Clostridium acetobutylicum |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the BcrAD/BadFGlike ATPase family | Clostridium acetobutylicum |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
510.2 | - |
N-acetyl-D-glucosamine | pH 7.5, 37°C | Clostridium acetobutylicum |