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Literature summary for 3.5.99.6 extracted from
- Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus (2019), FEBS Lett., 593, 52-66 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene nagB, coexpression with gene nagA in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain strain XL-1 Blue | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha-D-glucosamine 6-phosphate | substrate inhibition | Staphylococcus aureus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required, the sigmoidal response with respect to Zn2+ concentration suggests cooperativity and the binding of at least two metal ions within the active site | Staphylococcus aureus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28500 | - |
monomeric enzyme, gel filtration | Staphylococcus aureus |
| 57000 | - |
dimeric enzyme, gel filtration | Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucosamine 6-phosphate + H2O | Staphylococcus aureus | - |
D-fructose 6-phosphate + NH3 | - |
? | |
| alpha-D-glucosamine 6-phosphate + H2O | Staphylococcus aureus USA300 | - |
D-fructose 6-phosphate + NH3 | - |
? | |
| alpha-D-glucosamine 6-phosphate + H2O | Staphylococcus aureus TCH1516 | - |
D-fructose 6-phosphate + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | A8YZR7 | - |
- |
| Staphylococcus aureus TCH1516 | A8YZR7 | - |
- |
| Staphylococcus aureus USA300 | A8YZR7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme NagB from Escherichia coli strain BL21(DE3) by anion exchange chromatography, hydrophobic interaction chromatography, and gel filtration, to near homogeneity | Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucosamine 6-phosphate + H2O | - |
Staphylococcus aureus | D-fructose 6-phosphate + NH3 | - |
? | |
| alpha-D-glucosamine 6-phosphate + H2O | - |
Staphylococcus aureus USA300 | D-fructose 6-phosphate + NH3 | - |
? | |
| alpha-D-glucosamine 6-phosphate + H2O | - |
Staphylococcus aureus TCH1516 | D-fructose 6-phosphate + NH3 | - |
? | |
| additional information | kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+ | Staphylococcus aureus | ? | - |
- |
|
| additional information | kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+ | Staphylococcus aureus USA300 | ? | - |
- |
|
| additional information | kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+ | Staphylococcus aureus TCH1516 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer or dimer | x * 28500, SDS-PAGE | Staphylococcus aureus |
| More | Staphylococcus aureus NagB is active without the need for allosteric activation. No rate increase is observed when N-acetylglucosamine-6-phosphate (the allosteric activator for Escherichia coli NagB) is added to the assay mixture, or when incubated with the enzyme prior to adding it to the assay | Staphylococcus aureus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NagB | - |
Staphylococcus aureus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
assay at | Staphylococcus aureus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 105 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Staphylococcus aureus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the lack of allostery as for Staphlyococcus aureus NagB has also been observed in the monomeric Staphylococcus mutans and Bacillus subtilis NagB enzymes, and supports the hypothesis that Gram-positive NagB enzymes have lost the property of allosteric regulation | Staphylococcus aureus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 437.5 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
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