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Literature summary 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.25 | gene nagA, recombinant expression in Escherichia coli strain BL21(DE3) from plasmid pET30DELTASE/nagA | Staphylococcus aureus |
| 3.5.99.6 | gene nagB, coexpression with gene nagA in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain strain XL-1 Blue | Staphylococcus aureus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.25 | EDTA | - |
Staphylococcus aureus |  |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate | substrate inhibition | Staphylococcus aureus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.25 | additional information | - |
additional information | Michaelis-Mente kinetics. The initial rate measured for NagA has a significant substrate concentration-dependent lag phase which is not influenced by 1 mM Zn2+ and not pH-dependent | Staphylococcus aureus | |
| 3.5.1.25 | 0.16 | - |
N-acetyl-D-glucosamine-6-phosphate | pH 8.0, 30°C, recombinant enzyme | Staphylococcus aureus | |
| 3.5.99.6 | 0.24 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.25 | Zn2+ | NagA requires two Zn2+ metal ions for activity | Staphylococcus aureus | |
| 3.5.99.6 | 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]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.25 | 43200 | - |
recombinant reduced monomeric enzyme NagA, analytical gel filtration | Staphylococcus aureus |
| 3.5.1.25 | 86300 | - |
about, dimer, sequence calculation | Staphylococcus aureus |
| 3.5.1.25 | 86700 | - |
recombinant dimeric enzyme, analytical gel filtration | Staphylococcus aureus |
| 3.5.99.6 | 28500 | - |
monomeric enzyme, gel filtration | Staphylococcus aureus |
| 3.5.99.6 | 57000 | - |
dimeric enzyme, gel filtration | Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.25 | N-acetyl-D-glucosamine-6-phosphate + H2O | Staphylococcus aureus | - |
D-glucosamine 6-phosphate + acetate | - |
? | |
| 3.5.1.25 | N-acetyl-D-glucosamine-6-phosphate + H2O | Staphylococcus aureus USA300_TCH1516 | - |
D-glucosamine 6-phosphate + acetate | - |
? | |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O | Staphylococcus aureus | - |
D-fructose 6-phosphate + NH3 | - |
? | |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O | Staphylococcus aureus USA300 | - |
D-fructose 6-phosphate + NH3 | - |
? | |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O | Staphylococcus aureus TCH1516 | - |
D-fructose 6-phosphate + NH3 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.25 | Staphylococcus aureus | - |
- |
- |
| 3.5.1.25 | Staphylococcus aureus USA300_TCH1516 | - |
- |
- |
| 3.5.99.6 | Staphylococcus aureus | A8YZR7 | - |
- |
| 3.5.99.6 | Staphylococcus aureus TCH1516 | A8YZR7 | - |
- |
| 3.5.99.6 | Staphylococcus aureus USA300 | A8YZR7 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.25 | recombinant enzyme NagA from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, followed by gel filtration | Staphylococcus aureus |
| 3.5.99.6 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.25 | additional information | performance of a coupled assay with NagB (EC 3.5.99.6) resulting in production of fructose 6-phosphate and NH3 | Staphylococcus aureus | ? | - |
? | |
| 3.5.1.25 | additional information | performance of a coupled assay with NagB (EC 3.5.99.6) resulting in production of fructose 6-phosphate and NH3 | Staphylococcus aureus USA300_TCH1516 | ? | - |
? | |
| 3.5.1.25 | N-acetyl-D-glucosamine-6-phosphate + H2O | - |
Staphylococcus aureus | D-glucosamine 6-phosphate + acetate | - |
? | |
| 3.5.1.25 | N-acetyl-D-glucosamine-6-phosphate + H2O | - |
Staphylococcus aureus USA300_TCH1516 | D-glucosamine 6-phosphate + acetate | - |
? | |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O | - |
Staphylococcus aureus | D-fructose 6-phosphate + NH3 | - |
? | |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O | - |
Staphylococcus aureus USA300 | D-fructose 6-phosphate + NH3 | - |
? | |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O | - |
Staphylococcus aureus TCH1516 | D-fructose 6-phosphate + NH3 | - |
? | |
| 3.5.99.6 | additional information | kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+ | Staphylococcus aureus | ? | - |
- |
|
| 3.5.99.6 | additional information | kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+ | Staphylococcus aureus USA300 | ? | - |
- |
|
| 3.5.99.6 | additional information | kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+ | Staphylococcus aureus TCH1516 | ? | - |
- |
|
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.25 | dimer | NagA is an asymmetric dimer in solution, analytical ultracentrifugation and small-angle X-ray scattering data | Staphylococcus aureus |
| 3.5.1.25 | More | involvement of both subunits in binding substrate | Staphylococcus aureus |
| 3.5.99.6 | monomer or dimer | x * 28500, SDS-PAGE | Staphylococcus aureus |
| 3.5.99.6 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.25 | NagA | - |
Staphylococcus aureus |
| 3.5.99.6 | NagB | - |
Staphylococcus aureus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.25 | 30 | - |
assay at | Staphylococcus aureus |
| 3.5.99.6 | 20 | - |
assay at | Staphylococcus aureus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.25 | 345 | - |
N-acetyl-D-glucosamine-6-phosphate | pH 8.0, 30°C, recombinant enzyme | Staphylococcus aureus | |
| 3.5.99.6 | 105 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.25 | 8 | - |
assay at | Staphylococcus aureus |
| 3.5.99.6 | 8 | - |
assay at | Staphylococcus aureus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.99.6 | 3 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.25 | metabolism | N-acetylglucosamine-6-phosphate deacetylase (NagA) and glucosamine-6-phosphate deaminase (NagB) are branch point enzymes that direct amino sugars into different pathways | Staphylococcus aureus |
| 3.5.1.25 | additional information | involvement of both subunits in binding substrate by NagA. NagA requires two Zn2+ metal ions for activity and displays an unusual hysteretic behaviour, which may have a role in regulating flux at this step | Staphylococcus aureus |
| 3.5.99.6 | 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]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.25 | 2156.25 | - |
N-acetyl-D-glucosamine-6-phosphate | pH 8.0, 30°C, recombinant enzyme | Staphylococcus aureus | |
| 3.5.99.6 | 437.5 | - |
alpha-D-glucosamine 6-phosphate | pH 8.0, 20°C, recombinant enzyme | Staphylococcus aureus | |
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