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Literature summary extracted from
- Purification and properties of phosphoglucosamine mutase (1971), J. Biol. Chem., 246, 3485-3493.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.2.3 | 8-hydroxyquinoline | metal chelator required | Sus scrofa |  |
| 5.4.2.3 | Cys | metal chelator required | Sus scrofa | |
| 5.4.2.3 | diethyldithiocarbamate | metal chelator required | Sus scrofa | |
| 5.4.2.3 | fructose 1,6-diphosphate | or glucose 1,6-diphosphate activates, Km: 0.018 mM | Sus scrofa | |
| 5.4.2.3 | glucose 1,6-diphosphate | or fructose 1,6-diphosphate activates, Km: 0.002 mM | Sus scrofa | |
| 5.4.2.3 | sulfhydryl compound | increases activity | Sus scrofa | |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 5.4.2.3 | purified enzyme loses more than 90% activity upon one freezing and thawing | Sus scrofa |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.2.3 | Be2+ | 0.02 mM in presence of 1 mM Mg2+, complete inhibition | Sus scrofa | |
| 5.4.2.3 | Cd2+ | 0.5 mM in presence of 1 mM Mg2+, complete inhibition | Sus scrofa | |
| 5.4.2.3 | Cu2+ | 0.5 mM in presence of 1 mM Mg2+, complete inhibition | Sus scrofa | |
| 5.4.2.3 | Mn2+ | 1 mM in presence of 1 mM Mg2+, complete inhibition | Sus scrofa | |
| 5.4.2.3 | Zn2+ | 0.5 mM in presence of 1 mM Mg2+, complete inhibition | Sus scrofa | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.2.3 | 0.29 | - |
N-acetylglucosamine 1-phosphate | - |
Sus scrofa | |
| 5.4.2.3 | 0.39 | - |
glucose 1-phosphate | - |
Sus scrofa | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.2.3 | Mg2+ | divalent metal ion required. Optimal Mg2+ concentration in the presence of dithiothreitol is 10 mM, maximal activity with other metal chelators is obtained with 1 mM Mg2+ | Sus scrofa | |
| 5.4.2.3 | Mn2+ | divalent metal ion required. Mn2+ is less efficient than Mg2+ | Sus scrofa | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.2.3 | Sus scrofa | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.4.2.3 | - |
Sus scrofa |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.4.2.3 | submandibular gland | - |
Sus scrofa | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.4.2.3 | additional information | - |
- |
Sus scrofa |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 5.4.2.3 | 0°C, 30% sucrose or 30% glycerol, 50% loss of activity after 3 weeks. Addition of albumin or varying the pH does not appreciably enhance the stability of the enzyme | Sus scrofa |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.2.3 | Glucose 1-phosphate | - |
Sus scrofa | Glucose 6-phosphate | - |
? | |
| 5.4.2.3 | N-Acetyl-D-glucosamine 1-phosphate | - |
Sus scrofa | N-Acetyl-D-glucosamine 6-phosphate | - |
? | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.2.3 | 6.5 | 7 | Tris-HCl buffer | Sus scrofa |
| 5.4.2.3 | 7 | 7.5 | Tris-maleate buffer | Sus scrofa |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.2.3 | 6.5 | 9 | pH 6.5: about 45% of maximal activity, pH 9.0: about 40% of maximal activity, Tris-maleate buffer | Sus scrofa |
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