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Literature summary for 1.1.1.6 extracted from
- The improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions (2013), Biotechnol. Bioprocess Eng., 18, 796-800.
No PubMed abstract available
General Stability
| General Stability | Organism |
|---|---|
| manganese substitution increases the half-life of GDH by 6folds at 60°C and 70°C | Klebsiella pneumoniae subsp. pneumoniae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic and thermodynamic analysis, Michaelis-Menten kinetics, overview | Klebsiella pneumoniae subsp. pneumoniae | |
| 0.23 | - |
NAD+ | Mg-GDH, pH 12.0, 45°C, recombinant enzyme | Klebsiella pneumoniae subsp. pneumoniae |  |
| 0.38 | - |
NAD+ | wild-type Zn-GDH, pH 12.0, 45°C, recombinant enzyme | Klebsiella pneumoniae subsp. pneumoniae | |
| 1.12 | - |
NAD+ | Mg-GDH, pH 12.0, 45°C, recombinant enzyme | Klebsiella pneumoniae subsp. pneumoniae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions Mn2+ and Mg2+, overview. The activity of Mn-GDH and Mg-GDH improves several folds in comparison to the native GDH. The activity of substituted GDH towards non-natural substrates, 4-chloroacetoacetate, 3-chloroacetylpyridine, p-chloroacetophenone, and acetophenone is 30folds higher than native GDH. Manganese substitution increases the half-life of GDH by 6folds at 60°C and 70°C | Klebsiella pneumoniae subsp. pneumoniae | |
| Mn2+ | improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions Mn2+ and Mg2+, overview | Klebsiella pneumoniae subsp. pneumoniae | |
| additional information | bifunctional role of metal ions in GDH in catalysis and structure stabilization | Klebsiella pneumoniae subsp. pneumoniae | |
| Zn2+ | glycerol dehydrogenase from Klebsiella pneumoniae is a zinc-dependent metalloenzyme | Klebsiella pneumoniae subsp. pneumoniae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycerol + NAD+ | Klebsiella pneumoniae subsp. pneumoniae | - |
glycerone + NADH + H+ | - |
r | |
| glycerol + NAD+ | Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 | - |
glycerone + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Klebsiella pneumoniae subsp. pneumoniae | A6TGD6 | - |
- |
| Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 | A6TGD6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycerol + NAD+ | - |
Klebsiella pneumoniae subsp. pneumoniae | glycerone + NADH + H+ | - |
r | |
| glycerol + NAD+ | - |
Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 | glycerone + NADH + H+ | - |
r | |
| additional information | the enzyme is also active with substrates 4-chloroacetoacetate, 3-chloroacetylpyridine, 4-chloroacetophenone, and acetophenone, substrate specificities of enzyme with bound Zn2+, Mn2+, or Mg2+, overview | Klebsiella pneumoniae subsp. pneumoniae | ? | - |
? | |
| additional information | the enzyme is also active with substrates 4-chloroacetoacetate, 3-chloroacetylpyridine, 4-chloroacetophenone, and acetophenone, substrate specificities of enzyme with bound Zn2+, Mn2+, or Mg2+, overview | Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GDH | - |
Klebsiella pneumoniae subsp. pneumoniae |
| GldA | - |
Klebsiella pneumoniae subsp. pneumoniae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
assay at | Klebsiella pneumoniae subsp. pneumoniae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal inactivation of GDH is not a simple first-order process, thermal deactivation kinetics, modelling, overview | Klebsiella pneumoniae subsp. pneumoniae |
| 30 | 50 | purified recombinant enzyme, pH 12.0, quite stable over 150 min | Klebsiella pneumoniae subsp. pneumoniae |
| 60 | - |
purified recombinant enzyme, pH 12.0, loss of about 25% activity after 100 min | Klebsiella pneumoniae subsp. pneumoniae |
| 70 | - |
purified recombinant enzyme, pH 12.0, loss of about 75% activity after 80 min | Klebsiella pneumoniae subsp. pneumoniae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 12 | - |
assay at | Klebsiella pneumoniae subsp. pneumoniae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Klebsiella pneumoniae subsp. pneumoniae | |
| NADH | - |
Klebsiella pneumoniae subsp. pneumoniae | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 46.1 | - |
NAD+ | wild-type Zn-GDH, pH 12.0, 45°C, recombinant enzyme | Klebsiella pneumoniae subsp. pneumoniae | |
| 83.6 | - |
NAD+ | Mg-GDH, pH 12.0, 45°C, recombinant enzyme | Klebsiella pneumoniae subsp. pneumoniae | |
| 120.3 | - |
NAD+ | Mg-GDH, pH 12.0, 45°C, recombinant enzyme | Klebsiella pneumoniae subsp. pneumoniae | |
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