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Literature summary for 1.1.1.6 extracted from
- Bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines as artificial polypeptides (2016), Sci. Rep., 6, 24163.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| polyethyleneimines | PEI, activating at 0.5 mM, inhibitory at 1 mM | Klebsiella pneumoniae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinent expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pET-32a | Klebsiella pneumoniae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250650 nm are prepared that exhibit a 1.4fold enhancement catalytic efficiency. The oligomeric GDH assemblies are coated and stabilized by the excessive manganese-chelated PEIs, which further prevents the disassociation of the GDH subunits, metal-mediated oligomeric assemblies of the enzyme. Half-life of immobilized GDH is enhanced by 5.6folds in aqueous phase at 85°C. Formation of multi-level interactions in the PEI-metal-GDH complex, mechanism, overview. A potential technique for multimeric enzyme immobilization with the advantages of low cost, easy operation, high activity reservation, and high stability. The activity of PEI-Mn2+-GDH gradually decreases over 5 cycles. PEI-Mn2+-GDH retains 71% and 53% of its initial activity after cycling through 3 and 5 successive reactions, respectively. The decrease in the activity of the recycled catalyst may be due to the leakage of GDH | Klebsiella pneumoniae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | inhibits the enzyme at high concentrations | Klebsiella pneumoniae |  |
| Cu2+ | inhibits the enzyme at high concentrations | Klebsiella pneumoniae | |
| Mg2+ | inhibits the enzyme at high concentrations | Klebsiella pneumoniae | |
| Ni2+ | inhibits the enzyme at high concentrations | Klebsiella pneumoniae | |
| polyethyleneimines | activating at 0.5 mM, inhibitory at 1 mM | Klebsiella pneumoniae | |
| Zn2+ | inhibits the enzyme at high concentrations | Klebsiella pneumoniae | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme | Klebsiella pneumoniae | |
| 21.6 | - |
glycerol | pH 10.0, 30°C, free enzyme | Klebsiella pneumoniae | |
| 26 | - |
glycerol | pH 10.0, 30°C, immobilized enzyme | Klebsiella pneumoniae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mn2+ | activates, polyethyleneimines-immobilized enzyme PEI-Mn2+-GDH exhibits a 2.9fold increase in activity compared with free GDH | Klebsiella pneumoniae | |
| additional information | the natural GDH-bound Zn2+ are substituted with several divalent metal ions and the enzyme activity is significantly altered. Cu2+, Ni2+, Zn2+, Mn2+, Mg2+ and Ca2+ are used to investigate the effects of metal ions on GDH activity. Only Mn2+ improves the GDH activity by 1.1fold, whereas the other five metal ions inhibit the enzyme to varying degrees at high concentrations | Klebsiella pneumoniae | |
| Zn2+ | required | Klebsiella pneumoniae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycerol + NAD+ | Klebsiella pneumoniae | - |
glycerone + NADH + H+ | - |
r | |
| glycerol + NAD+ | Klebsiella pneumoniae DSM 2026 | - |
glycerone + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Klebsiella pneumoniae | B2ZPN8 | - |
- |
| Klebsiella pneumoniae DSM 2026 | B2ZPN8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinent His-tagged enzyme from Escherichia coli strain BL21(DE3) pET-32a by nickel affinity chromatography, desalting gel filtration, and ultrafiltration | Klebsiella pneumoniae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycerol + NAD+ | - |
Klebsiella pneumoniae | glycerone + NADH + H+ | - |
r | |
| glycerol + NAD+ | - |
Klebsiella pneumoniae DSM 2026 | glycerone + NADH + H+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GDH | - |
Klebsiella pneumoniae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Klebsiella pneumoniae |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme | Klebsiella pneumoniae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
metal ion-chelated polyethyleneimine-immobilized enzyme PEI-Mn2+-GDH exhibits greater heat resistance than free enzyme GDH. After incubation for 90 min at 70°C, PEI-Mn2+-GDH still presents nearly 50% of its initial activity, while free GDH is almost totally inactivated | Klebsiella pneumoniae |
| 85 | - |
metal ion-chelated polyethyleneimine-immobilized enzyme PEI-Mn2+-GDH exhibits a half-life that is enhanced by 5.6folds in aqueous phase at 85°C | Klebsiella pneumoniae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.06 | - |
glycerol | pH 10.0, 30°C, free enzyme | Klebsiella pneumoniae | |
| 3.36 | - |
glycerol | pH 10.0, 30°C, immobilized enzyme | Klebsiella pneumoniae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme | Klebsiella pneumoniae |
| 10 | 11 | the immobilized GDH changes the optimal pH from pH 11 to 10 and exhibits high activity in a relatively wide range of pH from pH 7 to 12, while free GDH only achieves high activity at pH 11 | Klebsiella pneumoniae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
immobilization of the enzyme by metal ion-chelated polyethyleneimines greatly broadens the pH adaptability of GDH from strong alkaline into alkalescence | Klebsiella pneumoniae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Klebsiella pneumoniae | |
| NADH | - |
Klebsiella pneumoniae | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 94 | - |
glycerol | pH 10.0, 30°C, free enzyme | Klebsiella pneumoniae | |
| 129 | - |
glycerol | pH 10.0, 30°C, immobilized enzyme | Klebsiella pneumoniae | |
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