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Literature summary extracted from
- Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterization and N-terminal sequence (1996), FEBS Lett., 383, 227-229.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.113 | EDTA | 2 mM | Haloferax mediterranei |  |
| 1.1.1.119 | EDTA | 2 mM | Haloferax mediterranei | |
| 1.1.1.175 | EDTA | 2 mM | Haloferax mediterranei | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.119 | 0.024 | - |
NADP+ | pH 8.8, 40°C | Haloferax mediterranei | |
| 1.1.1.119 | 1.2 | - |
NAD+ | pH 8.8, 40°C | Haloferax mediterranei | |
| 1.1.1.119 | 3.9 | - |
beta-D-glucose | pH 8.8, 40°C | Haloferax mediterranei | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.119 | KCl | the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M | Haloferax mediterranei | |
| 1.1.1.119 | Mg2+ | besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mg2+ is more effective than Mg2+ or Ni2+ | Haloferax mediterranei | |
| 1.1.1.119 | Mn2+ | besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mn2+ is less effective than Mg2+ and more effective than Ni2+ | Haloferax mediterranei | |
| 1.1.1.119 | NaCl | the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M | Haloferax mediterranei | |
| 1.1.1.119 | Ni2+ | besides KCl/NaCl, the activity also depends on presence of bivalent cations. Ni2+ is more effective than Mg2+ or Mn2+ | Haloferax mediterranei | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.113 | 53000 | - |
2 * 53000, SDS-PAGE | Haloferax mediterranei |
| 1.1.1.113 | 89000 | - |
gel filtration | Haloferax mediterranei |
| 1.1.1.119 | 53000 | - |
2 * 53000, SDS-PAGE | Haloferax mediterranei |
| 1.1.1.119 | 89000 | - |
gel filtration | Haloferax mediterranei |
| 1.1.1.175 | 53000 | - |
2 * 53000, SDS-PAGE | Haloferax mediterranei |
| 1.1.1.175 | 89000 | - |
gel filtration | Haloferax mediterranei |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.113 | Haloferax mediterranei | Q977U7 | - |
- |
| 1.1.1.113 | Haloferax mediterranei DSM 1411 | Q977U7 | - |
- |
| 1.1.1.119 | Haloferax mediterranei | Q977U7 | - |
- |
| 1.1.1.119 | Haloferax mediterranei DSM 1411 | Q977U7 | - |
- |
| 1.1.1.175 | Haloferax mediterranei | Q977U7 | - |
- |
| 1.1.1.175 | Haloferax mediterranei DSM 1411 | Q977U7 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.113 | - |
Haloferax mediterranei |
| 1.1.1.119 | - |
Haloferax mediterranei |
| 1.1.1.175 | - |
Haloferax mediterranei |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.119 | 550 | - |
pH 8.8, 40°C | Haloferax mediterranei |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.1.1.113 | 4°C, stable for several months | Haloferax mediterranei |
| 1.1.1.119 | 4°C, stable for several months | Haloferax mediterranei |
| 1.1.1.175 | 4°C, stable for several months | Haloferax mediterranei |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.113 | D-xylose + NADP+ | 88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+) | Haloferax mediterranei | ? | - |
? | |
| 1.1.1.113 | D-xylose + NADP+ | 88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+) | Haloferax mediterranei DSM 1411 | ? | - |
? | |
| 1.1.1.119 | beta-D-glucose + NAD+ | activity with NAD+ is 26% of the activity with NADP+ | Haloferax mediterranei | ? | - |
? | |
| 1.1.1.119 | beta-D-glucose + NAD+ | activity with NAD+ is 26% of the activity with NADP+ | Haloferax mediterranei DSM 1411 | ? | - |
? | |
| 1.1.1.119 | beta-D-glucose + NADP+ | activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+) | Haloferax mediterranei | ? | - |
? | |
| 1.1.1.119 | beta-D-glucose + NADP+ | activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+) | Haloferax mediterranei DSM 1411 | ? | - |
? | |
| 1.1.1.175 | D-xylose + NAD+ | 79% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+) | Haloferax mediterranei | ? | - |
? | |
| 1.1.1.175 | D-xylose + NAD+ | 79% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+) | Haloferax mediterranei DSM 1411 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.1.113 | dimer | 2 * 53000, SDS-PAGE | Haloferax mediterranei |
| 1.1.1.119 | dimer | 2 * 53000, SDS-PAGE | Haloferax mediterranei |
| 1.1.1.175 | dimer | 2 * 53000, SDS-PAGE | Haloferax mediterranei |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.113 | 65 | - |
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations | Haloferax mediterranei |
| 1.1.1.119 | 65 | - |
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations | Haloferax mediterranei |
| 1.1.1.175 | 65 | - |
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations | Haloferax mediterranei |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.119 | NAD+ | Km-value for NAD+ is 50fold higher than Km-value for NADP+ | Haloferax mediterranei | |
| 1.1.1.119 | NADP+ | Km-value for NAD+ is 50fold higher than Km-value for NADP+ | Haloferax mediterranei | |
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