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Literature summary for 1.1.1.388 extracted from
- The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase - The archaeal Zwischenferment (2015), FEBS Lett., 589, 1108-1111.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Haloferax volcanii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.18 | - |
NAD+ | pH 7.5, 42°C | Haloferax volcanii |  |
| 5.4 | - |
D-glucose 6-phosphate | pH 7.5, 42°C | Haloferax volcanii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| KCl | highest activity at about 3 M KCl | Haloferax volcanii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 34000 | - |
2 * 34000, SDS-PAGE | Haloferax volcanii |
| 59000 | - |
gel filtration | Haloferax volcanii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose 6-phosphate + NADP+ | Haloferax volcanii | the enzyme is functionally involved in pentose phosphate formation in vivo | 6-phospho-D-glucono-1,5-lactone + NADPH + H+ | - |
? | |
| D-glucose 6-phosphate + NADP+ | Haloferax volcanii DSM 3757 | the enzyme is functionally involved in pentose phosphate formation in vivo | 6-phospho-D-glucono-1,5-lactone + NADPH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax volcanii | D4GS48 | - |
- |
| Haloferax volcanii DSM 3757 | D4GS48 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Haloferax volcanii |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 42 | - |
pH 7.5, 42°C | Haloferax volcanii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose 6-phosphate + NAD+ | the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor | Haloferax volcanii | 6-phospho-D-glucono-1,5-lactone + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NAD+ | the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor | Haloferax volcanii DSM 3757 | 6-phospho-D-glucono-1,5-lactone + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NADP+ | the enzyme is functionally involved in pentose phosphate formation in vivo | Haloferax volcanii | 6-phospho-D-glucono-1,5-lactone + NADPH + H+ | - |
? | |
| D-glucose 6-phosphate + NADP+ | the enzyme is functionally involved in pentose phosphate formation in vivo | Haloferax volcanii DSM 3757 | 6-phospho-D-glucono-1,5-lactone + NADPH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 34000, SDS-PAGE | Haloferax volcanii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| archaeal zwischenferment | - |
Haloferax volcanii |
| azf | - |
Haloferax volcanii |
| Glc6PDH | ambiguous | Haloferax volcanii |
| HVO_0511 | locus name | Haloferax volcanii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.18 | - |
NAD+ | pH 7.5, 42°C | Haloferax volcanii | |
| 5.4 | - |
D-glucose 6-phosphate | pH 7.5, 42°C | Haloferax volcanii | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Haloferax volcanii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | the catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor | Haloferax volcanii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | compared to the wild type, the DELTAazf strain does not grow, but growth was fully recovered by in-trans complementation with azf. Growth of the deletion mutant can also be recovered by the addition of uridine to the medium, suggesting that Haloferax volcanii can circumvent the metabolic block for pentose phosphate formation via the oxidative pentose phosphate pathway by converting uridine to ribose-5-phosphate, catalyzed by uridine phosphorylase and phosphopentomutase | Haloferax volcanii |
| physiological function | the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate | Haloferax volcanii |
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