Cloned (Comment) | Organism |
---|---|
homologous overexpression of the his-tagged protein in Haloferax volcanii | Haloferax volcanii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.021 | - |
6-phospho-D-gluconate | pH 7.5, 42°C | Haloferax volcanii | |
0.033 | - |
NAD+ | pH 7.5, 42°C | Haloferax volcanii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | highest activity at about 1 M KCl | Haloferax volcanii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37000 | - |
4 * 37000, SDS-PAGE | Haloferax volcanii |
143000 | - |
gel filtration | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-phospho-D-gluconate + NAD+ | Haloferax volcanii | the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? | |
6-phospho-D-gluconate + NAD+ | Haloferax volcanii DSM 3757 | the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GST8 | - |
- |
Haloferax volcanii DSM 3757 | D4GST8 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Haloferax volcanii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-phospho-D-gluconate + NAD+ | - |
Haloferax volcanii | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? | |
6-phospho-D-gluconate + NAD+ | 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 | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? | |
6-phospho-D-gluconate + NAD+ | - |
Haloferax volcanii DSM 3757 | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? | |
6-phospho-D-gluconate + NAD+ | 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 DSM 3757 | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 37000, SDS-PAGE | Haloferax volcanii |
Synonyms | Comment | Organism |
---|---|---|
6PGDH | ambiguous | Haloferax volcanii |
gndA | - |
Haloferax volcanii |
HVO_1830 | locus name | Haloferax volcanii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10.5 | - |
- |
Haloferax volcanii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | the catalytic efficiency (kcat/Km) of the enzyme for NAD+ (174/s*mM) is about 2000fold higher than for NADP+ (0.082/s*mM) defining the enzyme as NAD+ specific | Haloferax volcanii |
General Information | Comment | Organism |
---|---|---|
malfunction | compared to the wild type, the deletion mutant strain DELTAgndA does not grow, but growth is fully recovered by in-trans complementation with gndA. 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 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
174 | - |
NAD+ | pH 7.5, 42°C | Haloferax volcanii |