Cloned (Comment) | Organism |
---|---|
glutathione S-transferase (GST)-tagged enzyme is expressed in Escherichia coli | Synechocystis sp. |
glutathione S-transferase (GST)-tagged Sy6PGDH is expressed in Escherichia coli | Synechocystis sp. |
glutathione S-transferase (GST)-tagged Sy6PGDH is expressed in Escherichia coli | Arthrospira platensis |
Protein Variants | Comment | Organism |
---|---|---|
S42T | amino acid substitution at position 42 from serine to threonine enhances the affinity for NADP+ and alters the mode of inhibition by NADPH from non-competitive (wild-type enzyme) to competitive (mutant enzyme S42T) | Synechocystis sp. |
S42T | the amino acid substitution (S42T) enhances the affinity for NADP+ and alters the mode of inhibition by NADPH | Synechocystis sp. |
T35S | NADPH acts as a competitive inhibitor of NADP+ for the wild-type enzyme and as a non-competitive inhibitor of NADP+ for mutant enzyme T35S | Arthrospira platensis |
T35S | wild-type enzyme shows higher affinity for NADP+ than mutant enzyme T35S | Arthrospira platensis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ATP | 1 mM, 45% inhibition; 1 mM, 55% decreases in activity | Synechocystis sp. | |
citrate | 1 mM, 16% inhibition; 1 mM, 84% decreases in activity | Synechocystis sp. | |
fructose-1,6-bisphosphate | 1 mM, 30% inhibition; 1 mM, 70% decreases in activity | Synechocystis sp. | |
NADPH | competitive inhibitor of NADP+ for wild-type enzyme and non-competitive inhibitor of NADP+ for mutant enzyme T35S; NADPH acts as a competitive inhibitor of NADP+ for the wild-type enzyme and as a non-competitive inhibitor of NADP+ for mutant enzyme T35S | Arthrospira platensis | |
NADPH | 0.2 mM, activity markedly decreases, wild-type enzyme shows non-competitive inhibition, mutant enzyme S42T shows competitive inhibition; non-competitive inhibition of wild-type enzyme. Activity markedly decreases to 14% in the presence of 0.2 mM NADPH. Competitive inhibitor of NADP+ in mutant enzyme S42T | Synechocystis sp. | |
phosphoenolpyruvate | 1 mM, 36% inhibition; 1 mM, 64% decreases in activity | Synechocystis sp. | |
ribose-5-phosphate | 1 mM, 29% inhibition; 1 mM, 71% decreases in activity | Synechocystis sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.015 | - |
NADP+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
0.019 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Arthrospira platensis | |
0.042 | - |
6-phospho-D-gluconate | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
0.042 | - |
NADP+ | pH 7.3, 32°C, mutant enzyme T35S | Arthrospira platensis | |
0.052 | - |
6-phospho-D-gluconate | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
0.058 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
4.46 | - |
NAD+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
6.6 | - |
NAD+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-phospho-D-gluconate + NADP+ | Synechocystis sp. | - |
D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | Arthrospira platensis | - |
D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | Arthrospira platensis NIES-39 | - |
D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arthrospira platensis | D4ZTT4 | - |
- |
Arthrospira platensis NIES-39 | D4ZTT4 | - |
- |
Synechocystis sp. | P52208 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Synechocystis sp. |
- |
Arthrospira platensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-phospho-D-gluconate + NAD+ | the enzyme is specific for NADP+ by approximately 1100-fold compared with its specificity for NAD+ | Synechocystis sp. | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? | |
6-phospho-D-gluconate + NAD+ | the enzyme is specific for NADP+ by approximately 1100fold compared with its specificity for NAD+ | Synechocystis sp. | D-ribulose 5-phosphate + CO2 + NADH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | - |
Synechocystis sp. | D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | - |
Arthrospira platensis | D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | the enzyme is specific for NADP+ by approximately 1100-fold compared with its specificity for NAD+ | Synechocystis sp. | D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | the enzyme is specific for NADP+ by approximately 1100fold compared with its specificity for NAD+ | Synechocystis sp. | D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? | |
6-phospho-D-gluconate + NADP+ | - |
Arthrospira platensis NIES-39 | D-ribulose 5-phosphate + CO2 + NADPH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
6-phosphogluconate dehydrogenase | - |
Synechocystis sp. |
6-phosphogluconate dehydrogenase | - |
Arthrospira platensis |
6PGDH | - |
Synechocystis sp. |
6PGDH | - |
Arthrospira platensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
32 | - |
- |
Synechocystis sp. |
43 | - |
- |
Arthrospira platensis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 45 | 25°C: about 40% of maximal activity, 45°C: about 60% of maximal activity | Synechocystis sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.48 | - |
NAD+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
4.89 | - |
NAD+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
16.6 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Arthrospira platensis | |
24.2 | - |
NADP+ | pH 7.3, 32°C, mutant enzyme T35S | Arthrospira platensis | |
50.6 | - |
NADP+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
51 | - |
6-phospho-D-gluconate | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
64.5 | - |
6-phospho-D-gluconate | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
69.9 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
- |
Synechocystis sp. |
7.8 | - |
- |
Arthrospira platensis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 8 | pH 7.0: about 60% of maximal activity, pH 8.0: about 55% of maximal activity | Synechocystis sp. |
7 | 8 | pH 7.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity | Synechocystis sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | the enzyme is specific for NADP+ by approximately 1100-fold compared with its specificity for NAD+ | Synechocystis sp. | |
NADP+ | the enzyme is specific for NADP+ by approximately 1100fold compared with its specificity for NAD+ | Synechocystis sp. | |
NADP+ | the enzyme is specific for NADP+ by approximately 1100fold compared with its specificity for NAD+ | Arthrospira platensis |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic analysis of cyanobacterial 6-phosphogluconate dehydrogenases (6PGDH) reveals that an amino acid residue at position 42 in Sy6PGDH is highly conserved for each order of cyanobacteria, but Synechocystis 6PGDH (Sy6PGDH) is phylogenetically unique. In Sy6PGDH, a single amino acid substitution at position 42 from serine to threonine enhances the affinity for NADP+ and alters the mode of inhibition by NADPH | Synechocystis sp. |
evolution | phylogenetic analysis of cyanobacterial 6PGDHs reveales that the amino acid residue at position 42 in Sy6PGDH is highly conserved | Synechocystis sp. |
physiological function | in the oxidative pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is one of the enzymes that catalyzes reactions generating NADPH | Synechocystis sp. |
physiological function | in the oxidative pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is one of the enzymes that catalyzes reactions generating NADPH | Arthrospira platensis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.7 | - |
NAD+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
0.74 | - |
NAD+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
1.1 | - |
NAD+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
1.1 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
585 | - |
NADP+ | pH 7.3, 32°C, mutant enzyme T35S | Arthrospira platensis | |
857 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Arthrospira platensis | |
1207 | - |
NADP+ | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
1225 | - |
6-phospho-D-gluconate | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. | |
1239 | - |
6-phospho-D-gluconate | pH 7.3, 32°C, wild-type enzyme | Synechocystis sp. | |
3719 | - |
NADP+ | pH 7.3, 32°C, mutant enzyme S42T | Synechocystis sp. |