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Literature summary extracted from

  • Ito, S.; Osanai, T.
    Single amino acid change in 6-phosphogluconate dehydrogenase from Synechocystis conveys higher affinity for NADP+ and altered mode of inhibition by NADPH (2018), Plant Cell Physiol., 59, 2452-2461 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.44 glutathione S-transferase (GST)-tagged enzyme is expressed in Escherichia coli Synechocystis sp.
1.1.1.44 glutathione S-transferase (GST)-tagged Sy6PGDH is expressed in Escherichia coli Synechocystis sp.
1.1.1.44 glutathione S-transferase (GST)-tagged Sy6PGDH is expressed in Escherichia coli Arthrospira platensis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.44 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.
1.1.1.44 S42T the amino acid substitution (S42T) enhances the affinity for NADP+ and alters the mode of inhibition by NADPH Synechocystis sp.
1.1.1.44 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
1.1.1.44 T35S wild-type enzyme shows higher affinity for NADP+ than mutant enzyme T35S Arthrospira platensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.44 ATP 1 mM, 45% inhibition; 1 mM, 55% decreases in activity Synechocystis sp.
1.1.1.44 citrate 1 mM, 16% inhibition; 1 mM, 84% decreases in activity Synechocystis sp.
1.1.1.44 fructose-1,6-bisphosphate 1 mM, 30% inhibition; 1 mM, 70% decreases in activity Synechocystis sp.
1.1.1.44 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
1.1.1.44 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.
1.1.1.44 phosphoenolpyruvate 1 mM, 36% inhibition; 1 mM, 64% decreases in activity Synechocystis sp.
1.1.1.44 ribose-5-phosphate 1 mM, 29% inhibition; 1 mM, 71% decreases in activity Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.44 0.015
-
 NADP+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 0.019
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Arthrospira platensis
1.1.1.44 0.042
-
 6-phospho-D-gluconate pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 0.042
-
 NADP+ pH 7.3, 32°C, mutant enzyme T35S Arthrospira platensis
1.1.1.44 0.052
-
 6-phospho-D-gluconate pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 0.058
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 4.46
-
 NAD+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 6.6
-
 NAD+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.44 6-phospho-D-gluconate + NADP+ Synechocystis sp.
-
 D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?
1.1.1.44 6-phospho-D-gluconate + NADP+ Arthrospira platensis
-
 D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?
1.1.1.44 6-phospho-D-gluconate + NADP+ Arthrospira platensis NIES-39
-
 D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.44 Arthrospira platensis D4ZTT4
-
-
1.1.1.44 Arthrospira platensis NIES-39 D4ZTT4
-
-
1.1.1.44 Synechocystis sp. P52208
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.44
-
 Synechocystis sp.
1.1.1.44
-
 Arthrospira platensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.44 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+
-
 ?
1.1.1.44 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+
-
 ?
1.1.1.44 6-phospho-D-gluconate + NADP+
-
 Synechocystis sp. D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?
1.1.1.44 6-phospho-D-gluconate + NADP+
-
 Arthrospira platensis D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?
1.1.1.44 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+
-
 ?
1.1.1.44 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+
-
 ?
1.1.1.44 6-phospho-D-gluconate + NADP+
-
 Arthrospira platensis NIES-39 D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.44 6-phosphogluconate dehydrogenase
-
 Synechocystis sp.
1.1.1.44 6-phosphogluconate dehydrogenase
-
 Arthrospira platensis
1.1.1.44 6PGDH
-
 Synechocystis sp.
1.1.1.44 6PGDH
-
 Arthrospira platensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.44 32
-
-
 Synechocystis sp.
1.1.1.44 43
-
-
 Arthrospira platensis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.44 25 45 25°C: about 40% of maximal activity, 45°C: about 60% of maximal activity Synechocystis sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.44 4.48
-
 NAD+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 4.89
-
 NAD+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 16.6
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Arthrospira platensis
1.1.1.44 24.2
-
 NADP+ pH 7.3, 32°C, mutant enzyme T35S Arthrospira platensis
1.1.1.44 50.6
-
 NADP+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 51
-
 6-phospho-D-gluconate pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 64.5
-
 6-phospho-D-gluconate pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 69.9
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.44 7.3
-
-
 Synechocystis sp.
1.1.1.44 7.8
-
-
 Arthrospira platensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.44 7 8 pH 7.0: about 60% of maximal activity, pH 8.0: about 55% of maximal activity Synechocystis sp.
1.1.1.44 7 8 pH 7.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.44 NADP+ the enzyme is specific for NADP+ by approximately 1100-fold compared with its specificity for NAD+ Synechocystis sp.
1.1.1.44 NADP+ the enzyme is specific for NADP+ by approximately 1100fold compared with its specificity for NAD+ Synechocystis sp.
1.1.1.44 NADP+ the enzyme is specific for NADP+ by approximately 1100fold compared with its specificity for NAD+ Arthrospira platensis

General Information

EC Number General Information Comment Organism
1.1.1.44 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.
1.1.1.44 evolution phylogenetic analysis of cyanobacterial 6PGDHs reveales that the amino acid residue at position 42 in Sy6PGDH is highly conserved Synechocystis sp.
1.1.1.44 physiological function in the oxidative pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is one of the enzymes that catalyzes reactions generating NADPH Synechocystis sp.
1.1.1.44 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.44 0.7
-
 NAD+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 0.74
-
 NAD+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 1.1
-
 NAD+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 1.1
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 585
-
 NADP+ pH 7.3, 32°C, mutant enzyme T35S Arthrospira platensis
1.1.1.44 857
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Arthrospira platensis
1.1.1.44 1207
-
 NADP+ pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 1225
-
 6-phospho-D-gluconate pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.
1.1.1.44 1239
-
 6-phospho-D-gluconate pH 7.3, 32°C, wild-type enzyme Synechocystis sp.
1.1.1.44 3719
-
 NADP+ pH 7.3, 32°C, mutant enzyme S42T Synechocystis sp.