EC Number | Cloned (Comment) | Organism |
---|---|---|
1.18.1.2 | expression in Escherichia coli | Escherichia coli |
1.18.1.2 | expression in Escherichia coli | Pisum sativum |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.18.1.2 | mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed | Escherichia coli |
1.18.1.2 | mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed | Pisum sativum |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.18.1.2 | additional information | mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. The plastidic enzyme lacking the beta-hairpin is unable to fold properly. An extra tryptophan at the carboxy terminus, emulating the bacterial enzyme, results in an enzyme with decreased affinity for FAD and reduced diaphorase and ferredoxin-dependent cytochrome c reductase activities. The insertion of the beta-hairpin into the corresponding position of the bacterial enzyme increases FAD affinity but does not affect its catalytic properties. The same insertion with simultaneous deletion of the carboxyterminal tryptophan produces a bacterial chimera emulating the plastidic architecture with an increased kcat and an increased catalytic efficiency for the diaphorase activity and a decrease in the enzyme's ability to react with its substrates ferredoxin and flavodoxin. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed | Pisum sativum |
1.18.1.2 | additional information | mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. The plastidic enzyme lacking the beta-hairpin is unable to fold properly. An extra tryptophan at the carboxy terminus, emulating the bacterial enzyme, results in an enzyme with decreased affinity for FAD and reduced diaphorase and ferredoxin-dependent cytochrome c reductase activities. The insertion of the beta-hairpin into the corresponding position of the bacterial enzyme increases FAD affinity but does not affect its catalytic properties. The same insertion with simultaneous deletion of the carboxyterminal tryptophan produces a bacterial chimera emulating the plastidic architecture with an increased kcat and an increased catalytic efficiency for the diaphorase activity and a decrease in the enzymes ability to react with its substrates ferredoxin and flavodoxin. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.1.2 | 0.0009 | - |
oxidized ferredoxin | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0009 | - |
oxidized ferredoxin | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0014 | - |
oxidized ferredoxin | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0018 | - |
oxidized ferredoxin | mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0022 | - |
oxidized ferredoxin | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0024 | - |
NADPH | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.003 | - |
NADPH | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.003 | - |
NADH | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0036 | - |
NADPH | mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0037 | - |
NADH | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0059 | - |
NADH | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0062 | - |
oxidized ferredoxin | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0065 | - |
NADH | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0076 | - |
oxidized ferredoxin | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0083 | - |
NADPH | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 0.0143 | - |
NADH | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0147 | - |
NADPH | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0153 | - |
NADPH | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.0207 | - |
NADPH | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.18.1.2 | plastid | - |
Pisum sativum | 9536 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.1.2 | Escherichia coli | P28861 | - |
- |
1.18.1.2 | Pisum sativum | P10933 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.1.2 | 2 ferricytochrome c2 + NADPH | - |
Escherichia coli | 2 ferrocytochrome c2 + NADP+ + H+ | - |
? | |
1.18.1.2 | 2 ferricytochrome c2 + NADPH | - |
Pisum sativum | 2 ferrocytochrome c2 + NADP+ + H+ | - |
? | |
1.18.1.2 | 2 ferrocytochrome c + NAD+ + H+ | NADH, poor substrate | Escherichia coli | 2 ferricytochrome c + NADH | - |
? | |
1.18.1.2 | 2 ferrocytochrome c + NAD+ + H+ | NADH, poor substrate | Pisum sativum | 2 ferricytochrome c + NADH | - |
? | |
1.18.1.2 | 2 oxidized ferredoxin + NADH + H+ | NADH, poor substrate | Escherichia coli | 2 reduced ferredoxin + NAD+ | - |
? | |
1.18.1.2 | 2 oxidized ferredoxin + NADH + H+ | NADH, poor substrate | Pisum sativum | 2 reduced ferredoxin + NAD+ | - |
? | |
1.18.1.2 | 2 oxidized ferredoxin + NADPH + H+ | source of ferredoxin: Pisum sativum | Escherichia coli | 2 reduced ferredoxin + NADP+ | - |
? | |
1.18.1.2 | 2 oxidized ferredoxin + NADPH + H+ | source of ferredoxin: Pisum sativum | Pisum sativum | 2 reduced ferredoxin + NADP+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.18.1.2 | FNR | - |
Escherichia coli |
1.18.1.2 | PETH | - |
Pisum sativum |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.1.2 | 2 | - |
NADH | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 3.7 | - |
oxidized ferredoxin | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 4.6 | - |
oxidized ferredoxin | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 5 | - |
NADH | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 7 | - |
NADH | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 19.4 | - |
oxidized ferredoxin | mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 22.8 | - |
oxidized ferredoxin | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 24.5 | - |
NADPH | mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 32.7 | - |
oxidized ferredoxin | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 35.9 | - |
oxidized ferredoxin | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 38.2 | - |
NADPH | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 45.3 | - |
NADH | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 54.1 | - |
NADH | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 75 | - |
oxidized ferredoxin | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 95.5 | - |
NADPH | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 99 | - |
NADPH | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 251.1 | - |
NADPH | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 360.5 | - |
NADPH | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 374.3 | - |
NADPH | wild-type, pH 8.0, 30°C | Pisum sativum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.18.1.2 | NADH | ratio NADPH/NADH is 49000 | Escherichia coli | |
1.18.1.2 | NADH | ratio NADPH/NADH is 49000 | Pisum sativum | |
1.18.1.2 | NADPH | ratio NADPH/NADH is 49000 | Escherichia coli | |
1.18.1.2 | NADPH | ratio NADPH/NADH is 49000 | Pisum sativum |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.1.2 | 0.5 | - |
NADH | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.6 | - |
NADH | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 0.8 | - |
NADH | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 8 | - |
NADH | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 15 | - |
NADH | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 500 | - |
oxidized ferredoxin | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 740 | - |
oxidized ferredoxin | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 1700 | - |
NADPH | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 4600 | - |
NADPH | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 6800 | - |
NADPH | mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 10700 | - |
oxidized ferredoxin | mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 16300 | - |
oxidized ferredoxin | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 17100 | - |
NADPH | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 24500 | - |
NADPH | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 33000 | - |
NADPH | mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 34100 | - |
oxidized ferredoxin | wild-type, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 36300 | - |
oxidized ferredoxin | mutant lacking the beta-hairpin, pH 8.0, 30°C | Pisum sativum | |
1.18.1.2 | 39800 | - |
NADPH | mutant DELTAW248, pH 8.0, 30°C | Escherichia coli | |
1.18.1.2 | 39800 | - |
oxidized ferredoxin | mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C | Pisum sativum |