EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.1.13 | C18S | mutant of GapB subunit still shows stron redox regulation | Spinacia oleracea |
1.2.1.13 | C274S | mutant of GapB subunit still shows stron redox regulation | Spinacia oleracea |
1.2.1.13 | C285S | mutant of GapB subunit still shows stron redox regulation | Spinacia oleracea |
1.2.1.13 | C349S | mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ | Spinacia oleracea |
1.2.1.13 | C349S/C358S | mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ | Spinacia oleracea |
1.2.1.13 | c358S | mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ | Spinacia oleracea |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.13 | NAD+ | a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity | Spinacia oleracea | |
1.2.1.13 | thioredoxin | a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity | Spinacia oleracea |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.2.1.13 | chloroplast | - |
Spinacia oleracea | 9507 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.13 | Spinacia oleracea | - |
- |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.13 | GAPDH | - |
Spinacia oleracea |