Cloned (Comment) | Organism |
---|---|
cloning of the alpha subunit of the enzyme, coexpression in insect cells with the Drosophila protein-disulfide isomerase polypeptide produces an active enzyme tetramer, coexpression in insect cells with human protein-disulfide isomerase polypeptide produces also small amounts of a hybrid tetramer | Drosophila melanogaster |
Protein Variants | Comment | Organism |
---|---|---|
R490H | the mutation reduces the percentage of uncoupled decarboxylation | Drosophila melanogaster |
R490S | the mutation increases the Km for 2-oxoglutarate, reduces the reaction velocity and increases the percentage of uncoupled decarboxylation | Drosophila melanogaster |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
poly(L-proline) | MW: 7000 and 44000 | Drosophila melanogaster | |
poly(L-proline) | MW: 7000 and 44000 | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.021 | - |
(Pro-Pro-Gly)10 | type I enzyme | Homo sapiens | |
0.022 | - |
2-oxoglutarate | type I and type II enzymes | Homo sapiens | |
0.084 | - |
2-oxoglutarate | wild-type enzyme | Drosophila melanogaster | |
0.088 | - |
(Pro-Pro-Gly)10 | type I enzyme | Homo sapiens | |
0.106 | - |
2-oxoglutarate | R490H mutant | Drosophila melanogaster | |
0.106 | - |
2-oxoglutarate | R490S mutant | Drosophila melanogaster | |
0.26 | - |
(L-Pro-L-Pro-Gly)10 | - |
Drosophila melanogaster |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | Km: 0.003 mM | Drosophila melanogaster | |
Fe2+ | type I enzyme: Km 0.003 mM, type II enzyme: Km 0.004 mM | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Drosophila melanogaster | - |
- |
- |
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
larva | - |
Drosophila melanogaster | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Homo sapiens |
additional information | - |
enzyme activity of mutants | Drosophila melanogaster |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2 | - |
Drosophila melanogaster | (L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2 | - |
r | |
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2 | - |
Homo sapiens | ? + succinate + CO2 | - |
? | |
(Pro-Pro-Gly)n + 2-oxoglutarate + O2 | n: 1,5,10 | Drosophila melanogaster | (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 | n: 1,5,10 | ? | |
(Pro-Pro-Gly)n + 2-oxoglutarate + O2 | n: 1,5,10 | Homo sapiens | (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 | n: 1,5,10 | ? |
Subunits | Comment | Organism |
---|---|---|
More | - |
Homo sapiens |
More | amino acid sequence of the alpha subunit and its comparison with those of the human alpha-I and alpha-II subunits and the Caenorhabditis elegans alpha subunit | Drosophila melanogaster |
tetramer | - |
Homo sapiens |
tetramer | the alpha subunit forms enzyme alpha2 beta2 tetramers with the Drosophila and human protein-disulfide isomerase polypeptides, nondenaturing-PAGE and Coomassie Blue-staining | Drosophila melanogaster |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ascorbate | Km: 0.3 mM | Drosophila melanogaster | |
ascorbate | type I enzyme: Km 0.32 mM, type II enzyme: Km 0.34 mM | Homo sapiens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00002 | - |
poly(L-proline) | MW: 44000, human type I enzyme | Homo sapiens | |
0.0006 | - |
poly(L-proline) | MW: 7000, human type I enzyme | Homo sapiens | |
0.0029 | - |
poly(L-proline) | MW: 44000 | Drosophila melanogaster | |
0.018 | - |
poly(L-proline) | MW: 7000 | Drosophila melanogaster | |
0.022 | - |
poly(L-proline) | MW: 44000, human type II enzyme | Homo sapiens | |
0.095 | - |
poly(L-proline) | MW: 7000, type II enzyme | Homo sapiens |