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Literature summary for 1.10.5.1 extracted from
- The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2) (2009), BMC Struct. Biol., 9, 7.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| X-ray crystal structure of NQO2 bound to imatinib to 1.75 A resolution. The X-ray structure provides an explanation for the binding specificity of NQO2 for imatinib and nilotinib, as well as for the effects of mutation of the reported phosphorylation sites on NQO2 | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| imatinib | the structure of the imatinib-NQO2 complex demonstrates that imatinib inhibits NQO2 activity by competing with substrate for the active site | Homo sapiens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P16083 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-carbamoylmethyl-3-carbamoyl-1,4-dihydropyrimidine + menadione | - |
Homo sapiens | 1-carbamoylmethyl-3-carbamoylpyrimidine + menadiol | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NQO2 | - |
Homo sapiens |
| quinone reductase 2 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
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Release 2023.1 (January 2023)
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