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Literature summary extracted from

  • Winger, J.A.; Hantschel, O.; Superti-Furga, G.; Kuriyan, J.
    The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2) (2009), BMC Struct. Biol., 9, 7.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.10.5.1
-
 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.10.5.1 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

EC Number Inhibitors Comment Organism Structure
1.10.5.1 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

EC Number Organism UniProt Comment Textmining
1.10.5.1 Homo sapiens P16083
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.5.1 1-carbamoylmethyl-3-carbamoyl-1,4-dihydropyrimidine + menadione
-
 Homo sapiens 1-carbamoylmethyl-3-carbamoylpyrimidine + menadiol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.10.5.1 NQO2
-
 Homo sapiens
1.10.5.1 quinone reductase 2
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.5.1 30
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.5.1 7.5
-
 assay at Homo sapiens