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Literature summary extracted from

  • Leung, K.K.; Shilton, B.H.
    Chloroquine binding reveals flavin redox switch function of quinone reductase 2 (2013), J. Biol. Chem., 288, 11242-11251.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.10.5.1 purified NQO2 in complex with primaquine and chloroquine, hanging drop vapor diffusion method, against reservoirs containing 0.1 M HEPES, pH 7.5, and 1.3-2.0 M (NH4)2SO4, crystals of NQO2-CQ are soaked in 0.001 ml of reducing-soak solution consisting of 0.1 M HEPES, pH 7.5, 2.0 M (NH4)2SO4, 10 mM 1-(3-sulfonatopropyl)-3-carbamoyl-1,4-dihydropyrimidine and 1 mM chloroquine, X-ray diffraction structure determination and analysis at 1.2-1.4 A resolution Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.5.1 Chloroquine binds preferentially to reduced NQO2, binding mode, closure of a flexible loop (Phe126-Leu136) over the active site, overview Homo sapiens
1.10.5.1 primaquine binding mode, overview Homo sapiens

Organism

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.10.5.1 FAD flavin redox switch, structural changes, overview Homo sapiens

General Information

EC Number General Information Comment Organism
1.10.5.1 physiological function quinone reductase 2 is an FAD-linked enzyme and the only known human target of two antimalarial drugs, primaquine and chloroquine, a functional role for NQO2 as a flavin redox switch Homo sapiens