Unknown

Dataset Information

0

Quinone reductase 2 is a catechol quinone reductase.


ABSTRACT: The functions of quinone reductase 2 have eluded researchers for decades even though a genetic polymorphism is associated with various neurological disorders. Employing enzymatic studies using adrenochrome as a substrate, we show that quinone reductase 2 is specific for the reduction of adrenochrome, whereas quinone reductase 1 shows no activity. We also solved the crystal structure of quinone reductase 2 in complexes with dopamine and adrenochrome, two compounds that are structurally related to catecholamine quinones. Detailed structural analyses delineate the mechanism of quinone reductase 2 specificity toward catechol quinones in comparison with quinone reductase 1; a side-chain rotational difference between quinone reductase 1 and quinone reductase 2 of a single residue, phenylalanine 106, determines the specificity of enzymatic activities. These results infer functional differences between two homologous enzymes and indicate that quinone reductase 2 could play important roles in the regulation of catecholamine oxidation processes that may be involved in the etiology of Parkinson disease.

SUBMITTER: Fu Y 

PROVIDER: S-EPMC2527206 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Quinone reductase 2 is a catechol quinone reductase.

Fu Yue Y   Buryanovskyy Leonid L   Zhang Zhongtao Z  

The Journal of biological chemistry 20080624 35


The functions of quinone reductase 2 have eluded researchers for decades even though a genetic polymorphism is associated with various neurological disorders. Employing enzymatic studies using adrenochrome as a substrate, we show that quinone reductase 2 is specific for the reduction of adrenochrome, whereas quinone reductase 1 shows no activity. We also solved the crystal structure of quinone reductase 2 in complexes with dopamine and adrenochrome, two compounds that are structurally related to  ...[more]

Similar Datasets

2023-08-15 | PXD033944 | Pride
| S-EPMC101880 | biostudies-literature
| S-EPMC3538594 | biostudies-literature
| S-EPMC6633588 | biostudies-literature
| S-EPMC3650734 | biostudies-literature
| S-EPMC3149192 | biostudies-literature
| S-EPMC3630856 | biostudies-literature
| S-EPMC9218516 | biostudies-literature
| S-EPMC2730739 | biostudies-literature
| S-EPMC2291545 | biostudies-literature