Ribosyldihydronicotinamide dehydrogenase (quinone)

dihydronicotinamide riboside quinone reductase

Ribosyldihydronicotinamide dehydrogenase dimer, Human

Identifiers
EC no.| 1.10.99.2
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
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KEGG| KEGG entry
MetaCyc| metabolic pathway
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Gene Ontology| AmiGO  / QuickGO
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In enzymology, a ribosyldihydronicotinamide dehydrogenase (quinone) (EC 1.10.99.2) is an enzyme that catalyzes the chemical reaction

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone  ⇌ {\displaystyle \rightleftharpoons } 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone

Thus, the two substrates of this enzyme are 1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide and quinone, whereas its two products are 1-(beta-D-ribofuranosyl)nicotinamide and hydroquinone.

This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with other acceptors. The systematic name of this enzyme class is 1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone oxidoreductase. Other names in common use include NRH:quinone oxidoreductase 2, NQO2, NQO2, NAD(P)H:quinone oxidoreductase-2 (misleading), QR2, quinone reductase 2, N-ribosyldihydronicotinamide dehydrogenase (quinone), and NAD(P)H:quinone oxidoreductase2 (misleading).

## References

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* LIAO S, DULANEY JT, WILLIAMS-ASHMAN HG (1962). "Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide". J. Biol. Chem. 237 (9): 2981–7. doi:10.1016/S0021-9258(18)60260-1. PMID 14465018.
* Zhao Q, Yang XL, Holtzclaw WD, Talalay P (1997). "Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)". Proc. Natl. Acad. Sci. U.S.A. 94 (5): 1669–74. doi:10.1073/pnas.94.5.1669. PMC 19974. PMID 9050836.
* S; Knox, R; Sun, XZ; Joseph, P; Jaiswal, AK; Zhang, D; Deng, PS; Chen, S (1997). "Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase". Arch. Biochem. Biophys. 347 (2): 221–8. doi:10.1006/abbi.1997.0344. PMID 9367528.
* Jaiswal AK (1994). "Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression". J. Biol. Chem. 269 (20): 14502–8. doi:10.1016/S0021-9258(17)36651-6. PMID 8182056.

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Oxidoreductases: diphenol family (EC 1.10)

1.10.1|

* Trans-acenaphthene-1,2-diol dehydrogenase

1.10.2|

* Coenzyme Q - cytochrome c reductase

1.10.3|

* Catechol oxidase
* Laccase

1.10.99|

* Cytochrome b6f complex

Other|

* Alternative oxidase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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