CatLogenzyme kinetics catalog

EC 1.10.5.1: ribosyldihydronicotinamide dehydrogenase (quinone)

OxidoreductasesOpen in Browse

CatLog read 23 records for EC 1.10.5.1 from 2 papers, for 1 organism. Names in these papers: quinone oxidoreductase 2 (QR2), NQO2, hNQO2-hDT43 chimeric enzyme.

Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units.

CatLog also holds 3 records for EC 1.10.5.1 that are not yet re-read: from its earlier version, built from the enzyme databases and partly checked against the papers. All records for EC 1.10.5.1 in Browse.

Papers

PaperOrganismsRecords
Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolinesHomo sapiens15
Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductaseHomo sapiens8

Records

EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsPaper
hNQO2-hDT43 chimeric enzymehNQO2-hDT43 chimeraHomo sapiens2,6-dichlorophenolindophenol91.80.0194.8 × 10³ calc.PMID 9367528Open
NQO2Homo sapiens2,6-dichlorophenolindophenol470.0076.7 × 10³PMID 9367528Open
NQO2Homo sapiens3-(4,5-dimethylthizaol-2-yl)-2,5-diphenyltetrazolium110.012920PMID 9367528Open
NQO2Homo sapiens5-(aziridin-1-yl)-2,4-dinitrobenzamide60.2623pH 7, 37 °CPMID 9367528Open
NQO2Homo sapiensdihydronicotinamide riboside430.0281.58 × 10³PMID 9367528Open
NQO2Homo sapiensmenadione380.00231.7 × 10⁴pH 7.5, 25 °CPMID 9367528Open
NQO2Homo sapiensmethyl red3.80.0047830pH 6.5, 25 °CPMID 9367528Open
NQO2Homo sapiensNADH2.60.25210 calc.PMID 9367528Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadionesimple Michaelis-Menten fit; cosubstrate NMeH (100 µM)2760.00416.7 × 10⁴ calc.pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadionesimple Michaelis-Menten fit; cosubstrate NMeH (100 µM)1890.00355.4 × 10⁴ calc.pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadionecosubstrate NMeH; expressed in E. coli BL-21 as GST fusion—0.0094—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadionecosubstrate NMeH; Table 2—0.0116—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadioneinhibition series with 0; 4; 10; cosubstrate NMeH (60 µM)—0.01—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadioneinhibition series with 0; 4; 10; 20 µM primaquine (Figure 5)—0.011—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensmenadioneinhibition series with 0; 0.5; 2; 5 µM quinacrine (Figure 5)—0.018—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamidesimple Michaelis-Menten fit; cosubstrate menadione (40 µM)2150.0415.2 × 10³ calc.pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamidesimple Michaelis-Menten fit; cosubstrate menadione (40 µM)2010.0171.2 × 10⁴ calc.pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamidecosubstrate menadione; GST removed by thrombin cleavage4620.01792.58 × 10⁴ calc.pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamidecosubstrate menadione; Table 28580.03032.83 × 10⁴ calc.pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamide98——pH 8.5, 4 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamideinhibition series with 0; 4; 10; Table 3—0.023—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamideinhibition series with 0; 4; 10; 20 µM primaquine (Figure 5)—0.013—pH 8.5, 25 °CPMID 15078100Open
quinone oxidoreductase 2 (QR2)Homo sapiensN-methyldihydronicotinamideinhibition series with 0; 0.5; 2; 5 µM quinacrine (Figure 5)—0.02—pH 8.5, 25 °CPMID 15078100Open