1.6.5.10: NADPH dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about NADPH dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.6.5.10
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1.6.5.10
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neutrophil
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endothelial
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p47phox
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phagocyte
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apocynin
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dismutase
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artery
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gp91phox
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cardiovascular
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nicotinamide
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hypertension
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angiotensin
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catalase
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oxidases
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cardiac
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leukocyte
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phorbol
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monocyte
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mapks
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sod
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aortic
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granulomatous
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diphenyleneiodonium
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diphenylene
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pma
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iodonium
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rac1
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atherosclerosis
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chemiluminescence
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phagocytosis
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xanthine
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polymorphonuclear
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myristate
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microglial
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myeloperoxidase
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ii-induced
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dihydroethidium
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endothelium-dependent
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flavocytochrome
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zymosan
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peroxynitrite
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phagosomes
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tempol
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fmlp
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ros-dependent
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microbicidal
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nadph-oxidase
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nitrotyrosine
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lucigenin
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medicine
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fmlp-induced
- 1.6.5.10
- neutrophil
- endothelial
- p47phox
- phagocyte
- apocynin
- dismutase
- artery
- gp91phox
- cardiovascular
- nicotinamide
- hypertension
- angiotensin
- catalase
- oxidases
- cardiac
- leukocyte
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phorbol
- monocyte
- mapks
- sod
- aortic
- granulomatous
- diphenyleneiodonium
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diphenylene
- pma
- iodonium
- rac1
- atherosclerosis
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chemiluminescence
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phagocytosis
- xanthine
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polymorphonuclear
- myristate
- microglial
- myeloperoxidase
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ii-induced
- dihydroethidium
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endothelium-dependent
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flavocytochrome
- zymosan
- peroxynitrite
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phagosomes
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tempol
- fmlp
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ros-dependent
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microbicidal
- nadph-oxidase
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nitrotyrosine
- lucigenin
- medicine
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fmlp-induced
Reaction
Synonyms
AKR1C9, ArsH, azoreductase, CBR4, dehydrogenase, reduced nicotinamide adenine dinucleotide phosphate (quinone), EC 1.6.99.6, MdaB, More, NADPH oxidase, NADPH quinone oxidoreductase, NADPH quinone oxidoreductase 1, NADPH quinone reductase, NADPH-dependent quinone reductase, NADPH-quinone oxidoreductase, NADPH:quinone oxidoreductase 1, NQO1, PA1225, PpAzoR, XAC2229, Zta1p
ECTree
Advanced search results
Engineering
Engineering on EC 1.6.5.10 - NADPH dehydrogenase (quinone)
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P187S
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Pro187Ser polymorphism in NQO1 has a limited role in the development of Tardive dyskinesia (a potentially irreversible side effect of antipsychotic medication treatment that occurs in approximately 25% of chronically treated schizophrenia patients)
Q192R
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant B1G6
Q192R/A46P/V159A
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 16B7
Q192R/A46P/V159A/A48P
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site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 2A1
Q192R/A46P/V159A/C129S
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site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 23C10
Q192R/A46P/V159A/C129S/A178D/A31S/K74E/A88G/L143Q
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site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 2F11
Q192R/A46P/V159A/C129S/A178D/A77T/F98L/N131D
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site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 3B9
Q192R/A46P/V159A/C129S/A178D/A88G/N131D/L143Q
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site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 1B6
Q192R/A46P/V159A/C129S/A178D/K74E/L143Q
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site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 2E4
Q192R/A46P/V159A/C129S/A178D/N131D/L143Q
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site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 6F11
Q192R/A46P/V159A/C129S/A77T/N131D
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 14D4
Q192R/A46P/V159A/C129S/D7H/A178D
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 13G10
Q192R/A46P/V159A/C129S/E36D/L143Q
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 1C11
Q192R/A46P/V159A/C129S/I6V/T79R/Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 32F5
Q192R/A46P/V159A/C129S/K74E/A88G
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 23C5
Q192R/A46P/V159A/C129S/L161M/L169P
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 27E4
Q192R/A46P/V159A/C129S/N14D/L143Q
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 6F10
Q192R/A46P/V159A/C129S/Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 23E4
Q192R/A46P/V159A/Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 19E4
Q192R/Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 12B8
Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant K7E3
Q192R
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant B1G6
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Q192R/A46P/V159A
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 16B7
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Q192R/Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 12B8
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Y179H
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site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant K7E3
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Y55F
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
Y55S
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
additional information
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improvement of the kinetic and thermodynamic stability of the azoreductase by directed evolution via rational design approaches, five rounds of mutagenesis/recombination are followed by high-throughput screening. Mutant 1B6 shows a 300fold higher half-life at 50°C compared to the wild-type enzyme. mutant 1B6 has a folded state slightly less stable than the wild-type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant is therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturb hydrophobic patches and increase the surface net charge of the protein. Mutants 2A1 and 2A1-Y179H show increased thermodynamic stability with a 10-20°C higher melting temperature than wild-type, these residues are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state. Molecular details of mutations that improve stability, overview
additional information
-
improvement of the kinetic and thermodynamic stability of the azoreductase by directed evolution via rational design approaches, five rounds of mutagenesis/recombination are followed by high-throughput screening. Mutant 1B6 shows a 300fold higher half-life at 50°C compared to the wild-type enzyme. mutant 1B6 has a folded state slightly less stable than the wild-type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant is therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturb hydrophobic patches and increase the surface net charge of the protein. Mutants 2A1 and 2A1-Y179H show increased thermodynamic stability with a 10-20°C higher melting temperature than wild-type, these residues are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state. Molecular details of mutations that improve stability, overview
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