DB code: S00343
| CATH domain | 3.40.50.360 : Rossmann fold | Catalytic domain |
|---|---|---|
| E.C. | 1.6.5.2 | |
| CSA | 1d4a | |
| M-CSA | 1d4a | |
| MACiE | M0003 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.50.360 : Rossmann fold | S00522 M00006 M00154 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P15559 |
NAD(P)H dehydrogenase [quinone] 1
|
EC
1.6.5.2
Quinone reductase 1 NAD(P)H:quinone oxidoreductase 1 QR1 DT-diaphorase DTD Azoreductase Phylloquinone reductase Menadione reductase |
NP_000894.1
(Protein)
NM_000903.2 (DNA/RNA sequence) NP_001020604.1 (Protein) NM_001025433.1 (DNA/RNA sequence) NP_001020605.1 (Protein) NM_001025434.1 (DNA/RNA sequence) |
PF02525
(Flavodoxin_2)
[Graphical View] |
| Q64669 |
NAD(P)H dehydrogenase [quinone] 1
|
EC
1.6.5.2
Quinone reductase 1 NAD(P)H:quinone oxidoreductase 1 QR1 DT-diaphorase DTD Azoreductase Phylloquinone reductase Menadione reductase |
NP_032732.3
(Protein)
NM_008706.5 (DNA/RNA sequence) |
PF02525
(Flavodoxin_2)
[Graphical View] |
| P05982 |
NAD(P)H dehydrogenase [quinone] 1
|
EC
1.6.5.2
Quinone reductase 1 NAD(P)H:quinone oxidoreductase 1 QR1 DT-diaphorase DTD Azoreductase Phylloquinone reductase Menadione reductase |
NP_058696.2
(Protein)
NM_017000.3 (DNA/RNA sequence) |
PF02525
(Flavodoxin_2)
[Graphical View] |
| KEGG enzyme name |
|---|
|
NAD(P)H dehydrogenase (quinone)
menadione reductase phylloquinone reductase quinone reductase dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,quinone) DT-diaphorase flavoprotein NAD(P)H-quinone reductase menadione oxidoreductase NAD(P)H dehydrogenase NAD(P)H menadione reductase NAD(P)H-quinone dehydrogenase NAD(P)H-quinone oxidoreductase NAD(P)H: (quinone-acceptor)oxidoreductase NAD(P)H: menadione oxidoreductase NADH-menadione reductase naphthoquinone reductase p-benzoquinone reductase reduced NAD(P)H dehydrogenase viologen accepting pyridine nucleotide oxidoreductase vitamin K reductase diaphorase reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase vitamin-K reductase NAD(P)H2 dehydrogenase (quinone) NQO1 QR1 NAD(P)H:(quinone-acceptor) oxidoreductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P15559 | NQO1_HUMAN | NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone. | Homodimer. | Cytoplasm. | FAD. |
| Q64669 | NQO1_MOUSE | NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone. | Homodimer (By similarity). | Cytoplasm. | FAD. |
| P05982 | NQO1_RAT | NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone. | Homodimer. | Cytoplasm. | FAD. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00100 | Biosynthesis of steroids |
| Compound table | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||||
| KEGG-id | C00016 | C00038 | C00005 | C00004 | C00080 | C00472 | C00006 | C00003 | C00530 | ||||||
| E.C. | |||||||||||||||
| Compound | FAD | Zinc | NADPH | NADH | H+ | Quinone | NADP+ | NAD+ | Hydroquinone | ||||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | heavy metal | amide group,amine group,nucleotide | amide group,amine group,nucleotide | others | aromatic ring (only carbon atom) | amide group,amine group,nucleotide | amide group,amine group,nucleotide | aromatic ring (only carbon atom) | ||||||
| ChEBI |
16238 16238 |
29105 29105 |
16474 16474 |
16908 16908 |
15378 15378 |
16509 16509 |
18009 18009 |
15846 15846 |
17594 17594 |
||||||
| PubChem |
643975 643975 |
32051 32051 |
5884 5884 |
439153 439153 |
1038 1038 |
4650 4650 |
5886 5886 |
5893 5893 |
785 785 |
||||||
| 1d4aA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d4aB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d4aC |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d4aD |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dxoA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:DQN | Unbound | Unbound | Unbound | ||
| 1dxoB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:DQN | Unbound | Unbound | Unbound | ||
| 1dxoC |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:2xDQN | Unbound | Unbound | Unbound | ||
| 1dxoD |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dxqA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dxqB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dxqC |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dxqD |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gg5A |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:E09 | Unbound | Unbound | Unbound | ||
| 1gg5B |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:E09 | Unbound | Unbound | Unbound | ||
| 1gg5C |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:E09 | Unbound | Unbound | Unbound | ||
| 1gg5D |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:E09 | Unbound | Unbound | Unbound | ||
| 1h66A |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:RH1 | Unbound | Unbound | Unbound | ||
| 1h66B |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:RH1 | Unbound | Unbound | Unbound | ||
| 1h66C |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:RH1 | Unbound | Unbound | Unbound | ||
| 1h66D |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:RH1 | Unbound | Unbound | Unbound | ||
| 1h69A |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:ARH | Unbound | Unbound | Unbound | ||
| 1h69B |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:ARH | Unbound | Unbound | Unbound | ||
| 1h69C |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:ARH | Unbound | Unbound | Unbound | ||
| 1h69D |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:ARH | Unbound | Unbound | Unbound | ||
| 1kboA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:340 | Unbound | Unbound | Unbound | ||
| 1kboB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:340 | Unbound | Unbound | Unbound | ||
| 1kboC |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:340 | Unbound | Unbound | Unbound | ||
| 1kboD |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:340 | Unbound | Unbound | Unbound | ||
| 1kbqA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:936 | Unbound | Unbound | Unbound | ||
| 1kbqB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:936 | Unbound | Unbound | Unbound | ||
| 1kbqC |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:936 | Unbound | Unbound | Unbound | ||
| 1kbqD |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:936 | Unbound | Unbound | Unbound | ||
| 1qbgA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1qbgB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1qbgC |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1qbgD |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1qrdA |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:DQN | Unbound | Unbound | Unbound | ||
| 1qrdB |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Analogue:DQN | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| PDB;1h66 & literature [3] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1d4aA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1d4aB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1d4aC |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1d4aD |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxoA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxoB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxoC |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxoD |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxqA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxqB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxqC |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1dxqD |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1gg5A |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1gg5B |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1gg5C |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1gg5D |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h66A |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h66B |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h66C |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h66D |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h69A |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h69B |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h69C |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1h69D |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kboA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kboB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kboC |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kboD |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kbqA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kbqB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kbqC |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1kbqD |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1qbgA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1qbgB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1qbgC |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1qbgD |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1qrdA |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| 1qrdB |
|
|
|
|
|
GLY 149;TYR 155;HIS 161 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
|
Fig.8, p.8849-8850 | |
|
[6]
|
p.612-614 | |
|
[7]
|
p.9985-9986 | |
|
[10]
|
p.278-279 | |
|
[13]
|
Fig.1, Fig.4, p.130-131 | |
|
[14]
|
p.244 | |
|
[15]
|
p.664-665 | |
|
[19]
|
Fig.8 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1510975 |
| Journal | Biochemistry |
| Year | 1992 |
| Volume | 31 |
| Pages | 7879-85 |
| Authors | Siegel D, Beall H, Senekowitsch C, Kasai M, Arai H, Gibson NW, Ross D |
| Title | Bioreductive activation of mitomycin C by DT-diaphorase. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7530954 |
| Journal | Biochem Pharmacol |
| Year | 1995 |
| Volume | 49 |
| Pages | 127-40 |
| Authors | Cadenas E |
| Title | Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 7568029 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1995 |
| Volume | 92 |
| Pages | 8846-50 |
| Authors | Li R, Bianchet MA, Talalay P, Amzel LM |
| Title |
The three-dimensional structure of NAD(P)H:quinone reductase, |
| Related PDB | 1qrd |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8999809 |
| Journal | J Biol Chem |
| Year | 1997 |
| Volume | 272 |
| Pages | 1437-9 |
| Authors | Chen S, Knox R, Wu K, Deng PS, Zhou D, Bianchet MA, Amzel LM |
| Title |
Molecular basis of the catalytic differences among DT-diaphorase of human, |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9050836 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1997 |
| Volume | 94 |
| Pages | 1669-74 |
| Authors | Zhao Q, Yang XL, Holtzclaw WD, Talalay P |
| Title | Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase). |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10917652 |
| Journal | Biochem Soc Trans |
| Year | 1999 |
| Volume | 27 |
| Pages | 610-5 |
| Authors | Bianchet MA, Foster C, Faig M, Talalay P, Amzel LM |
| Title | Structure and mechanism of cytosolic quinone reductases. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10433694 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 9881-6 |
| Authors | Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM |
| Title |
Crystal structure of human quinone reductase type 2, |
| Related PDB | 1qr2 2qr2 |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10543876 |
| Journal | J Med Chem |
| Year | 1999 |
| Volume | 42 |
| Pages | 4325-30 |
| Authors | Skelly JV, Sanderson MR, Suter DA, Baumann U, Read MA, Gregory DS, Bennett M, Hobbs SM, Neidle S |
| Title | Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954). |
| Related PDB | 1qbg |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10419545 |
| Journal | Mol Pharmacol |
| Year | 1999 |
| Volume | 56 |
| Pages | 272-8 |
| Authors | Chen S, Wu K, Zhang D, Sherman M, Knox R, Yang CS |
| Title |
Molecular characterization of binding of substrates and inhibitors to DT-diaphorase: combined approach involving site-directed mutagenesis, |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11035256 |
| Journal | Free Radic Biol Med |
| Year | 2000 |
| Volume | 29 |
| Pages | 276-84 |
| Authors | Chen S, Wu K, Knox R |
| Title | Structure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2). |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10877993 |
| Journal | Front Biosci |
| Year | 2000 |
| Volume | 5 |
| Pages | D639-48 |
| Authors | Beall HD, Winski SI |
| Title |
Mechanisms of action of quinone-containing alkylating agents. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| Medline ID | 20202608 |
| PubMed ID | 10706635 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 2000 |
| Volume | 97 |
| Pages | 3177-82 |
| Authors | Faig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM |
| Title | Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. |
| Related PDB | 1d4a 1dxo 1dxq |
| Related UniProtKB | P15559 |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10694883 |
| Journal | Trends Biochem Sci |
| Year | 2000 |
| Volume | 25 |
| Pages | 126-32 |
| Authors | Fraaije MW, Mattevi A |
| Title | Flavoenzymes: diverse catalysts with recurrent features. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11035252 |
| Journal | Free Radic Biol Med |
| Year | 2000 |
| Volume | 29 |
| Pages | 241-5 |
| Authors | Foster CE, Bianchet MA, Talalay P, Faig M, Amzel LM |
| Title | Structures of mammalian cytosolic quinone reductases. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 11587640 |
| Journal | Structure (Camb) |
| Year | 2001 |
| Volume | 9 |
| Pages | 659-67 |
| Authors | Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM |
| Title | Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones. |
| Related PDB | 1gg5 1h66 1h69 |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 11735396 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 15135-42 |
| Authors | Winski SL, Faig M, Bianchet MA, Siegel D, Swann E, Fung K, Duncan MW, Moody CJ, Amzel LM, Ross D |
| Title |
Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, |
| Related PDB | 1kbo 1kbq |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11340659 |
| Journal | Proteins |
| Year | 2001 |
| Volume | 43 |
| Pages | 420-32 |
| Authors | Cavelier G, Amzel LM |
| Title | Mechanism of NAD(P)H:quinone reductase: Ab initio studies of reduced flavin. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12147263 |
| Journal | Arch Biochem Biophys |
| Year | 2002 |
| Volume | 404 |
| Pages | 254-62 |
| Authors | Anusevicius Z, Sarlauskas J, Cenas N |
| Title | Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15078100 |
| Journal | Biochemistry |
| Year | 2004 |
| Volume | 43 |
| Pages | 4538-47 |
| Authors | Kwiek JJ, Haystead TA, Rudolph J |
| Title | Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
| Created | Updated |
|---|---|
| 2004-10-26 | 2009-02-26 |