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Literature summary extracted from

  • Mano, J.; Babiychuk, E.; Belles-Boix, E.; Hiratake, J.; Kimura, A.; Inze, D.; Kushnir, S.; Asada, K.
    A novel NADPH:diamide oxidoreductase activity in Arabidopsis thaliana P1 zeta-crystallin (2000), Eur. J. Biochem., 267, 3661-3671.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.5.5 expressed in Escherichia coli Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.5.5 4-chloromercuribenzoate both NADPH and NADP1 suppress the inhibition, but NADH does not Arabidopsis thaliana
1.6.5.5 dicoumarol mixed-type inhibition against NADPH Arabidopsis thaliana
1.6.5.5 N-ethylmaleimide both NADPH and NADP1 suppress the inhibition, but NADH does not Arabidopsis thaliana
1.6.5.5 Nitrofurantoin uncompetitive against NADPH Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.5.5 0.00065
-
 9,10-phenanthrenequinone pH 7.5 Arabidopsis thaliana
1.6.5.5 0.0025
-
 NADPH pH 7.5, cosubstrate: 9,10-phenanthrenequinone Arabidopsis thaliana
1.6.5.5 0.011
-
 5-hydroxy-1,4-naphthoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 0.013
-
 9,10-phenanthrenequinone pH 7.5 Cavia porcellus
1.6.5.5 0.02
-
 Ferricytochrome pH 7.5 Arabidopsis thaliana
1.6.5.5 0.025
-
 decyl-plastoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 0.027
-
 5-hydroxy-1,4-naphthoquinone pH 7.5 Cavia porcellus
1.6.5.5 0.143
-
 1,4-benzoquinone pH 7.5 Cavia porcellus
1.6.5.5 0.152
-
 1,4-benzoquinone pH 7.5 Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.5.5 cytosol it is possible that Arabidopsis P1-ZCr functions as a quinone reductase in vivo. Possible substrate quinones are not abundant in the cytosol, but under severe stress the quinones might be liberated from the cell compartments where they are normally sequestered, as exemplified by the release of polyphenols from vacuoles and polyphenol oxidase from thylakoid lumen upon the disruption of cells. Quinone reduction would not lead to the radical chain reaction, because superoxide dismutase is ubiquitous in cells Arabidopsis thaliana 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.5.5 38700
-
 2 * 38700, recombinant P1-ZCr is a noncovalent dimer, SDS-PAGE Arabidopsis thaliana
1.6.5.5 83200
-
 gel filtration Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.5 Arabidopsis thaliana
-
-
-
1.6.5.5 Cavia porcellus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.5.5
-
 Cavia porcellus
1.6.5.5
-
 Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.5.5 lens
-
 Cavia porcellus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.5 1,2-naphthoquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus 1,2-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 1,4-benzoquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus 1,4-benzosemiquinone + NADP+
-
 ?
1.6.5.5 1,4-naphthoquinone + NADPH + H+
-
 Arabidopsis thaliana 1,4-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 1,4-naphthoquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus 1,4-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 2 1,2-naphthoquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 2 1,2-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 2 1,4-benzoquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 2 1,4-benzosemiquinone + NADP+
-
 ?
1.6.5.5 2 1,4-naphthosemiquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 2 1,4-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 2 5-hydroxy-1,4-naphthoquinone + NADPH + H+ i.e. juglone. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 2 5-hydroxy-1,4-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 2 5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+ i.e. plumbagin. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 5-hydroxy-2-methyl-1,4-naphthoquinone + NADP+
-
 ?
1.6.5.5 2 9,10-phenanthrenequinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 2 9,10-phenanthrenesemiquinone + NADP+
-
 ?
1.6.5.5 2 decyl-plastoquinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Arabidopsis thaliana 2 decyl-plastosemiquinone + NADP+
-
 ?
1.6.5.5 5-hydroxy-1,4-naphthoquinone + NADPH + H+ i.e. juglone. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus 5-hydroxy-1,4-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+ i.e. plumbagin. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus 5-hydroxy-2-methyl-1,4-naphthosemiquinone + NADP+
-
 ?
1.6.5.5 9,10-phenanthrenequinone + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus 9,10-phenanthrenesemiquinone + NADP+
-
 ?
1.6.5.5 dichlorophenolindophenol + NADPH + H+
-
 Arabidopsis thaliana reduced dichlorophenolindophenol + NADP+
-
 ?
1.6.5.5 dichlorophenolindophenol + NADPH + H+ production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c Cavia porcellus reduced dichlorophenolindophenol + NADP+
-
 ?
1.6.5.5 ferricytochrome + NADPH + H+
-
 Arabidopsis thaliana ferrocytochrome + NADP+
-
 ?
1.6.5.5 additional information no activity with: phylloquinone (vitamin K1), menaquinone (vitamin K2), menadione (vitamin K3) and ferricyanide. Preference for o-quinones over p-quinones, and the inability to recognize menadione and ferricyanide as substrates, clearly distinguishe P1-ZCr and guinea-pig ZCr from the flavin-containing NAD(P)H-quinone oxidoreductases in plants and animals. P1-ZCr also catalyzed the divalent reduction of diamide to 1,2-bis(N,N-dimethylcarbamoyl)hydrazine, with a kcat comparable with that for quinones. Two other azodicarbonyl compounds also served as substrates of P1-ZCr. Guinea-pig ZCr, however, did not catalyze the azodicarbonyl reduction. Hence, plant ZCr is distinct from mammalian ZCr, and can be referred to as NADPH:azodicarbonyl/quinone reductase. The quinone-reducing reaction is accompanied by radical chain reactions to produce superoxide radicals, while the azodicarbonyl reducing reaction is not Arabidopsis thaliana ?
-
 ?
1.6.5.5 additional information no activity with: phylloquinone (vitamin K1), menaquinone (vitamin K2), menadione (vitamin K3), ferricytochrome and ferricyanide. Preference for o-quinones over p-quinones, and the inability to recognize menadione and ferricyanide as substrates, clearly distinguishe Arabidopsis thaliana P1-ZCr and guinea-pig ZCr from the flavin-containing NAD(P)H-quinone oxidoreductases in plants and animals Cavia porcellus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.5.5 dimer 2 * 38700, recombinant P1-ZCr is a noncovalent dimer, SDS-PAGE Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.6.5.5 NADPH:azodicarbonyl/quinone reductase
-
 Arabidopsis thaliana
1.6.5.5 NADPH:quinone oxidoreductase
-
 Cavia porcellus
1.6.5.5 NADPH:quinone oxidoreductase
-
 Arabidopsis thaliana
1.6.5.5 P1-ZCr
-
 Arabidopsis thaliana
1.6.5.5 P1-zeta-crystallin
-
 Cavia porcellus
1.6.5.5 P1-zeta-crystallin
-
 Arabidopsis thaliana
1.6.5.5 ZCr
-
 Cavia porcellus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.5.5 0.03
-
 Ferricytochrome pH 7.5 Arabidopsis thaliana
1.6.5.5 0.1
-
 decyl-plastoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 0.37
-
 5-Hydroxy-2-methyl-1,4-naphthoquinone pH 7.5 Cavia porcellus
1.6.5.5 1
-
 1,4-Naphthoquinone pH 7.5 Cavia porcellus
1.6.5.5 1.5
-
 dichlorophenolindophenol pH 7.5 Cavia porcellus
1.6.5.5 1.9
-
 5-hydroxy-1,4-naphthoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 3
-
 1,4-Naphthoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 3.8
-
 5-hydroxy-2-methyl-1,4-naphtoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 4.9
-
 5-hydroxy-1,4-naphthoquinone pH 7.5 Cavia porcellus
1.6.5.5 5.9
-
 1,4-benzoquinone pH 7.5 Cavia porcellus
1.6.5.5 7.5
-
 dichlorophenolindophenol pH 7.5 Arabidopsis thaliana
1.6.5.5 12
-
 1,4-benzoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 19
-
 9,10-phenanthrenequinone pH 7.5 Cavia porcellus
1.6.5.5 39
-
 1,2-naphthoquinone pH 7.5 Cavia porcellus
1.6.5.5 54
-
 1,2-naphthoquinone pH 7.5 Arabidopsis thaliana
1.6.5.5 98
-
 9,10-phenanthrenequinone pH 7.5 Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.5.5 8
-
-
 Arabidopsis thaliana

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.6.5.5 7.5 9.2 half-maximal activity at pH 7.5 and pH 9.2 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.5.5 NADPH
-
 Cavia porcellus
1.6.5.5 NADPH specificity to NADPH, as judged by kcat/Km, is more than 1000fold higher than that to NADH Arabidopsis thaliana