Information on EC 1.6.5.5 - NADPH:quinone reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.6.5.5
-
RECOMMENDED NAME
GeneOntology No.
NADPH:quinone reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADPH + H+ + 2 quinone = NADP+ + 2 semiquinone
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NADPH:quinone oxidoreductase
A zinc enzyme, specific for NADPH. Catalyses the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates [1]. Dicoumarol [cf. EC 1.6.5.2 NAD(P)H dehydrogenase (quinone)] and nitrofurantoin are competitive inhibitors with respect to the quinone substrate. The semiquinone free-radical product may be non-enzymically reduced to the hydroquinone or oxidized back to quinone in the presence of O2 [1]. In some mammals, the enzyme is abundant in the lens of the eye, where it is identified with the protein zeta-crystallin.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-20-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
zeta crystallin shows minimal NADPH:quinone reductase activity
-
-
Manually annotated by BRENDA team
strain 13/N
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pv. tomato DC3000
-
-
Manually annotated by BRENDA team
-
Q7A492
UniProt
Manually annotated by BRENDA team
gene arsh, encoded in the arsenic resistance operon
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
ArsH plays a role in the response to oxidative stress caused by arsenite
additional information
-
in silico structural model of ArsH reconstituted with FMN, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-naphthoquinone + NADPH
1,2-naphthoquinol + NADP+
show the reaction diagram
1,2-naphthoquinone + NADPH + H+
1,2-naphthosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
1,2-naphthoquinone + NADPH + H+
? + NADP+
show the reaction diagram
-
the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
-
-
?
1,4-benzoquinone + NADPH
1,4-benzoquinol + NADP+
show the reaction diagram
1,4-benzoquinone + NADPH + H+
1,4-benzosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
1,4-naphthoquinone + NADPH
1,4-naphthoquinol + NADP+
show the reaction diagram
1,4-naphthoquinone + NADPH + H+
1,4-naphthosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 1,2-naphthoquinone + NADPH + H+
2 1,2-naphthosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 1,2-naphthoquinone + NADPH + H+
? + NADP+
show the reaction diagram
-
the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
-
-
?
2 1,4-benzoquinone + NADPH + H+
2 1,4-benzosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 1,4-benzoquinone + NADPH + H+
? + NADP+
show the reaction diagram
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weak activity
-
-
?
2 1,4-naphthosemiquinone + NADPH + H+
2 1,4-naphthosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 5-hydroxy-1,4-naphthoquinone + NADPH + H+
2 5-hydroxy-1,4-naphthosemiquinone + NADP+
show the reaction diagram
-
i.e. juglone. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+
5-hydroxy-2-methyl-1,4-naphthoquinone + NADP+
show the reaction diagram
-
i.e. plumbagin. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 9,10-phenanthrenequinone + NADPH + H+
2 9,10-phenanthrenesemiquinone + NADP+
show the reaction diagram
2 9,10-phenanthrenequinone + NADPH + H+
? + NADP+
show the reaction diagram
-
70% of the activity with 9,10-phenanthrenequinone
-
-
?
2 decyl-plastoquinone + NADPH + H+
2 decyl-plastosemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2-hexenal + NADPH
hexanal + NADP+
show the reaction diagram
-
-
-
-
?
2-nonenal + NADPH
nonanal + NADP+
show the reaction diagram
-
-
-
-
?
2-pentenal + NADPH
pentanal + NADP+
show the reaction diagram
-
-
-
-
?
3-buten-2-one + NADPH
2-butanone + NADP+
show the reaction diagram
-
-
-
-
?
3-nonen-2-one + NADPH
2-nonanone + NADP+
show the reaction diagram
-
-
-
-
?
3-penten-2-one + NADPH
2-pentanone + NADP+
show the reaction diagram
-
-
-
-
?
4-hydroxy-2-hexenal + NADPH
4-hydroxy-hexanal + NADP+
show the reaction diagram
-
-
-
-
?
4-hydroxy-2-nonenal + NADPH
4-hydroxy-nonanal + NADP+
show the reaction diagram
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH
5-hydroxy-1,4-naphthoquinol + NADP+
show the reaction diagram
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthosemiquinone + NADP+
show the reaction diagram
-
i.e. juglone. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
?
show the reaction diagram
-
i.e. juglone
-
-
?
5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH
5-hydroxy-2-methyl-1,4-naphthoquinol + NADP+
show the reaction diagram
-
i.e. plumbagin, 0.9% of the activity with 1,2-naphthoquinone
-
-
-
5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+
5-hydroxy-2-methyl-1,4-naphthosemiquinone + NADP+
show the reaction diagram
-
i.e. plumbagin. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
9,10-phenanthrenequinone + NADPH
9,10-phenanthrenequinol + NADP+
show the reaction diagram
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
show the reaction diagram
Q7A492
one-electron reduction mechanism. Concomitantly with NADPH consumption, generation of superoxide is observed
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenesemiquinone + NADP+
show the reaction diagram
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
show the reaction diagram
-
the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
-
-
?
dichlorophenolindophenol + NADPH + H+
reduced dichlorophenolindophenol + NADP+
show the reaction diagram
ferricytochrome + NADPH + H+
ferrocytochrome + NADPH
show the reaction diagram
-
-
-
-
?
menadione + NADPH + H+
menadiol + NADP+
show the reaction diagram
methyl-1,4-benzoquinone + NADPH
methyl-1,4-benzoquinol + NADP+
show the reaction diagram
-
20.6% of the activity with 1,2-naphthoquinone
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-
-
NADPH + H+ + 2 2,5-dimethyl-4-benzoquinone
NADP+ + 2 2,5-dimethyl-4-benzosemiquinone
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 2-hydroxy-1,4-naphthoquinone
NADP+ + 2 2-hydroxy-1,4-naphthosemiquinone
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 anthraquinone-2-sulfonate
NADP+ + ?
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 coenzyme Q10
NADP+ + ?
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 dibromothymoquinone
NADP+ + 2 dibromothymosemiquinone
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 duroquinone
NADP+ + 2 durosemiquinone
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 menadione
NADP+ + ?
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 2 quinone
NADP+ + 2 semiquinone
show the reaction diagram
NADPH + H+ + komaroviquinone
NADP+ + ?
show the reaction diagram
-
reduction of komaroviquinone to its semiquinone radical. Antichagasic activity of komaroviquinone is due to generation of reactive oxygen species catalyzed by Trypanosoma cruzi old yellow enzyme
-
-
?
NADPH + H+ + menadione
NADP+ + ?
show the reaction diagram
-
-
-
-
?
NADPH + H+ + nifurtimox
NADP+ + ?
show the reaction diagram
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
propenal + NADPH
propanal + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + 2 quinone
NADP+ + 2 semiquinone
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
-
in silico structural model of ArsH reconstituted with FMN, overview
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Dimercaptopropanol
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-
2,5-Dichloro-3,6-dihydroxy-1,4-benzoquinone
-
i.e. chloranilic acid, noncompetitive with respect to both NADPH and 9,10-phenanthrenequinone
4-chloromercuribenzoate
-
both NADPH and NADP1 suppress the inhibition, but NADH does not
4-Hydroxycoumarin
-
reversible time-independent inhibition. Only dicoumarol, 4-hydroxycoumarin and warfarin inhibit in micromolar ranges. 7-Hydroxy-4-methylcoumarin is ineffective. Competitive inhibition with respect to 2,6-dichlorophenolindophenol, uncompetitive with respect to NADPH. Phenolic hydroxyl group at the C-4 position in the coumarin skeleton is important for the maximal inhibition. Sequence of potency for the inhibitors in descending order: dicoumarol, 4-hydroxycoumarin, warfarin, coumarin
5,5'-dithiobis(2-nitrobenzoate)
ADP
-
10% inhibition at 0.2 mM
Cibacron blue 3GA
coumarin
-
reversible time-independent inhibition. Only dicoumarol, 4-hydroxycoumarin and warfarin inhibit in micromolar ranges. 7-Hydroxy-4-methylcoumarin is ineffective. Competitive inhibition with respect to 2,6-dichlorophenolindophenol, uncompetitive with respect to NADPH. Phenolic hydroxyl group at the C-4 position in the coumarin skeleton is important for the maximal inhibition. Sequence of potency for the inhibitors in descending order: dicoumarol, 4-hydroxycoumarin, warfarin, coumarin
Cu2+
-
25% inhibition at 1 mM
dicoumarol
dithiothreitol
FAD
-
60% inhibition at 0.2 mM
FMN
-
40% inhibition at 0.2 mM
menadione
-
-
N-ethylmaleimide
-
both NADPH and NADP1 suppress the inhibition, but NADH does not
NAD+
-
5% inhibition at 0.2 mM
Nitrofurantoin
o-phthalaldehyde
-
-
p-Chloromercuriphenylsulfonate
-
-
pyridoxal-5'-phosphate
-
inactivation follows pseudo-first-order kinetics. NADPH protects against inactivation, 9,10-phenanthrenequinone does not protect. Inhibition is uncompetitive with NADPH and non-competitive with respect to 9,10-phenanthrenequinone
warfarin
Zn2+
-
25% inhibition at 1 mM
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024 - 0.029
1,2-naphthoquinone
0.065 - 0.152
1,4-benzoquinone
0.26
1,4-Naphthoquinone
-
-
0.0013
2,5-dimethyl-4-benzoquinone
-
pH 7.5, 10C
0.013 - 0.0153
2,6-dichlorophenolindophenol
0.13 - 6.12
2-hexenal
0.0237
2-Hydroxy-1,4-naphthoquinone
-
pH 7.5, 10C
0.482
2-nonenal
-
pH 7, 25C, wild-type
8.6
2-pentenal
-
pH 7, 25C, wild-type
0.035 - 0.13
3-buten-2-one
0.05 - 0.94
3-nonen-2-one
0.06 - 0.535
3-penten-2-one
0.08 - 1.26
4-hydroxy-2-hexenal
0.55
4-hydroxy-2-nonenal
-
pH 7, 25C, wild-type
0.011 - 0.027
5-hydroxy-1,4-naphthoquinone
0.00065 - 0.0491
9,10-phenanthrenequinone
0.0345
anthraquinone-2-sulfonate
-
pH 7.5, 10C
0.0119
coenzyme Q10
-
pH 7.5, 10C
0.025
decyl-plastoquinone
-
pH 7.5
0.0012
dibromothymoquinone
-
pH 7.5, 10C
0.0028
duroquinone
-
pH 7.5, 10C
0.02
Ferricytochrome
-
pH 7.5
0.03
komaroviquinone
-
-
0.0057 - 0.019
menadione
0.0025 - 0.07
NADPH
0.013
nifurtimox
-
-
0.86 - 2.3
propenal
additional information
additional information
-
stopped-flow and laser-flash photolysis kinetic analyses, steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 54
1,2-naphthoquinone
3.4 - 12
1,4-benzoquinone
1 - 3
1,4-Naphthoquinone
36.7
2,5-dimethyl-4-benzoquinone
Synechocystis sp.
-
pH 7.5, 10C
0.28 - 73.27
2-hexenal
11
2-Hydroxy-1,4-naphthoquinone
Synechocystis sp.
-
pH 7.5, 10C
0.11
2-nonenal
Homo sapiens
-
pH 7, 25C, wild-type
0.2
2-pentenal
Homo sapiens
-
pH 7, 25C, wild-type
0.16 - 0.97
3-buten-2-one
0.21 - 3.11
3-nonen-2-one
0.2 - 2.66
3-penten-2-one
1.33 - 3.67
4-hydroxy-2-hexenal
1.15
4-hydroxy-2-nonenal
Homo sapiens
-
pH 7, 25C, wild-type
1.9 - 4.9
5-hydroxy-1,4-naphthoquinone
0.37
5-Hydroxy-2-methyl-1,4-naphthoquinone
Cavia porcellus
-
pH 7.5
3.8
5-hydroxy-2-methyl-1,4-naphtoquinone
Arabidopsis thaliana
-
pH 7.5
-
2.2 - 98
9,10-phenanthrenequinone
9.4
anthraquinone-2-sulfonate
Synechocystis sp.
-
pH 7.5, 10C
5
coenzyme Q10
Synechocystis sp.
-
pH 7.5, 10C
0.1
decyl-plastoquinone
Arabidopsis thaliana
-
pH 7.5
35
dibromothymoquinone
Synechocystis sp.
-
pH 7.5, 10C
1.5 - 7.5
dichlorophenolindophenol
25
duroquinone
Synechocystis sp.
-
pH 7.5, 10C
0.03
Ferricytochrome
Arabidopsis thaliana
-
pH 7.5
26
menadione
Synechocystis sp.
-
pH 7.5, 10C
1.25 - 39.74
propenal
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.06
2-hexenal
0.23
2-nonenal
Homo sapiens
-
pH 7, 25C, wild-type
5769
0.023
2-pentenal
Homo sapiens
-
pH 7, 25C, wild-type
42626
0.13 - 4.8
3-buten-2-one
0.016 - 0.23
3-nonen-2-one
0.025 - 0.36
3-penten-2-one
0.023 - 10.21
4-hydroxy-2-hexenal
2.1
4-hydroxy-2-nonenal
Homo sapiens
-
pH 7, 25C, wild-type
1426
0.058 - 1.5
propenal
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.8
Q7A492
substrate menadione, pH 7.5, 25C
311
Q7A492
substrate 9,10-phenanthrenequinone, pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
assay at
7.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
-
pH 4.5: about 60% of maximal activity, pH 10: about 50% of maximal activity
7.5 - 9.2
-
half-maximal activity at pH 7.5 and pH 9.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
about 60% of maximal activity at 20C and at 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
Q7A492
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is expressed throughout the Trypanosoma cruzi life cycle
Manually annotated by BRENDA team
the gene for QR1 is isolated from an expressed sequence tag collection derived from the epidermis of a diploid Triticum monococcum L. 24 h after inoculation with the powdery mildew fungus Blumeria graminis EO Speer f. sp. tritici Em. Marchal. TmQR1 is repressed while TmQR2 is induced in the epidermis during powdery mildew infection
Manually annotated by BRENDA team
-
the enzyme is expressed throughout the Trypanosoma cruzi life cycle
Manually annotated by BRENDA team
-
the enzyme is expressed throughout the Trypanosoma cruzi life cycle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
localizes in both cytoplasm and nucleus
Manually annotated by BRENDA team
additional information
-
not in nucleus
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Pseudomonas syringae pv. tomato (strain DC3000)
Pseudomonas syringae pv. tomato (strain DC3000)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
gel filtration
70000
-
gel filtration
83200
-
gel filtration
108000
-
gel filtration
140000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 36000, SDS-PAGE
homotetramer
multimer
Q7A492
x * 36300, calculated and co-purification results
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallographic structure of human zeta-crystallin is reported. Enzyme shows a tetrameric structure
-
crystal structures of zeta-crystallin-like quinone oxidoreductase and its complexes with NADPH determined at 2.4 and 2.01 A resolution
-
native enzyme and its complex with NADPH at 2.3 A and 2.8 A resolution. QOR forms a homodimer in the crystal by interaction of the betaF-strands in domain II, forming a large beta-sheet that crosses the dimer interface. NADPH is located between the two domains in the QOR-NADPH complex. The disordered segment involved in the coenzyme binding of apo-QOR becomes ordered upon NADPH binding. The segment covers an NADPH-binding cleft and may serve as a lid. The 2'-phosphate group of the adenine of NADPH is surrounded by polar and positively charged residues in QOR, suggesting that QOR binds NADPH more readily than NADH. The putative substrate-binding site of QOR, is largely blocked by nearby residues
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
10 min, 65% loss of activity
51
-
10 min, complete loss of activity
80
thermal denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADPH protects against inactivation caused by heat, NEM or H2O2
-
very stable to freezing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 5 months, stable
-
-20C, less than 10% loss of activity after 4-6 weeks
-
4C, 1 week, complete inactivation of purified enzyme
4C, stable for at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the quinone oxidoreductase activity of purified his-tagged recombinant mouse zeta-crystallin is comparable to that of purified native guinea pig lens zeta-crystallin, and to that of recombinant guinea pig zeta-crystallin. The method permits production of substantial amounts of recombinant zeta-crystallin for conducting studies on the biological role of this protein
-
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
expression in Escherichia coli, expression of TmQR1 is lethal to the cells, it is not possible to purify enough protein for further analysis
expression of His-tagged enzyme in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced in presence of 9,10-phenanthrenequinone and by oxidative stress
Q7A492
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T53F
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Tyr53Phe mutant displays a large increase in Km values for all substrates and the cofactor, but mainly towards 3-buten-2-one and propenal with a 30fold increase. For 3-penten-2-one, 3-nonen-2-one, 2-hexenal and 4-hydroxy-2-hexenal mutant also shows a decrease in kcat
T59F
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Tyr59Phe mutant exhibits almost the same kinetic parameter values as the wild-type enzyme for 2-alkenals,while the Km is increased for 4-hydroxy-2-hexenal
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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QAO does not possess a protective role in menadione-induced free radical production and DNA damage in human cancer cells. Under aerobic conditions, menadiol produced by QAR is readily oxidized to menadione by two 1-electron steps producing the semiquinone and the parent quinone with concomitant production of superoxide anion, which leads to generation of hydroxyl radicals
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