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Information on EC 1.6.5.5 - NADPH:quinone reductase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38230

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EC Tree
IUBMB Comments
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 . 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 . In some mammals, the enzyme is abundant in the lens of the eye, where it is identified with the protein zeta-crystallin.
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Saccharomyces cerevisiae
UNIPROT: P38230
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
zeta-crystallin, old yellow enzyme, vat-1, nadph:quinone oxidoreductase, nad(p)h:menadione oxidoreductase, tcoye, nad(p)h:(quinone-acceptor) oxidoreductase, nad(p)h-quinone reductase, p1-zcr, zta1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate) (quinone)
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DT-diaphorase
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Flavoprotein NAD(P)H:quinone reductase
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Menadione oxidoreductase
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Menadione reductase
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NAD(P)H dehydrogenase
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NAD(P)H dehydrogenase (quinone)
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NAD(P)H menadione reductase
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NAD(P)H quinone reductase
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NAD(P)H-quinone dehydrogenase
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NAD(P)H-quinone oxidoreductase
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NAD(P)H-quinone reductase
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NAD(P)H:(quinone-acceptor) oxidoreductase
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NAD(P)H:menadione oxidoreductase
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NAD(P)H:paraquat diaphorase
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NADH-menadione reductase
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NADH-menaquinone reductase
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NADH:quinone reductase
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NADPH DT-diaphorase
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NADPH:quinone oxidoreductase
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NADPH:quinone reductase
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Naphthoquinone reductase
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p-Benzoquinone reductase
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P36
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Phylloquinone reductase
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Quinone reductase
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Reduced NAD(P)H dehydrogenase
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Viologen accepting pyridine nucleotide oxidoreductase
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Vitamin K reductase
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zeta-Crystallin
zeta-crystallin homolog protein
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zeta-crystallin/NADPH:quinone oxidoreductase
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zeta-Crystallin/quinone reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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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
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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 + H+
? + NADP+
show the reaction diagram
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the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
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?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
show the reaction diagram
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the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
interference of NADPH on Zta1p binding to RNA is much lower than that of NADPH on human zeta-crystallin, consistent with a weaker binding of NADPH to the yeast enzyme
NADPH
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completely specific for NADPH as cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009
1,2-naphthoquinone
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pH 7.5
0.004
9,10-phenanthrenequinone
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pH 7.5
0.07
NADPH
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pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.17
1,2-naphthoquinone
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pH 7.5
4.17
9,10-phenanthrenequinone
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pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
localizes in both cytoplasm and nucleus
Manually annotated by BRENDA team
localizes in both cytoplasm and nucleus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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yeast zeta-crystallin is a quinone oxidoreductase belonging to the zeta-crystallin family, with activity in the reduction of alkenal/alkenone compounds. The lack of Zta1 negatively affects the expression of a group of genes involved in amino acid biosynthesis. Zta1 participates in the post-transcriptional regulation of ARG4 expression by increasing the ARG4 mRNA half-life. Expression of the zeta-crystallin gene is itself regulated by nutrient availability through the general amino acid control and target of rapamycin pathways
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
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2 * 36000, SDS-PAGE
70000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 36000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 week, complete inactivation of purified enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandez, M.R.; Porte, S.; Crosas, E.; Barbera, N.; Farres, J.; Biosca, J.A.; Pares, X.
Human and yeast zeta-crystallins bind AU-rich elements in RNA
Cell. Mol. Life Sci.
64
1419-1427
2007
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Porte, S.; Crosas, E.; Yakovtseva, E.; Biosca, J.A.; Farres, J.; Fernandez, M.R.; Pares, X.
MDR quinone oxidoreductases: the human and yeast zeta-crystallins
Chem. Biol. Interact.
178
288-294
2009
Saccharomyces cerevisiae (P38230), Saccharomyces cerevisiae, Homo sapiens (Q08257), Homo sapiens
Manually annotated by BRENDA team
Crosas, E.; Sumoy, L.; Gonzalez, E.; Diaz, M.; Bartolome, S.; Farres, J.; Pares, X.; Biosca, J.A.; Fernandez, M.R.
The yeast zeta-crystallin/NADPH quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life
FEBS J.
282
1953-1964
2015
Saccharomyces cerevisiae
Manually annotated by BRENDA team