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Information on EC 1.6.5.5 - NADPH:quinone reductase and Organism(s) Thermus thermophilus and UniProt Accession Q8L3C8

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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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This record set is specific for:
Thermus thermophilus
UNIPROT: Q8L3C8
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
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
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADPH is located in the cleft between domains I and II. The adenine ring is sandwiched between the main chains of Ala220 and Glu221 and the side chain of Arg292. Ala220 and Glu221 are disordered in apo-QOR
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8L3C8_THETH
302
0
32089
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
80
thermal denaturation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimomura, Y.; Kakuta, Y.; Fukuyama, K.
Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: Implication for NADPH and substrate recognition
J. Bacteriol.
185
4211-4218
2003
Thermus thermophilus (Q8L3C8), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q8L3C8)
Manually annotated by BRENDA team