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EC 1.8.5.7 Details

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EC number

1.8.5.7

Accepted name

glutathionyl-hydroquinone reductase

Reaction

glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone

Other name(s)

pcpF (gene name), yqjG (gene name)

Systematic name

2-(glutathione-S-yl)-hydroquinone:glutathione oxidoreductase

Comment

This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyse the glutathione-dependent reduction of glutathionyl-hydroquinones. The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)-hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone. Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.

History

created 2017

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.2 With a cytochrome as acceptor

1.8.3 With oxygen as acceptor

1.8.4 With a disulfide as acceptor

1.8.5 With a quinone or similar compound as acceptor

1.8.5.1 glutathione dehydrogenase (ascorbate)

1.8.5.2 thiosulfate dehydrogenase (quinone)

1.8.5.3 respiratory dimethylsulfoxide reductase

1.8.5.4 bacterial sulfide:quinone reductase

1.8.5.5 thiosulfate reductase (quinone)

1.8.5.6 sulfite dehydrogenase (quinone)

1.8.5.7 glutathionyl-hydroquinone reductase

1.8.5.8 eukaryotic sulfide quinone oxidoreductase

1.8.5.9 protein dithiol:quinone oxidoreductase DsbB

1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass)

1.8.7 With an iron-sulfur protein as acceptor

1.8.98 With other, known, physiological acceptors

1.8.99 With unknown physiological acceptors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.12.1 With NAD⁺ or NADP⁺ as acceptor

1.12.2 With a cytochrome as acceptor

1.12.5 With a quinone or similar compound as acceptor

1.12.7 With an iron-sulfur protein as acceptor

1.12.98 With other, known, physiological acceptors

1.12.99 With unknown physiological acceptors

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.97.1.1 chlorate reductase

1.97.1.2 pyrogallol hydroxytransferase

1.97.1.3 sulfur reductase

1.97.1.4 [formate-C-acetyltransferase]-activating enzyme

1.97.1.5 created 2000 deleted 2001

1.97.1.6 created 2000 deleted 2001

1.97.1.7 created 2000, deleted 2001

1.97.1.8 tetrachloroethene reductive dehalogenase

1.97.1.9 selenate reductase

1.97.1.10 thyroxine 5′-deiodinase

1.97.1.11 thyroxine 5-deiodinase

1.97.1.12 photosystem I

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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Release 2023.1 (January 2023)