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EC 1.11.1.17 Details

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EC number

1.11.1.17

Accepted name

glutathione amide-dependent peroxidase

Reaction

2 glutathione amide + H₂O₂ = glutathione amide disulfide + 2 H₂O

Systematic name

glutathione amide:hydrogen-peroxide oxidoreductase

Comment

This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress [1]. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase).

History

created 2010

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

1.9 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

1.11.1 Peroxidases

1.11.1.1 NADH peroxidase

1.11.1.2 NADPH peroxidase

1.11.1.3 fatty-acid peroxidase

1.11.1.4 created 1961, deleted 1964, reinstated 1965 as EC 1.13.1.12, deleted 1972

1.11.1.5 cytochrome-c peroxidase

1.11.1.6 catalase

1.11.1.7 peroxidase

1.11.1.8 iodide peroxidase

1.11.1.9 glutathione peroxidase

1.11.1.10 chloride peroxidase

1.11.1.11 L-ascorbate peroxidase

1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase

1.11.1.13 manganese peroxidase

1.11.1.14 lignin peroxidase

1.11.1.15 peroxiredoxin

1.11.1.16 versatile peroxidase

1.11.1.17 glutathione amide-dependent peroxidase

1.11.1.18 bromide peroxidase

1.11.1.19 dye decolorizing peroxidase

1.11.1.20 prostamide/prostaglandin F_2α synthase

1.11.1.21 catalase-peroxidase

1.11.1.22 hydroperoxy fatty acid reductase

1.11.1.23 (S)-2-hydroxypropylphosphonic acid epoxidase

1.11.1.24 thioredoxin-dependent peroxiredoxin

1.11.1.25 glutaredoxin-dependent peroxiredoxin

1.11.1.26 NADH-dependent peroxiredoxin

1.11.1.27 glutathione-dependent peroxiredoxin

1.11.1.28 lipoyl-dependent peroxiredoxin

1.11.1.29 mycoredoxin-dependent peroxiredoxin

1.11.2 Peroxygenases

1.12 Acting on hydrogen as donor

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

1.16.1 With NAD⁺ or NADP⁺ as acceptor

1.16.3 With oxygen as acceptor

1.16.5 With a quinone or similar compound as acceptor

1.16.8 With a flavin as acceptor

1.16.9 With a copper protein as acceptor

1.16.98 With other, known, physiological acceptors

1.16.99 With unknown physiological acceptors

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

1.22 Acting on halogen in donors

1.22.1 With NAD⁺ or NADP⁺ as acceptor

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

1.99.1 Hydroxylases (now covered by EC 1.14)

1.99.2 Oxygenases (now covered by EC 1.13)

1.99.2.1 created 1961, deleted 1965

1.99.2.2 created 1961, deleted 1965

1.99.2.3 created 1961, deleted 1965

1.99.2.4 created 1961, deleted 1965

1.99.2.5 created 1961, deleted 1965

1.99.2.6 created 1961, deleted 1965

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Release 2023.1 (January 2023)