EC Explorer

[browse EC tree] - [search]

EC 1.11.1.17 Details

show Brenda entry

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

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

1.6.99.1 NADPH dehydrogenase

1.6.99.2 created 1961 as EC 1.6.5.2, transferred 1965 to EC 1.6.99.2, deleted 2005

1.6.99.3 NADH dehydrogenase

1.6.99.4 created 1965, deleted 1972

1.6.99.5 NADH dehydrogenase (quinone)

1.6.99.6 NADPH dehydrogenase (quinone)

1.6.99.7 created 1972, modified 1981 (EC 1.6.99.10 created 1978, incorporated 1981), deleted 2003

1.6.99.8 created 1972, deleted 2002

1.6.99.9 created 1972, deleted 2002

1.6.99.10 created 1978, deleted 1981

1.6.99.11 created 1989, deleted 2002

1.6.99.12 created 1989, deleted 2002

1.6.99.13 created 1992, deleted 2002

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

1.17 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

1.21.3.1 isopenicillin-N synthase

1.21.3.2 columbamine oxidase

1.21.3.3 reticuline oxidase

1.21.3.4 sulochrin oxidase [(+)-bisdechlorogeodin-forming]

1.21.3.5 sulochrin oxidase [(-)-bisdechlorogeodin-forming]

1.21.3.6 aureusidin synthase

1.21.3.7 tetrahydrocannabinolic acid synthase

1.21.3.8 cannabidiolic acid synthase

1.21.3.9 dichlorochromopyrrolate synthase

1.21.3.10 hercynylcysteine S-oxide synthase

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

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)