Misplaced Pages

List of EC numbers (EC 1)

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
(Redirected from EC 1.17)

This list contains a list of EC numbers for the first group, EC 1, oxidoreductases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald.

EC 1.1 Acting on the CH-OH group of donors

EC 1.1.1 With Nicotinamide adenine dinucleotide or NADP as acceptor

At present (October 2021) most of the entries from 343 onwards have no Misplaced Pages articles
  • EC 1.1.1.343: phosphogluconate dehydrogenase (NAD-dependent, decarboxylating)
  • EC 1.1.1.344: dTDP-6-deoxy-L-talose 4-dehydrogenase
  • EC 1.1.1.345: D-2-hydroxyacid dehydrogenase (NAD)
  • EC 1.1.1.346: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
  • EC 1.1.1.347: geraniol dehydrogenase (NAD)
  • EC 1.1.1.348: (3R)-2′-hydroxyisoflavanone reductase
  • EC 1.1.1.349: norsolorinic acid ketoreductase
  • EC 1.1.1.350: ureidoglycolate dehydrogenase (NAD)
  • EC 1.1.1.351: phosphogluconate dehydrogenase
  • EC 1.1.1.352: 5′-hydroxyaverantin dehydrogenase
  • EC 1.1.1.353: versiconal hemiacetal acetate reductase
  • EC 1.1.1.354: farnesol dehydrogenase (NAD)
  • EC 1.1.1.355: 2′-dehydrokanamycin reductase
  • EC 1.1.1.356: GDP-L-colitose synthase
  • EC 1.1.1.357: 3α-hydroxysteroid 3-dehydrogenase
  • EC 1.1.1.358: 2-dehydropantolactone reductase
  • EC 1.1.1.359: aldose 1-dehydrogenase
  • EC 1.1.1.360: glucose/galactose 1-dehydrogenase
  • EC 1.1.1.361: glucose-6-phosphate 3-dehydrogenase
  • EC 1.1.1.362: aklaviketone reductase
  • EC 1.1.1.363: glucose-6-phosphate dehydrogenase
  • EC 1.1.1.364: dTDP-4-dehydro-6-deoxy-α-D-gulose 4-ketoreductase
  • EC 1.1.1.365: D-galacturonate reductase
  • EC 1.1.1.366: L-idonate 5-dehydrogenase (NAD)
  • EC 1.1.1.367: UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase
  • EC 1.1.1.368: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
  • EC 1.1.1.369: D-chiro-inositol 1-dehydrogenase
  • EC 1.1.1.370: scyllo-inositol 2-dehydrogenase (NAD)
  • EC 1.1.1.371: scyllo-inositol 2-dehydrogenase (NADP)
  • EC 1.1.1.372: D/L-glyceraldehyde reductase
  • EC 1.1.1.373: sulfolactaldehyde 3-reductase
  • EC 1.1.1.374: UDP-N-acetylglucosamine 3-dehydrogenase
  • EC 1.1.1.375: L-2-hydroxycarboxylate dehydrogenase
  • EC 1.1.1.376: L-arabinose 1-dehydrogenase
  • EC 1.1.1.377: L-rhamnose 1-dehydrogenase (NADP)
  • EC 1.1.1.378: L-rhamnose 1-dehydrogenase
  • EC 1.1.1.379: (R)-mandelate dehydrogenase
  • EC 1.1.1.380: L-gulonate 5-dehydrogenase
  • EC 1.1.1.381: 3-hydroxy acid dehydrogenase
  • EC 1.1.1.382: ketol-acid reductoisomerase (NAD)
  • EC 1.1.1.383: ketol-acid reductoisomerase
  • EC 1.1.1.384: dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase
  • EC 1.1.1.385: dihydroanticapsin dehydrogenase
  • EC 1.1.1.386: ipsdienol dehydrogenase
  • EC 1.1.1.387: L-serine 3-dehydrogenase (NAD)
  • EC 1.1.1.388: glucose-6-phosphate dehydrogenase (NAD)
  • EC 1.1.1.389: 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase
  • EC 1.1.1.390: sulfoquinovose 1-dehydrogenase
  • EC 1.1.1.391: 3β-hydroxycholanate 3-dehydrogenase (NAD)
  • EC 1.1.1.392: 3α-hydroxycholanate dehydrogenase (NADP)
  • EC 1.1.1.393: 3β-hydroxycholanate 3-dehydrogenase (NADP)
  • EC 1.1.1.394: aurachin B dehydrogenase
  • EC 1.1.1.395: 3α-hydroxy bile acid-CoA-ester 3-dehydrogenase
  • EC 1.1.1.396: bacteriochlorophyllide a dehydrogenase
  • EC 1.1.1.397: β-methylindole-3-pyruvate reductase
  • EC 1.1.1.398: 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase
  • EC 1.1.1.399: 2-oxoglutarate reductase
  • EC 1.1.1.400: 2-methyl-1,2-propanediol dehydrogenase
  • EC 1.1.1.401: 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD)
  • EC 1.1.1.402: D-erythritol 1-phosphate dehydrogenase
  • EC 1.1.1.403: D-threitol dehydrogenase (NAD)
  • EC 1.1.1.404: tetrachlorobenzoquinone reductase
  • EC 1.1.1.405: ribitol-5-phosphate 2-dehydrogenase (NADP)
  • EC 1.1.1.406: galactitol 2-dehydrogenase (L-tagatose-forming)
  • EC 1.1.1.407: D-altritol 5-dehydrogenase
  • EC 1.1.1.408: 4-phospho-D-threonate 3-dehydrogenase
  • EC 1.1.1.409: 4-phospho-D-erythronate 3-dehydrogenase
  • EC 1.1.1.410: D-erythronate 2-dehydrogenase
  • EC 1.1.1.411: L-threonate 2-dehydrogenase
  • EC 1.1.1.412: 2-alkyl-3-oxoalkanoate reductase
  • EC 1.1.1.413: A-factor type γ-butyrolactone 1′-reductase (1S-forming)
  • EC 1.1.1.414: L-galactonate 5-dehydrogenase
  • EC 1.1.1.415: noscapine synthase
  • EC 1.1.1.416: isopyridoxal dehydrogenase (5-pyridoxolactone-forming)
  • EC 1.1.1.417: 3β-hydroxysteroid-4β-carboxylate 3-dehydrogenase (decarboxylating)
  • EC 1.1.1.418: plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating)
  • EC 1.1.1.419: nepetalactol dehydrogenase
  • EC 1.1.1.420: D-apiose dehydrogenase
  • EC 1.1.1.421: D-apionate oxidoisomerase
  • EC 1.1.1.422: pseudoephedrine dehydrogenase
  • EC 1.1.1.423: (1R,2S)-ephedrine 1-dehydrogenase
  • EC 1.1.1.424: D-xylose 1-dehydrogenase (NADP, D-xylono-1,4-lactone-forming)
  • EC 1.1.1.425: levoglucosan dehydrogenase
  • EC 1.1.1.426: UDP-N-acetyl-α-D-quinovosamine dehydrogenase

EC 1.1.2 With a cytochrome as acceptor

*No Misplaced Pages article

EC 1.1.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.1.4 With a disulfide as acceptor

  • EC 1.1.4.1: Now EC 1.17.4.4, vitamin-K-epoxide reductase (warfarin-sensitive)
  • EC 1.1.4.2: Now EC 1.17.4.5, vitamin-K-epoxide reductase (warfarin-insensitive)

EC 1.1.5 With a quinone or similar compound as acceptor

EC 1.1.9 With a copper protein as acceptor

EC 1.1.98 With other, known, acceptors

*No Misplaced Pages article

EC 1.1.99 With unknown physiological acceptors

*No Misplaced Pages article

EC 1.2 Acting on the aldehyde or oxo group of donors

EC 1.2.1 With NAD or NADP as acceptor

* No Misplaced Pages article

EC 1.2.2 With a cytochrome as acceptor

  • EC 1.2.2.1: formate dehydrogenase (cytochrome)
  • EC 1.2.2.2: Now covered by EC 1.2.5.1, pyruvate dehydrogenase (quinone)
  • EC 1.2.2.3: Now EC 1.17.2.3, formate dehydrogenase (cytochrome-c-553)
  • EC 1.2.2.4: Now classified as EC 1.2.5.3, aerobic carbon monoxide dehydrogenase

EC 1.2.3 With oxygen as acceptor

* No Misplaced Pages article

EC 1.2.4 With a disulfide as acceptor

EC 1.2.5 With a quinone or similar compound as acceptor

*No Misplaced Pages article

EC 1.2.7 With an iron–sulfur protein as acceptor

*No Misplaced Pages article

EC 1.2.99: With unknown physiological acceptors

  • EC 1.2.99.1: Now EC 1.17.99.4, uracil/thymine dehydrogenase
  • EC 1.2.99.2: Now EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin)
  • EC 1.2.99.3: Now EC 1.2.5.2, aldehyde dehydrogenase (quinone)
  • EC 1.2.99.4: Now EC 1.2.98.1, formaldehyde dismutase
  • EC 1.2.99.5: Now EC 1.2.7.12, formylmethanofuran dehydrogenase
  • EC 1.2.99.6: carboxylate reductase
  • EC 1.2.99.7: aldehyde dehydrogenase (FAD-independent)
  • EC 1.2.99.8: glyceraldehyde dehydrogenase (FAD-containing) *
  • EC 1.2.99.9: Now EC 1.17.98.3, formate dehydrogenase (coenzyme F420)
  • EC 1.2.99.10: 4,4′-diapolycopenoate synthase *
*No Misplaced Pages article

EC 1.3 Acting on the CH-CH group of donors

EC 1.3.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.3.2 With a cytochrome as acceptor

EC 1.3.3 With oxygen as acceptor

EC 1.3.5 With a quinone or related compound as acceptor

EC 1.3.7 With an iron–sulfur protein as acceptor

EC 1.3.8 With a flavin as acceptor

*No Misplaced Pages article

EC 1.3.98 With FMN acceptor

  • EC 1.3.98.1: dihydroorotate dehydrogenase (fumarate)
  • EC 1.3.98.2: Now EC 1.3.4.1, fumarate reductase (CoM/CoB)
  • EC 1.3.98.3: coproporphyrinogen dehydrogenase *
  • EC 1.3.98.4: 5a,11a-dehydrotetracycline reductase *
  • EC 1.3.98.5: hydrogen peroxide-dependent heme synthase *
  • EC 1.3.98.6: AdoMet-dependent heme synthase *
  • EC 1.3.98.7: -tyrosine decarboxylase
*No Misplaced Pages article

EC 1.3.99 With unknown physiological acceptors

*No Misplaced Pages article

EC 1.4 Acting on the CH-NH2 group of donors

EC 1.4.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.4.2 With a cytochrome as acceptor

EC 1.4.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.4.4 With a disulfide as acceptor

EC 1.4.5 With a quinone or other compound as acceptor

EC 1.4.7 With an iron–sulfur protein as acceptor

EC 1.4.9 With a copper protein as acceptor

EC 1.4.98 With tryptophan tryptophylquinone acceptors

EC 1.4.99 With unknown physiological acceptors

*No Misplaced Pages article

EC 1.5 Acting on the CH-NH group of donors

EC 1.5.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.5.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.5.4 With a disulfide as acceptor

EC 1.5.5 With a quinone or similar compound as acceptor

*No Misplaced Pages article

EC 1.5.7 With an iron–sulfur protein as acceptor

*No Misplaced Pages article

EC 1.5.8 With a flavin or flavoprotein as acceptor

EC 1.5.98 With other, known, physiological acceptors

  • EC 1.5.98.1: ethylenetetrahydromethanopterin dehydrogenase
  • EC 1.5.98.2: 5,10-methylenetetrahydromethanopterin reductase
  • EC 1.5.98.3: coenzyme F420:methanophenazine dehydrogenase

EC 1.5.99 With unknown physiological acceptors

*No Misplaced Pages article

EC 1.6 Acting on NADH or NADPH

EC 1.6.1 With NAD or NADP as acceptor

EC 1.6.2 With a heme protein as acceptor

EC 1.6.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.6.4 With a disulfide as acceptor (deleted sub-class)

  • EC 1.6.4.1: now EC 1.8.1.6 cystine reductase
  • EC 1.6.4.2: now EC 1.8.1.7 glutathione-disulfide reductase
  • EC 1.6.4.3: now EC 1.8.1.4 dihydrolipoyl dehydrogenase
  • EC 1.6.4.4: now EC 1.8.1.8 protein-disulfide reductase
  • EC 1.6.4.5: now EC 1.8.1.9 thioredoxin-disulfide reductase
  • EC 1.6.4.6: now EC 1.8.1.10 CoA-glutathione reductase
  • EC 1.6.4.7: now EC 1.8.1.11 asparagusate reductase
  • EC 1.6.4.8: now EC 1.8.1.12 trypanothione-disulfide reductase
  • EC 1.6.4.9: now EC 1.8.1.13 bis-γ-glutamylcystine reductase
  • EC 1.6.4.10: now EC 1.8.1.14 CoA-disulfide reductase

EC 1.6.5 With a quinone or similar compound as acceptor

*No Misplaced Pages article

EC 1.6.6 With a nitrogenous group as acceptor

  • EC 1.6.6.1: Now EC 1.7.1.1, nitrate reductase (NADH)
  • EC 1.6.6.2: Now EC 1.7.1.2, nitrate reductase
  • EC 1.6.6.3: Now EC 1.7.1.3, nitrate reductase (NADPH)
  • EC 1.6.6.4: Now EC 1.7.1.4, nitrite reductase
  • EC 1.6.6.5: Now EC 1.7.2.1, nitrite reductase (NO-forming)
  • EC 1.6.6.6: Now EC 1.7.1.5, hyponitrite reductase
  • EC 1.6.6.7: Now EC 1.7.1.6, azobenzene reductase
  • EC 1.6.6.8: Now EC 1.7.1.7, GMP reductase
  • EC 1.6.6.9: Now known to be catalysed by EC 1.7.2.3, trimethylamine-N-oxide reductase
  • EC 1.6.6.10: Now EC 1.7.1.9, nitroquinoline-N-oxide reductase]
  • EC 1.6.6.11: Now EC 1.7.1.10, hydroxylamine reductase (NADH)
  • EC 1.6.6.12: Now EC 1.7.1.11, 4-(dimethylamino)phenylazoxybenzene reductase
  • EC 1.6.6.13: Now EC 1.7.1.12, N-hydroxy-2-acetamidofluorene reductase

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

  • EC 1.6.7.1: now EC 1.18.1.2 ferredoxin—NADP reductase
  • EC 1.6.7.2: now EC 1.18.1.1 rubredoxin—NAD reductase
  • EC 1.6.7.3: now EC 1.18.1.3 ferredoxin—NAD reductase

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

EC 1.6.99 With unknown physiological acceptors

  • EC 1.6.99.1: NADPH dehydrogenase
  • EC 1.6.99.2: Now EC 1.6.5.2, NAD(P)H dehydrogenase (quinone
  • EC 1.6.99.3: The activity is covered by EC 7.1.1.2, NADH:ubiquinone reductase (H-translocating)
  • EC 1.6.99.4: Now EC 1.18.1.2, ferredoxin—NADP reductase
  • EC 1.6.99.5: Now EC 1.6.5.11, NADH dehydrogenase (quinone)
  • EC 1.6.99.6: Now EC 1.6.5.10, NADPH dehydrogenase (quinone)
  • EC 1.6.99.7: Now EC 1.5.1.34, 6,7-dihydropteridine reductase
  • EC 1.6.99.8: Deleted
  • EC 1.6.99.9: Now EC 1.16.1.4, cob(II)alamin reductase
  • EC 1.6.99.10: included in EC 1.5.1.34, 6,7-dihydropteridine reductase
  • EC 1.6.99.11: Deleted
  • EC 1.6.99.12: Now EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating)
  • EC 1.6.99.13: Now EC 1.16.1.7, ferric-chelate reductase

EC 1.7 Acting on other nitrogenous compounds as donors

EC 1.7.1 With NAD or NADP as acceptor

EC 1.7.2 With a cytochrome as acceptor

*No Misplaced Pages article

EC 1.7.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.7.5 With a quinone or similar compound as acceptor

EC 1.7.6 With a nitrogenous group as acceptor

EC 1.7.7 With an iron–sulfur protein as acceptor

EC 1.7.99 With other acceptors

EC 1.8 Acting on a sulfur group of donors

EC 1.8.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.8.2 With a cytochrome as acceptor

*No Misplaced Pages article

EC 1.8.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.8.4 With a disulfide as acceptor

*No Misplaced Pages article

EC 1.8.5 With a quinone or similar compound as acceptor

*No Misplaced Pages article

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

EC 1.8.7 With an iron–sulfur protein as acceptor

*No Misplaced Pages article

EC 1.8.98 With other, known, acceptors

EC 1.8.99 With other acceptors

  • EC 1.8.99.1: Now covered by EC 1.8.1.2, assimilatory sulfite reductase (NADPH) and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin)
  • EC 1.8.99.2: adenylyl-sulfate reductase
  • EC 1.8.99.3: an in vitro artifact of EC 1.8.99.5, dissimilatory sulfite reductase
  • EC 1.8.99.4: Now EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin)
  • EC 1.8.99.5: dissimilatory sulfite reductase *
*No Misplaced Pages article

EC 1.9 Acting on a heme group of donors

EC 1.9.3 With oxygen as acceptor

  • EC 1.9.3.1: Now EC 7.1.1.9, cytochrome-c oxidase
  • EC 1.9.3.2: Now included with EC 1.7.2.1, nitrite reductase (NO-forming)

EC 1.9.6 With a nitrogenous group as acceptor

EC 1.9.98 With other, known, physiological acceptors

EC 1.9.99 With other acceptors

  • EC 1.9.99.1: Now EC 1.9.98.1, iron—cytochrome-c reductase

EC 1.10 Acting on diphenols and related substances as donors

EC 1.10.1 With NAD or NADP as acceptor

EC 1.10.2 With a cytochrome as acceptor

  • EC 1.10.2.1: The activity is covered by EC 7.2.1.3, ascorbate ferrireductase (transmembrane)
  • EC 1.10.2.2: Now EC 7.1.1.8, quinol—cytochrome-c reductase

EC 1.10.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.10.5 With a quinone or related compound as acceptor

  • EC 1.10.5.1: ribosyldihydronicotinamide dehydrogenase (quinone)
*No Misplaced Pages article

EC 1.10.9 With a copper protein as acceptor

  • EC 1.10.9.1: Now EC 7.1.1.6, plastoquinol—plastocyanin reductase

EC 1.10.99 With unknown physiological acceptors

  • EC 1.10.99.1: Now EC 1.10.9.1 plastoquinol—plastocyanin reductase
  • EC 1.10.99.2: Now EC 1.10.5.1 ribosyldihydronicotinamide dehydrogenase (quinone)
  • EC 1.10.99.3: Now EC 1.23.5.1 violaxanthin de-epoxidase

EC 1.11 Acting on a peroxide as acceptor

EC 1.11.1 Peroxidases

*No Misplaced Pages article

EC 1.11.2 Peroxygenase

*No Misplaced Pages article

EC 1.12 Acting on hydrogen as donor

EC 1.12.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.12.2 With a cytochrome as acceptor

EC 1.12.5 With a quinone or similar compound as acceptor

EC 1.12.7 With an iron–sulfur protein as acceptor

EC 1.12.98 With other known acceptors

EC 1.12.99 With unknown physiological acceptors

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

EC 1.13.11 With incorporation of two atoms of oxygen

*No Misplaced Pages article

EC 1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)

*No Misplaced Pages article

EC 1.13.99 Miscellaneous

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

EC 1.14.1 With NADH or NADPH as one donor (deleted sub-subclass)

  • EC 1.14.1.1: now EC 1.14.14.1, unspecific monooxygenase
  • EC 1.14.1.2: now EC 1.14.13.9, kynurenine 3-monooxygenase
  • EC 1.14.1.3: deleted, covered by EC 1.14.99.7, squalene monooxygenase and EC 5.4.99.7, lanosterol synthase
  • EC 1.14.1.4: now EC 1.14.99.2, kynurenine 7,8-hydroxylase
  • EC 1.14.1.5: now EC 1.14.13.5; imidazoleacetate 4-monooxygenase
  • EC 1.14.1.6: now EC 1.14.15.4, steroid 11β-monooxygenase
  • EC 1.14.1.7: now EC 1.14.99.9, steroid 17α-monooxygenase
  • EC 1.14.1.8: now EC 1.14.99.10, steroid 21-monooxygenase
  • EC 1.14.1.9: deleted
  • EC 1.14.1.10: now EC 1.14.99.11 estradiol 6β-monooxygenase
  • EC 1.14.1.11: deleted

EC 1.14.2 With ascorbate as one donor (deleted sub-subclass)

  • EC 1.14.2.1: now EC 1.14.17.1, dopamine β-monooxygenase
  • EC 1.14.2.2: now EC 1.13.11.27, 4-hydroxyphenylpyruvate dioxygenase

EC 1.14.3 With reduced pteridine as one donor (deleted sub-subclass)

  • EC 1.14.3.1: now EC 1.14.16.1, phenylalanine 4-monooxygenase

EC 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors

EC 1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor

*No Misplaced Pages article

EC 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

Most of the entries from here on have no Misplaced Pages articles

EC 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen

Most of the entries from here on have no Misplaced Pages articles

EC 1.14.15 With reduced iron–sulfur protein as one donor, and incorporation of one atom of oxygen

Most entries from here on have no Misplaced Pages articles

EC 1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor

EC 1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor

EC 1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor

*No Misplaced Pages article

EC 1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water

Most of the entries from here on have no Misplaced Pages articles

EC 1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated

*No Misplaced Pages article

EC 1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated

*No Misplaced Pages article

EC 1.14.99 Miscellaneous

Most of the entries from here on have no Misplaced Pages article

EC 1.15 Acting on superoxide as acceptor

EC 1.15.1

EC 1.16 Oxidizing metal ions

EC 1.16.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.16.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.16.5 With a quinone or similar compound as acceptor

  • EC 1.16.5.1: Now EC 7.2.1.3, ascorbate ferrireductase (transmembrane)

EC 1.16.8 With a flavin as acceptor

  • EC 1.16.8.1: activity now known to be catalyzed by EC 2.5.1.17, corrinoid adenosyltransferase

EC 1.16.9 With a copper protein as acceptor

EC 1.16.98 With other, known, physiological acceptors

  • EC 1.16.98.1: Now EC 1.16.9.1 iron:rusticyanin reductase

EC 1.16.99 With unknown physiological acceptors

EC 1.17 Acting on CH or CH2 groups

EC 1.17.1 With NAD or NADP as acceptor

*No Misplaced Pages article

EC 1.17.2 With a cytochrome as acceptor

*No Misplaced Pages article

EC 1.17.3 With oxygen as acceptor

*No Misplaced Pages article

EC 1.17.4 With a disulfide as acceptor

*No Misplaced Pages article

EC 1.17.5 With a quinone or similar compound as acceptor

*No Misplaced Pages article

EC 1.17.7 With an iron–sulfur protein as acceptor

*No Misplaced Pages article

EC 1.17.98 With other, known, physiological acceptors

  • EC 1.17.98.1: bile-acid 7α-dehydroxylase. Now known to be catalyzed by multiple enzymes.
  • EC 1.17.98.2: bacteriochlorophyllide c C-7-hydroxylase *
  • EC 1.17.98.3: formate dehydrogenase (coenzyme F420) *
  • EC 1.17.98.4: formate dehydrogenase (hydrogenase) *
*No Misplaced Pages article

EC 1.17.99 With unknown physiological acceptors

No Misplaced Pages article for any of these
  • EC 1.17.99.1: Now EC 1.17.9.1, 4-methylphenol dehydrogenase (hydroxylating)
  • EC 1.17.99.2: ethylbenzene hydroxylase
  • EC 1.17.99.3: 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase
  • EC 1.17.99.4: uracil/thymine dehydrogenase
  • EC 1.17.99.5: Now classified as EC 1.17.98.1, bile-acid 7α-dehydroxylase
  • EC 1.17.99.6: epoxyqueuosine reductase
  • EC 1.17.99.7: Now classified as EC 1.17.98.4, formate dehydrogenase (hydrogenase)
  • EC 1.17.99.8: limonene dehydrogenase
  • EC 1.17.99.9: heme a synthase
  • EC 1.17.99.10: steroid C-25 hydroxylase
  • EC 1.17.99.11: 3-oxo-Δ-steroid hydratase/dehydrogenase

EC 1.18 Acting on iron–sulfur proteins as donors

EC 1.18.1 With NAD or NADP as acceptor

EC 1.18.2 With dinitrogen as acceptor (deleted sub-subclass)

EC 1.18.3 With H as acceptor (deleted sub-subclass)

  • EC 1.18.3.1: Now EC 1.12.7.2, ferredoxin hydrogenase

EC 1.18.6 With dinitrogen as acceptor

*No Misplaced Pages article

EC 1.18.96 With other, known, acceptors (deleted sub-subclass)

  • EC 1.18.96.1: Now EC 1.15.1.2, superoxide reductase

EC 1.18.99 With H as acceptor (deleted sub-subclass)

  • EC 1.18.99.1: Now EC 1.12.7.2, ferredoxin hydrogenase

EC 1.19 Acting on reduced flavodoxin as donor

EC 1.19.1 With NAD or NADP as acceptor

EC 1.19.6 With dinitrogen as acceptor

EC 1.20 Acting on phosphorus or arsenic in donors

EC 1.20.1 Acting on phosphorus or arsenic in donors, with NAD as acceptor

EC 1.20.2 Acting on phosphorus or arsenic in donors, with NAD(P) as acceptor

EC 1.20.4 Acting on phosphorus or arsenic in donors, with disulfide as acceptor

*No Misplaced Pages article

EC 1.20.9 With a copper protein as acceptor

EC 1.20.98 With other, known acceptors

  • EC 1.20.98.1: Now EC 1.20.9.1, arsenate reductase (azurin)

EC 1.20.99 With unknown physiological acceptors

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

EC 1.21.3 With oxygen as acceptor

EC 1.21.4 With a disulfide as acceptor

*No Misplaced Pages article

EC 1.21.98 With other, known, physiological acceptors

  • EC 1.21.98.1: cyclic dehypoxanthinyl futalosine synthase *
  • EC 1.21.98.2: dichlorochromopyrrolate synthase *
  • EC 1.21.98.3: anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase *
  • EC 1.21.98.4: PqqA peptide cyclase *
*No Misplaced Pages article

EC 1.21.99 With unknown physiological acceptors

*No Misplaced Pages article

EC 1.22 Acting on halogen in donors

EC 1.22.1 With NAD or NADP as acceptor

  • EC 1.22.1.1: Now EC 1.21.1.1, iodotyrosine deiodinase

EC 1.23 Reducing C-O-C group as acceptor

EC 1.23.1 With NADH or NADPH as donor

*No Misplaced Pages article

EC 1.97 Other oxidoreductases

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

EC 1.98 Enzymes using H2 as reductant (deleted subclass)

EC 1.98.1.1: Now EC 1.12.7.2, ferredoxin hydrogenase

EC 1.99 Other enzymes using O2 as oxidant

EC 1.99.1 Hydroxylases (now covered by EC 1.14)

  • EC 1.99.1.1: deleted, Now EC 1.12.7.2, ferredoxin hydrogenase
  • EC 1.99.1.2: deleted, Now EC 1.14.16.1, phenylalanine 4-monooxygenase
  • EC 1.99.1.3: deleted, nicotinate 6-hydroxylase
  • EC 1.99.1.4: deleted, tryptophan 5-hydroxylase
  • EC 1.99.1.5: deleted, Now EC 1.14.13.9, kynurenine 3-monooxygenase
  • EC 1.99.1.6: deleted, steroid 11α-hydroxylase
  • EC 1.99.1.7: deleted, Now EC 1.14.15.4, steroid 11β-monooxygenase
  • EC 1.99.1.8: deleted, steroid 6β-hydroxylase
  • EC 1.99.1.9: deleted, Now EC 1.14.99.9, steroid 17α-monooxygenase
  • EC 1.99.1.10: deleted, steroid 19-hydroxylase
  • EC 1.99.1.11: deleted, Now EC 1.14.99.10, steroid 21-monooxygenase
  • EC 1.99.1.12: deleted, alkoxyaryl hydroxylase
  • EC 1.99.1.13: deleted, covered by EC 1.14.99.7 (squalene monooxygenase) and by EC 5.4.99.7 (lanosterol synthase)
  • EC 1.99.1.14: deleted, Now EC 1.13.11.27, 4-hydroxyphenylpyruvate dioxygenase

EC 1.99.2 Oxygenases (now covered by EC 1.13)

  • EC 1.99.2.1: deleted, now EC 1.13.11.12, lipoxygenase
  • EC 1.99.2.2: deleted, now EC 1.13.11.1, catechol 1,2-dioxygenase
  • EC 1.99.2.3: deleted, now EC 1.13.11.3, protocatechuate 3,4-dioxygenase
  • EC 1.99.2.4: deleted, now EC 1.13.11.4, gentisate 1,2-dioxygenase
  • EC 1.99.2.5: deleted, now EC 1.13.11.5, homogentisate 1,2-dioxygenase
  • EC 1.99.2.6: deleted, now EC 1.13.99.1, inositol oxygenase
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor
1.1.2: cytochrome acceptor
1.1.3: oxygen acceptor
1.1.4: disulfide as acceptor
1.1.5: quinone/similar acceptor
1.1.99: other acceptors
Aldehyde/oxo oxidoreductases (EC 1.2)
1.2.1: NAD or NADP
1.2.2: cytochrome
1.2.3: oxygen
1.2.4: disulfide
1.2.7: iron–sulfur protein
Oxidoreductases: CH–CH oxidoreductases (EC 1.3)
1.3.1: NAD/NADP acceptor
1.3.3: Oxygen acceptor
1.3.5: Quinone
1.3.99: Other acceptors
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases
1.4.1: NAD/NADP acceptor
1.4.3: oxygen acceptor
1.4.4: disulfide acceptor
1.4.99: other acceptors
Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor
1.5.3: oxygen acceptor
1.5.5: quinone acceptor
1.5.99
Oxidoreductases: NADH or NADPH (EC 1.6)
1.6.1: NAD/NADP
1.6.2: Heme
1.6.3: Oxygen
1.6.5: Quinone or similar
1.6.6: Nitrogenous group
1.6.99: other
Oxidoreductases: nitrogenous donor (EC 1.7)
1.7.1
1.7.2
1.7.3
1.7.7
1.7.99
Oxidoreductases: sulfur oxidoreductases (EC 1.8)
1.8.1: NAD or NADP
1.8.2: cytochrome
1.8.3: oxygen
1.8.4: disulfide
1.8.5: quinone
1.8.98: Other, known
1.8.99: Other
Oxidoreductases: Acting on a heme group of donors (EC 1.9)
1.9.3
1.9.6
1.9.99
Oxidoreductases: diphenol family (EC 1.10)
1.10.1
1.10.2
1.10.3
1.10.99
Other
Oxidoreductases: peroxidases (EC 1.11)
1.11.1.1-14
1.11.1.15 (peroxiredoxin)
Oxidoreductases: Acting on hydrogen as donor (EC 1.12)
1.12.1
1.12.2
1.12.5
1.12.7
1.10.98
1.10.99
Oxidoreductases: monooxygenases (EC 1.13)
1.13.11: two atoms of oxygen
1.13.12: one atom of oxygen
1.13.99: other
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate
1.14.13: NADH or NADPH
1.14.14: reduced flavin or flavoprotein
1.14.15: reduced iron–sulfur protein
1.14.16: reduced pteridine (BH4 dependent)
1.14.17: reduced ascorbate
1.14.18-19: other
1.14.99 - miscellaneous
Other oxidoreductases (EC 1.15–1.21)
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: Acting on X-H and Y-H to form an X-Y bond
Portal:

References

  1. "ExplorEnz – The Enzyme Database".
  2. McDonald, A.G.; Boyce, S.; K.F., Tipton (2009). "ExplorEnz: the primary source of the IUBMB enzyme list". Nucleic Acids Res. 37 (Database issue): D593–D597. doi:10.1093/nar/gkn582. PMC 2686581. PMID 18776214.
Categories: