List of EC numbers (EC 1)

Last updated

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. [1] The database is developed and maintained by Andrew McDonald. [2]

Contents

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 Wikipedia articles

EC 1.1.2 With a cytochrome as acceptor

*No Wikipedia article

EC 1.1.3 With oxygen as acceptor

*No Wikipedia article

EC 1.1.4 With a disulfide as acceptor

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 Wikipedia article

EC 1.1.99 With unknown physiological acceptors

*No Wikipedia article

EC 1.2 Acting on the aldehyde or oxo group of donors

EC 1.2.1 With NAD+ or NADP+ as acceptor

* No Wikipedia article

EC 1.2.2 With a cytochrome as acceptor

EC 1.2.3 With oxygen as acceptor

* No Wikipedia article

EC 1.2.4 With a disulfide as acceptor

EC 1.2.5 With a quinone or similar compound as acceptor

*No Wikipedia article

EC 1.2.7 With an iron–sulfur protein as acceptor

*No Wikipedia article

EC 1.2.99: With unknown physiological acceptors

*No Wikipedia article

EC 1.3 Acting on the CH-CH group of donors

EC 1.3.1 With NAD+ or NADP+ as acceptor

*No Wikipedia article

EC 1.3.2 With a cytochrome as acceptor

EC 1.3.3 With oxygen as acceptor

EC 1.3.7 With an iron–sulfur protein as acceptor

EC 1.3.8 With a flavin as acceptor

*No Wikipedia article

EC 1.3.98 With FMN acceptor

*No Wikipedia article

EC 1.3.99 With unknown physiological acceptors

*No Wikipedia article

EC 1.4 Acting on the CH-NH2 group of donors

EC 1.4.1 With NAD+ or NADP+ as acceptor

*No Wikipedia article

EC 1.4.2 With a cytochrome as acceptor

EC 1.4.3 With oxygen as acceptor

*No Wikipedia 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 Wikipedia article

EC 1.5 Acting on the CH-NH group of donors

EC 1.5.1 With NAD+ or NADP+ as acceptor

*No Wikipedia article

EC 1.5.3 With oxygen as acceptor

*No Wikipedia article

EC 1.5.4 With a disulfide as acceptor

EC 1.5.5 With a quinone or similar compound as acceptor

*No Wikipedia article

EC 1.5.7 With an iron–sulfur protein as acceptor

*No Wikipedia article

EC 1.5.8 With a flavin or flavoprotein as acceptor

EC 1.5.98 With other, known, physiological acceptors

EC 1.5.99 With unknown physiological acceptors

*No Wikipedia 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 Wikipedia article

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

EC 1.6.5 With a quinone or similar compound as acceptor

*No Wikipedia article

EC 1.6.6 With a nitrogenous group as acceptor

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

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

EC 1.6.99 With unknown physiological acceptors

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 Wikipedia article

EC 1.7.3 With oxygen as acceptor

*No Wikipedia 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 Wikipedia article

EC 1.8.2 With a cytochrome as acceptor

*No Wikipedia article

EC 1.8.3 With oxygen as acceptor

*No Wikipedia article

EC 1.8.4 With a disulfide as acceptor

*No Wikipedia article

EC 1.8.5 With a quinone or similar compound as acceptor

*No Wikipedia 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 Wikipedia article

EC 1.8.98 With other, known, acceptors

EC 1.8.99 With other acceptors

*No Wikipedia article

EC 1.9 Acting on a heme group of donors

EC 1.9.3 With oxygen as acceptor

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 1.10.1 With NAD+ or NADP+ as acceptor

EC 1.10.2 With a cytochrome as acceptor

EC 1.10.3 With oxygen as acceptor

*No Wikipedia article
*No Wikipedia article

EC 1.10.9 With a copper protein as acceptor

EC 1.10.99 With unknown physiological acceptors

EC 1.11 Acting on a peroxide as acceptor

EC 1.11.1 Peroxidases

*No Wikipedia article

EC 1.11.2 Peroxygenase

*No Wikipedia article

EC 1.12 Acting on hydrogen as donor

EC 1.12.1 With NAD+ or NADP+ as acceptor

*No Wikipedia 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 Wikipedia article

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

*No Wikipedia 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 1.14.2 With ascorbate as one donor (deleted sub-subclass)

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

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 Wikipedia 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 Wikipedia 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 Wikipedia 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 Wikipedia 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 Wikipedia 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 Wikipedia articles

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

*No Wikipedia article

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

*No Wikipedia article

EC 1.14.99 Miscellaneous

Most of the entries from here on have no Wikipedia 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 Wikipedia article

EC 1.16.3 With oxygen as acceptor

*No Wikipedia article

EC 1.16.5 With a quinone or similar compound as acceptor

EC 1.16.8 With a flavin as acceptor

EC 1.16.9 With a copper protein as acceptor

EC 1.16.98 With other, known, physiological acceptors

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 Wikipedia article

EC 1.17.2 With a cytochrome as acceptor

*No Wikipedia article

EC 1.17.3 With oxygen as acceptor

*No Wikipedia article

EC 1.17.4 With a disulfide as acceptor

*No Wikipedia article

EC 1.17.5 With a quinone or similar compound as acceptor

*No Wikipedia article

EC 1.17.7 With an iron–sulfur protein as acceptor

*No Wikipedia article

EC 1.17.98 With other, known, physiological acceptors

*No Wikipedia article

EC 1.17.99 With unknown physiological acceptors

No Wikipedia article for any of these

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 1.18.6 With dinitrogen as acceptor

*No Wikipedia article

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

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

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 Wikipedia article

EC 1.20.9 With a copper protein as acceptor

EC 1.20.98 With other, known acceptors

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 Wikipedia article

EC 1.21.98 With other, known, physiological acceptors

*No Wikipedia article

EC 1.21.99 With unknown physiological acceptors

*No Wikipedia article

EC 1.22 Acting on halogen in donors

EC 1.22.1 With NAD+ or NADP+ as acceptor

EC 1.23 Reducing C-O-C group as acceptor

EC 1.23.1 With NADH or NADPH as donor

*No Wikipedia 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 1.99.2 Oxygenases (now covered by EC 1.13)

Related Research Articles

In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

<span class="mw-page-title-main">Cytochrome P450</span> Class of enzymes

Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. However, they are not omnipresent; for example, they have not been found in Escherichia coli. In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses. By hydroxylation, CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted.

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide phosphate</span> Chemical compound

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP+ is the oxidized form. NADP+ is used by all forms of cellular life.

Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

This is a list of topics in molecular biology. See also index of biochemistry articles.

Aromatic-ring-hydroxylating dioxygenases (ARHD) incorporate two atoms of dioxygen (O2) into their substrates in the dihydroxylation reaction. The product is (substituted) cis-1,2-dihydroxycyclohexadiene, which is subsequently converted to (substituted) benzene glycol by a cis-diol dehydrogenase.

Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.

Cytochrome b<sub>5</sub>

Cytochromes b5 are ubiquitous electron transport hemoproteins found in animals, plants, fungi and purple phototrophic bacteria. The microsomal and mitochondrial variants are membrane-bound, while bacterial and those from erythrocytes and other animal tissues are water-soluble. The family of cytochrome b5-like proteins includes hemoprotein domains covalently associated with other redox domains in flavocytochrome cytochrome b2, sulfite oxidase, plant and fungal nitrate reductases, and plant and fungal cytochrome b5/acyl lipid desaturase fusion proteins.

<span class="mw-page-title-main">Acyl-CoA dehydrogenase (NADP+)</span> Class of enzymes

In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction

In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) (EC 1.3.1.39) is an enzyme that catalyzes the chemical reaction

In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphatidylcholine desaturase (EC 1.14.19.22, previously EC 1.3.1.35) is an enzyme that catalyzes the chemical reaction

In enzymology, a Δ7-sterol 5(6)-desaturase is an enzyme that catalyzes the chemical reaction

In enzymology, a ferredoxin–NAD+ reductase (EC 1.18.1.3) is an enzyme that catalyzes the chemical reaction:

Flavoprotein pyridine nucleotide cytochrome reductases catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin-NADP+ reductases, plant and fungal NAD(P)H:nitrate reductases, cytochrome b5 reductases, cytochrome P450 reductases, sulphite reductases, nitric oxide synthases, phthalate dioxygenase reductase, and various other flavoproteins.

The biosynthesis of isoflavonoids involves several enzymes; These are:

Abieta-7,13-dien-18-ol hydroxylase (EC 1.14.13.109, CYP720B1, PTAO) is an enzyme with systematic name abieta-7,13-dien-18-ol,NADPH:oxygen oxidoreductase (18-hydroxylating). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Chlorophyllide</span> Chemical compound

Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.

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.