Oxidoreductase
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Overview
Oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydrogen acceptor or electron donor) to another (the oxidant, also called the hydrogen donor or electron acceptor). For example, an enzyme that catalyzed this reaction would be an oxidoreductase:
- A– + B → A + B–
In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor).
In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:
- Pi + glyceraldehyde-3-phosphate + NAD+ → NADH + H+ + 1,3-bisphosphoglycerate
In this reaction, NAD+ is the oxidant (electron acceptor), and glyceraldehyde-3-phosphate is the reductant (electron donor).
Nomenclature
Proper names of oxidoreductases are formed as "donor:acceptor oxidoreductase." However, other names are much more common. The common name is "donor dehydrogenase" when possible, such as glyceraldehyde-3-phosphate dehydrogenase for the second reaction above. Common names are also sometimes formed as "acceptor reductase", such as NAD+ reductase. "Donor oxidase" is a special case where O2 is the acceptor.
Classification
Oxidoreductases are classified as EC 1 in the EC number classification of enzymes. Oxidoreductases can be further classified into 22 subclasses:
- EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (alcohol oxidoreductases)
- EC 1.2 includes oxidoreductases that act on the aldehyde or oxo group of donors
- EC 1.3 includes oxidoreductases that act on the CH-CH group of donors (CH-CH oxidoreductases)
- EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (Amino acid oxidoreductases, Monoamine oxidase)
- EC 1.5 includes oxidoreductases that act on CH-NH group of donors
- EC 1.6 includes oxidoreductases that act on NADH or NADPH
- EC 1.7 includes oxidoreductases that act on other nitrogenous compounds as donors
- EC 1.8 includes oxidoreductases that act on a sulfur group of donors
- EC 1.9 includes oxidoreductases that act on a heme group of donors
- EC 1.10 includes oxidoreductases that act on diphenols and related substances as donors
- EC 1.11 includes oxidoreductases that act on peroxide as an acceptor (peroxidases)
- EC 1.12 includes oxidoreductases that act on hydrogen as donors
- EC 1.13 includes oxidoreductases that act on single donors with incorporation of molecular oxygen (oxygenases)
- EC 1.14 includes oxidoreductases that act on paired donors with incorporation of molecular oxygen
- EC 1.15 includes oxidoreductases that act on superoxide radicals as acceptors
- EC 1.16 includes oxidoreductases that oxidize metal ions
- EC 1.17 includes oxidoreductases that act on CH or CH2 groups
- EC 1.18 includes oxidoreductases that act on iron-sulfur proteins as donors
- EC 1.19 includes oxidoreductases that act on reduced flavodoxin as a donor
- EC 1.20 includes oxidoreductases that act on phosphorus or arsenic in donors
- EC 1.21 includes oxidoreductases that act on X-H and Y-H to form an X-Y bond
- EC 1.97 includes other oxidoreductases
See also
External link
- EC 1 Introduction from the Department of Chemistry at Queen Mary, University of London
Proteins: enzymes | |
|---|---|
| Topics | Active site - Allosteric regulation - Binding site - Catalytically perfect enzyme - Coenzyme - Cofactor - Cooperativity - EC number Enzyme catalysis - Enzyme inhibitor - Enzyme kinetics - Lineweaver-Burk plot - Michaelis-Menten kinetics - List of enzymes |
| Types | EC1 Oxidoreductases/list - EC2 Transferases/list - EC3 Hydrolases/list - EC4 Lyases/list - EC5 Isomerases/list - EC6 Ligases/list |
Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1 - NAD or NADP acceptor | Aldehyde dehydrogenase - Acetaldehyde dehydrogenase (ALDH2) - Glyceraldehyde 3-phosphate dehydrogenase - Long-chain-aldehyde dehydrogenase |
| 1.2.4 - disulfide acceptor | Oxoglutarate dehydrogenase - Pyruvate dehydrogenase - Branched-chain alpha-keto acid dehydrogenase complex |
Oxidoreductases: CH-CH oxidoreductases (EC 1.3) | |
|---|---|
| 1.3.1. NAD/NADP acceptor | Enoyl-acyl carrier protein reductase/Enoyl ACP reductase - 7-Dehydrocholesterol reductase - Biliverdin reductase - 2,4 Dienoyl-CoA reductase |
| 1.3.3. Oxygen acceptor | Dihydroorotate dehydrogenase - Coproporphyrinogen III oxidase - Protoporphyrinogen oxidase - |
| 1.3.5. Quinone | Succinate - coenzyme Q reductase |
| 1.3.99. Other acceptors | Fumarate reductase - Butyryl CoA dehydrogenase - Acyl CoA dehydrogenase - 5-alpha reductase - Glutaryl-CoA dehydrogenase - Isovaleryl coenzyme A dehydrogenase |
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1 - NAD/NADP acceptor | Glutamate dehydrogenase (GLUD1) |
| 1.4.3 - oxygen acceptor | D-amino acid oxidase - Amine oxidase - Lysyl oxidase - Monoamine oxidase |
| 1.4.4 - disulfide acceptor | Glycine decarboxylase complex |
| 1.4.99 - other acceptors | D-amino acid dehydrogenase - Amine dehydrogenase |
CH-NH oxidoreductases (EC 1.5) | |
|---|---|
| 1.5.1 - NAD or NADP acceptor | Dihydrofolate reductase - Saccharopine dehydrogenase - Methylenetetrahydrofolate reductase |
| 1.5.3 - oxygen acceptor | Dihydrobenzophenanthridine oxidase - Sarcosine oxidase |
| 1.5.5 - quinone acceptor | Electron-transferring-flavoprotein dehydrogenase |
NADH or NADPH oxidoreductases (EC 1.6) |
|---|
| Methemoglobin reductase - NADPH oxidase (P91-PHOX) - NADH dehydrogenase |
Oxidoreductases: nitrogenous donor (EC 1.7) |
|---|
| GMP reductase - Urate oxidase |
Oxidoreductases: sulfur oxidoreductases (EC 1.8) |
|---|
| Dihydrolipoamide dehydrogenase - Glutathione reductase - Thioredoxin reductase - Sulfite oxidase |
Diphenol family oxidoreductases (EC 1.10) |
|---|
| Coenzyme Q - cytochrome c reductase - Catechol oxidase - Laccase - Alternative oxidase |
Oxidoreductases: peroxidases (EC 1.11) |
|---|
| Catalase - Cytochrome c peroxidase - Eosinophil peroxidase - Glutathione peroxidase - Horseradish peroxidase - Lactoperoxidase - Myeloperoxidase - Thyroid peroxidase - Deiodinase (Tetraiodothyronine 5' deiodinase) |
Oxidoreductases: monooxygenases (EC 1.13) | |
|---|---|
| 1.13.11 - two atoms of oxygen | Catechol dioxygenase - Homogentisate 1,2-dioxygenase - Cysteine dioxygenase - 4-Hydroxyphenylpyruvate dioxygenase - Indoleamine 2,3-dioxygenase - Lipoxygenase (5) |
| 1.13.12 - one atom of oxygen | Firefly luciferase |
| 1.13.99 - other | Inositol oxygenase |
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) | |
|---|---|
| 1.14.11 - 2-oxoglutarate | Prolyl hydroxylase - Lysyl hydroxylase |
| 1.14.13 - NADH or NADPH | Flavin-containing monooxygenase - Nitric oxide synthase - Cholesterol 7 alpha-hydroxylase - Methane monooxygenase - 3A4 -51A1 |
| 1.14.14 - reduced flavin or flavoprotein | 19A1 - 2D6 - 2E1 |
| 1.14.15 - reduced iron-sulfur protein | 11B1 - 11B2 - 11A1 |
| 1.14.16 - reduced pteridine | Phenylalanine hydroxylase - Tyrosine hydroxylase - Tryptophan hydroxylase |
| 1.14.17 - reduced ascorbate | Dopamine beta hydroxylase |
| 1.14.18-19 - other | Tyrosinase - Stearoyl-CoA desaturase-1 |
| 1.14.99 - miscellaneous | Cyclooxygenase - Heme oxygenase (HMOX1) - Squalene monooxygenase - 17A1 - 21A2 |
Other oxidoreductases (EC 1.15-1.18) | |
|---|---|
| 1.15 - Acting on superoxide as acceptor | Superoxide dismutase |
| 1.16 - Oxidizing metal ions | Ceruloplasmin |
| 1.17 - Acting on CH or CH2 groups | Xanthine oxidase - Ribonucleotide reductase |
| 1.18 - Acting on iron-sulfur proteins as donors | Nitrogenase |
bg:Оксидоредуктаза ca:Oxidoreductasa cs:Oxidoreduktasa de:Oxidoreduktasenfr:Oxydo-réductase it:Ossidoreduttasi ja:酸化還元酵素
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

