酸化還元酵素、オキシドレダクターゼ
- 関
- 酸化還元酵素 dehydrogenase oxidase reductase
WordNet
- an enzyme that catalyzes oxidation-reduction
- any of the enzymes that catalyze biological oxidation
- an enzyme that catalyses the biochemical reduction of some specified substance
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2018/01/10 21:50:56」(JST)
[Wiki en表示]
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.[1][2]
Contents
- 1 Reactions
- 2 Nomenclature
- 3 Classification
- 4 See also
- 5 References
- 6 External links
Reactions
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
- Hydroxylase
- List of enzymes
References
- ^ Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 ed.). Wiley-Interscience. ISBN 0471205036.
- ^ Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third ed.). USA: Oxford University Press. ISBN 019850229X.
External links
- EC 1 Introduction from the Department of Chemistry at Queen Mary, University of London
|
Oxidoreductases: alcohol oxidoreductases (EC 1.1)
|
| 1.1.1: NAD/NADP acceptor |
- 3-hydroxyacyl-CoA dehydrogenase
- 3-hydroxybutyryl-CoA dehydrogenase
- Alcohol dehydrogenase
- Aldo-keto reductase
- 1A1
- 1B1
- 1B10
- 1C1
- 1C3
- 1C4
- 7A2
- Aldose reductase
- Beta-Ketoacyl ACP reductase
- Carbohydrate dehydrogenases
- Carnitine dehydrogenase
- D-malate dehydrogenase (decarboxylating)
- DXP reductoisomerase
- Glucose-6-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
- HMG-CoA reductase
- IMP dehydrogenase
- Isocitrate dehydrogenase
- Lactate dehydrogenase
- L-threonine dehydrogenase
- L-xylulose reductase
- Malate dehydrogenase
- Malate dehydrogenase (decarboxylating)
- Malate dehydrogenase (NADP+)
- Malate dehydrogenase (oxaloacetate-decarboxylating)
- Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
- Phosphogluconate dehydrogenase
- Sorbitol dehydrogenase
- Hydroxysteroid dehydrogenase: 3β
- 11β
- 17β
|
| 1.1.2: cytochrome acceptor |
- D-lactate dehydrogenase (cytochrome)
- D-lactate dehydrogenase (cytochrome c-553)
- Mannitol dehydrogenase (cytochrome)
|
| 1.1.3: oxygen acceptor |
- Glucose oxidase
- L-gulonolactone oxidase
- Xanthine oxidase
|
| 1.1.4: disulfide as acceptor |
- Vitamin K epoxide reductase
- Vitamin-K-epoxide reductase (warfarin-insensitive)
|
| 1.1.5: quinone/similar acceptor |
- Malate dehydrogenase (quinone)
- Quinoprotein glucose dehydrogenase
|
| 1.1.99: other acceptors |
- Choline dehydrogenase
- L2HGDH
|
|
Aldehyde/oxo oxidoreductases (EC 1.2)
|
| 1.2.1: NAD or NADP |
- Aldehyde dehydrogenase
- Acetaldehyde dehydrogenase
- Long-chain-aldehyde dehydrogenase
|
| 1.2.2: cytochrome |
- Formate dehydrogenase (cytochrome)
|
| 1.2.3: oxygen |
|
| 1.2.4: disulfide |
- Oxoglutarate dehydrogenase complex
- Pyruvate dehydrogenase
- Branched-chain alpha-keto acid dehydrogenase complex
|
| 1.2.7: iron-sulfur protein |
|
|
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
- Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase
|
| 1.3.3: Oxygen acceptor |
- Dihydroorotate dehydrogenase
- Coproporphyrinogen III oxidase
- Protoporphyrinogen oxidase
- Bilirubin oxidase
- Acyl-CoA oxidase
- Dihydrouracil oxidase
- Tetrahydroberberine oxidase
- Secologanin synthase
- Tryptophan alpha,beta-oxidase
- Pyrroloquinoline-quinone synthase
- L-galactonolactone oxidase
|
| 1.3.5: Quinone |
|
| 1.3.99: Other acceptors |
- Fumarate reductase
- Butyryl-CoA dehydrogenase
- Acyl CoA dehydrogenase
- 5α-reductase
- Glutaryl-CoA dehydrogenase
- Isovaleryl coenzyme A dehydrogenase
- 3-oxo-5beta-steroid 4-dehydrogenase
|
|
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases
|
| 1.4.1: NAD/NADP acceptor |
- Glutamate dehydrogenase
- Glutamate synthase (NADPH)
|
| 1.4.3: oxygen acceptor |
- D-amino acid oxidase
- Amine oxidase (Copper-containing (Lysyl
- Diamine
- Primary-amine)) (Flavin-containing (Monoamine)))
|
| 1.4.4: disulfide acceptor |
|
| 1.4.99: other acceptors |
- D-amino acid dehydrogenase
- Amine dehydrogenase
|
|
Oxidoreductases: CH-NH (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
- Proline oxidase
|
| 1.5.5: quinone acceptor |
- Electron-transferring-flavoprotein dehydrogenase
|
| 1.5.99 |
- Sarcosine dehydrogenase
- Cytokinin dehydrogenase
|
|
Oxidoreductases: NADH or NADPH (EC 1.6)
|
| 1.6.1: NAD/NADP |
- NAD(P)+ transhydrogenase (Si-specific)
- NAD(P)+ transhydrogenase (Re/Si-specific)
|
| 1.6.2: Heme |
- Methemoglobin reductase
- NADPH—hemoprotein reductase/Cytochrome P450 reductase
- NADPH—cytochrome-c2 reductase
- Leghemoglobin reductase
|
| 1.6.3: Oxygen |
- NADPH oxidase
- P91-PHOX
- Neutrophil cytosolic factor 1
- Neutrophil cytosolic factor 2
- Neutrophil cytosolic factor 4
- dual oxidase
- Dual oxidase 1
- Dual oxidase 2
|
| 1.6.5: Quinone or similar |
|
| 1.6.6: Nitrogenous group |
- Trimethylamine-N-oxide reductase
|
| 1.6.99: other |
- NADH dehydrogenase (quinone)
|
|
Oxidoreductases: nitrogenous donor (EC 1.7)
|
| 1.7.1 |
|
| 1.7.2 |
- Nitrite reductase (NO-forming)
|
| 1.7.3 |
|
| 1.7.7 |
- Ferredoxin—nitrite reductase
|
| 1.7.99 |
|
|
Oxidoreductases: sulfur oxidoreductases (EC 1.8)
|
| 1.8.1: NAD or NADP |
- Dihydrolipoamide dehydrogenase
- Glutathione reductase
- Thioredoxin reductase
|
| 1.8.2: cytochrome |
- Sulfite dehydrogenase
- Thiosulfate dehydrogenase
|
| 1.8.3: oxygen |
|
| 1.8.4: disulfide |
- Glutathione—homocystine transhydrogenase
|
| 1.8.5: quinone |
- Glutathione dehydrogenase (ascorbate)
|
| 1.8.98: Other, known |
- CoB—CoM heterodisulfide reductase
|
| 1.8.99: Other |
|
|
Oxidoreductases: Acting on a heme group of donors (EC 1.9)
|
| 1.9.3 |
|
| 1.9.6 |
- Nitrate reductase (cytochrome)
|
| 1.9.99 |
- Iron—cytochrome-c reductase
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|
Oxidoreductases: diphenol family (EC 1.10)
|
| 1.10.1 |
- Trans-acenaphthene-1,2-diol dehydrogenase
|
| 1.10.2 |
- Coenzyme Q - cytochrome c reductase
|
| 1.10.3 |
|
| 1.10.99 |
|
| Other |
|
|
Oxidoreductases: peroxidases (EC 1.11)
|
| 1.11.1.1-14 |
- Catalase
- Cytochrome c peroxidase
- Eosinophil peroxidase
- Glutathione peroxidase
- Horseradish peroxidase
- Lactoperoxidase
- Myeloperoxidase
- Thyroid peroxidase
- Deiodinase
- Iodothyronine deiodinase
- Iodotyrosine deiodinase
|
| 1.11.1.15 (peroxiredoxin) |
|
|
Oxidoreductases: Acting on hydrogen as donor (EC 1.12)
|
| 1.12.1 |
- Hydrogen dehydrogenase
- Hydrogen dehydrogenase (NADP+)
- Hydrogenase (NAD+, ferredoxin)
|
| 1.12.2 |
- Cytochrome-c3 hydrogenase
|
| 1.12.5 |
- Hydrogen:quinone oxidoreductase
|
| 1.12.7 |
|
| 1.10.98 |
- Coenzyme F420 hydrogenase
- 5,10-Methenyltetrahydromethanopterin hydrogenase
- Methanosarcina-phenazine hydrogenase
- Sulfhydrogenase
|
| 1.10.99 |
|
|
Oxidoreductases: monooxygenases (EC 1.13)
|
| 1.13.11: two atoms of oxygen |
- lipoxygenase: Arachidonate 5-lipoxygenase
- Arachidonate 12-lipoxygenase/ALOX12
- Arachidonate 8-lipoxygenase
- Arachidonate 15-lipoxygenase/ALOX15
- Linoleate 11-lipoxygenase
- other dioxygenase: Catechol dioxygenase
- Homogentisate 1,2-dioxygenase
- Cysteine dioxygenase
- 4-Hydroxyphenylpyruvate dioxygenase
- Indoleamine 2,3-dioxygenase
- Chlorite dismutase
|
| 1.13.12: one atom of oxygen |
|
| 1.13.99: other |
|
|
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
- Lanosterol 14 alpha-demethylase
- 24-hydroxycholesterol 7α-hydroxylase
|
| 1.14.14: reduced flavin or flavoprotein |
|
| 1.14.15: reduced iron-sulfur protein |
|
| 1.14.16: reduced pteridine (BH4 dependent) |
- 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 1.15-1.21)
|
| 1.15: Acting on superoxide as acceptor |
|
| 1.16: Oxidizing metal ions |
|
| 1.17: Acting on CH or CH2 groups |
- Xanthine oxidase
- Ribonucleotide reductase
- 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
|
| 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 |
- Isopenicillin N synthase
- Columbamine oxidase
- Reticuline oxidase
- Sulochrin oxidase
- (+)-bisdechlorogeodin-forming
- (-)-bisdechlorogeodin-forming
- Aureusidin synthase
- Tetrahydrocannabinolic acid synthase
- Cannabidiolic acid synthase
- Dichlorochromopyrrolate synthase
|
|
Enzymes
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
|
UpToDate Contents
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English Journal
- Drosophila CYP6g1 and its human homolog CYP3A4 confer tolerance to methylmercury during development.
- Rand MD, Lowe JA, Mahapatra CT.SourceDepartment of Anatomy and Neurobiology, College of Medicine, University of Vermont, Burlington, VT 05405, United States.
- Toxicology.Toxicology.2012 Oct 9;300(1-2):75-82. Epub 2012 Jun 12.
- Methylmercury (MeHg) is a persistent environmental toxicant that is commonly encountered through dietary fish and seafood. While the fetal nervous system is a well-known primary target for MeHg toxicity, the risks of MeHg exposures that are commonly experienced today through diet and environmental e
- PMID 22699155
- Comparative structural modeling of a monothiol GRX from chickpea: Insight in iron-sulfur cluster assembly.
- Yadav S, Kushwaha HR, Kumar K, Verma PK.SourcePlant Immunity Laboratory, National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi 110067, India.
- International journal of biological macromolecules.Int J Biol Macromol.2012 Oct;51(3):266-73. Epub 2012 May 18.
- Glutaredoxins (GRXs) are small, ubiquitous, multifunctional, heat-stable and glutathione-dependent thiol-disulphide oxidoreductases, classified under thioredoxin-fold superfamily. In the green lineage, GRXs constitute a complex family of proteins. Based on their active site, GRXs are classified into
- PMID 22613454
Japanese Journal
- Kinetics of NADP+/NADPH reduction–oxidation catalyzed by the ferredoxin-NAD(P)+ reductase from the green sulfur bacterium Chlorobaculum tepidum
- A microfluidic-based protein crystallization method in 10 micrometer-sized crystallization space
- Roles of subunit NuoL in the proton pumping coupling mechanism of NADH : ubiquinone oxidoreductase (complex I) from Escherichia coli
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Related Pictures
★リンクテーブル★
[★]
- (酵素)還元酵素、レダクターゼ、リダクターゼ
- 関
- dehydrogenase、oxidase、oxidoreductase、reducing enzyme
[★]
- 英
- oxidoreductase
- 関
- オキシダーゼ、酸化還元酵素、デヒドロゲナーゼ、レダクターゼ
[★]
- 英
- oxidoreductase
- 同
- オキシドレダクターゼ
- 関
- 脱水素酵素、酵素、レダクターゼ
[★]
[★]
アルコール酸化還元酵素
[★]
NADH-NADPH酸化還元酵素
[★]
分子内酸化還元酵素
[★]
- 関
- See also specific type