Ranelic acid (T3D1709)
| Record Information | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Version | 2.0 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Creation Date | 2009-06-22 16:08:29 UTC | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Update Date | 2014-12-24 20:24:30 UTC | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Accession Number | T3D1709 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Identification | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Common Name | Ranelic acid | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Class | Small Molecule | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Description | Ranelic acid is an organic acid capable of chelating metal cations. (4) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Compound Type |
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| Chemical Structure |  | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Synonyms |
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| Chemical Formula | C7H9ClO4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Average Molecular Mass | 192.597 g/mol | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Monoisotopic Mass | 192.019 g/mol | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CAS Registry Number | 5459-90-4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| IUPAC Name | 1-(acetyloxy)-2-chloroprop-2-en-1-yl acetate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Traditional Name | 1-(acetyloxy)-2-chloroprop-2-en-1-yl acetate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SMILES | CC(=O)OC(OC(C)=O)C(Cl)=C | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InChI Identifier | InChI=1S/C7H9ClO4/c1-4(8)7(11-5(2)9)12-6(3)10/h7H,1H2,2-3H3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=PPHOKWJFQIHKNR-UHFFFAOYSA-N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chemical Taxonomy | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Description | belongs to the class of organic compounds known as acylals. These are diesters of geminal diols. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Organic compounds | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Super Class | Organic acids and derivatives | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Class | Carboxylic acids and derivatives | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sub Class | Carboxylic acid derivatives | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Direct Parent | Acylals | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative Parents | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Substituents |
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| Molecular Framework | Aliphatic acyclic compounds | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| External Descriptors | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological Properties | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Status | Detected and Not Quantified | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Origin | Exogenous | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Cellular Locations |
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| Biofluid Locations | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Tissue Locations | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Applications | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological Roles | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chemical Roles | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Physical Properties | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| State | Solid | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Appearance | White powder. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties |
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| Predicted Properties |
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| Spectra | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Spectra |
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| Toxicity Profile | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Route of Exposure | Oral (2) ; inhalation (2) ; dermal (2) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mechanism of Toxicity | Cyanide is an inhibitor of cytochrome c oxidase in the fourth complex of the electron transport chain (found in the membrane of the mitochondria of eukaryotic cells). It complexes with the ferric iron atom in this enzyme. The binding of cyanide to this cytochrome prevents transport of electrons from cytochrome c oxidase to oxygen. As a result, the electron transport chain is disrupted and the cell can no longer aerobically produce ATP for energy. Tissues that mainly depend on aerobic respiration, such as the central nervous system and the heart, are particularly affected. Cyanide is also known produce some of its toxic effects by binding to catalase, glutathione peroxidase, methemoglobin, hydroxocobalamin, phosphatase, tyrosinase, ascorbic acid oxidase, xanthine oxidase, succinic dehydrogenase, and Cu/Zn superoxide dismutase. Cyanide binds to the ferric ion of methemoglobin to form inactive cyanmethemoglobin. (3) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Cyanide is rapidly alsorbed through oral, inhalation, and dermal routes and distributed throughout the body. Cyanide is mainly metabolized into thiocyanate by either rhodanese or 3-mercaptopyruvate sulfur transferase. Cyanide metabolites are excreted in the urine. (2) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Toxicity Values | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Lethal Dose | 226 to 300 milligrams for an adult human (cyanide salts). (1) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Carcinogenicity (IARC Classification) | No indication of carcinogenicity to humans (not listed by IARC). | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Uses/Sources | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Minimum Risk Level | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Health Effects | Exposure to high levels of cyanide for a short time harms the brain and heart and can even cause coma, seizures, apnea, cardiac arrest and death. Chronic inhalation of cyanide causes breathing difficulties, chest pain, vomiting, blood changes, headaches, and enlargement of the thyroid gland. Skin contact with cyanide salts can irritate and produce sores. (2, 3) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Symptoms | Cyanide poisoning is identified by rapid, deep breathing and shortness of breath, general weakness, giddiness, headaches, vertigo, confusion, convulsions/seizures and eventually loss of consciousness. (2, 3) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Treatment | Antidotes to cyanide poisoning include hydroxocobalamin and sodium nitrite, which release the cyanide from the cytochrome system, and rhodanase, which is an enzyme occurring naturally in mammals that combines serum cyanide with thiosulfate, producing comparatively harmless thiocyanate. Oxygen therapy can also be administered. (3) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Normal Concentrations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Abnormal Concentrations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| External Links | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| DrugBank ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HMDB ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PubChem Compound ID | 79576 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ChEMBL ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ChemSpider ID | 71884 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| UniProt ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| OMIM ID | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ChEBI ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| BioCyc ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CTD ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Stitch ID | Ranelic acid | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PDB ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ACToR ID | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Wikipedia Link | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| References | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Synthesis Reference | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| General References |
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| Gene Regulation | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Up-Regulated Genes | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Down-Regulated Genes | Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Targets
- General Function:
- Metal ion binding
- Specific Function:
- Not Available
- Gene Name:
- ALPPL2
- Uniprot ID:
- P10696
- Molecular Weight:
- 57376.515 Da
References
- Gerbitz KD: Human alkaline phosphatases. II. Metalloenzyme properties of the enzyme from human liver. Hoppe Seylers Z Physiol Chem. 1977 Nov;358(11):1491-7. [924371 ]
- General Function:
- Pyrophosphatase activity
- Specific Function:
- This isozyme may play a role in skeletal mineralization.
- Gene Name:
- ALPL
- Uniprot ID:
- P05186
- Molecular Weight:
- 57304.435 Da
References
- Gerbitz KD: Human alkaline phosphatases. II. Metalloenzyme properties of the enzyme from human liver. Hoppe Seylers Z Physiol Chem. 1977 Nov;358(11):1491-7. [924371 ]
- General Function:
- Receptor binding
- Specific Function:
- Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.
- Gene Name:
- CAT
- Uniprot ID:
- P04040
- Molecular Weight:
- 59755.82 Da
References
- Kang YS, Lee DH, Yoon BJ, Oh DC: Purification and characterization of a catalase from photosynthetic bacterium Rhodospirillum rubrum S1 grown under anaerobic conditions. J Microbiol. 2006 Apr;44(2):185-91. [16728955 ]
- General Function:
- Iron ion binding
- Specific Function:
- Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
- Gene Name:
- MT-CO1
- Uniprot ID:
- P00395
- Molecular Weight:
- 57040.91 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.
- Gene Name:
- MT-CO2
- Uniprot ID:
- P00403
- Molecular Weight:
- 25564.73 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX4I1
- Uniprot ID:
- P13073
- Molecular Weight:
- 19576.6 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX4I2
- Uniprot ID:
- Q96KJ9
- Molecular Weight:
- 20010.02 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Metal ion binding
- Specific Function:
- This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX5A
- Uniprot ID:
- P20674
- Molecular Weight:
- 16761.985 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Metal ion binding
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX5B
- Uniprot ID:
- P10606
- Molecular Weight:
- 13695.57 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX6A1
- Uniprot ID:
- P12074
- Molecular Weight:
- 12154.8 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX6A2
- Uniprot ID:
- Q02221
- Molecular Weight:
- 10815.32 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX6C
- Uniprot ID:
- P09669
- Molecular Weight:
- 8781.36 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX7A1
- Uniprot ID:
- P24310
- Molecular Weight:
- 9117.44 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX7A2
- Uniprot ID:
- P14406
- Molecular Weight:
- 9395.89 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Plays a role in proper central nervous system (CNS) development in vertebrates.
- Gene Name:
- COX7B
- Uniprot ID:
- P24311
- Molecular Weight:
- 9160.485 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX7B2
- Uniprot ID:
- Q8TF08
- Molecular Weight:
- 9077.43 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX7C
- Uniprot ID:
- P15954
- Molecular Weight:
- 7245.45 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX8A
- Uniprot ID:
- P10176
- Molecular Weight:
- 7579.0 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Cytochrome-c oxidase activity
- Specific Function:
- This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
- Gene Name:
- COX8C
- Uniprot ID:
- Q7Z4L0
- Molecular Weight:
- 8128.575 Da
References
- Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
- General Function:
- Glutathione peroxidase activity
- Specific Function:
- Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.
- Gene Name:
- GPX5
- Uniprot ID:
- O75715
- Molecular Weight:
- 25202.14 Da
References
- Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
- General Function:
- Zinc ion binding
- Specific Function:
- Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
- Gene Name:
- SOD3
- Uniprot ID:
- P08294
- Molecular Weight:
- 25850.675 Da
References
- Lee WG, Hwang JH, Na BK, Cho JH, Lee HW, Cho SH, Kong Y, Song CY, Kim TS: Functional expression of a recombinant copper/zinc superoxide dismutase of filarial nematode, Brugia malayi. J Parasitol. 2005 Feb;91(1):205-8. [15856906 ]
- General Function:
- Sh3 domain binding
- Specific Function:
- Protects the hemoglobin in erythrocytes from oxidative breakdown.
- Gene Name:
- GPX1
- Uniprot ID:
- P07203
- Molecular Weight:
- 22087.94 Da
References
- Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
- General Function:
- Glutathione peroxidase activity
- Specific Function:
- Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.
- Gene Name:
- GPX2
- Uniprot ID:
- P18283
- Molecular Weight:
- 21953.835 Da
References
- Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
- General Function:
- Transcription factor binding
- Specific Function:
- Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
- Gene Name:
- GPX3
- Uniprot ID:
- P22352
- Molecular Weight:
- 25552.185 Da
References
- Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
- General Function:
- Peroxidase activity
- Specific Function:
- It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.
- Gene Name:
- GPX7
- Uniprot ID:
- Q96SL4
- Molecular Weight:
- 20995.88 Da
References
- Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
- General Function:
- Nadp binding
- Specific Function:
- Maintains high levels of reduced glutathione in the cytosol.
- Gene Name:
- GSR
- Uniprot ID:
- P00390
- Molecular Weight:
- 56256.565 Da
References
- Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
- General Function:
- Phospholipid-hydroperoxide glutathione peroxidase activity
- Specific Function:
- Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage.
- Gene Name:
- GPX4
- Uniprot ID:
- P36969
- Molecular Weight:
- 22174.52 Da
References
- Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
- General Function:
- Ubiquinone binding
- Specific Function:
- Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
- Gene Name:
- SDHD
- Uniprot ID:
- O14521
- Molecular Weight:
- 17042.82 Da
References
- Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
- General Function:
- Succinate dehydrogenase activity
- Specific Function:
- Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
- Gene Name:
- SDHA
- Uniprot ID:
- P31040
- Molecular Weight:
- 72690.975 Da
References
- Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
- General Function:
- Ubiquinone binding
- Specific Function:
- Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
- Gene Name:
- SDHB
- Uniprot ID:
- P21912
- Molecular Weight:
- 31629.365 Da
References
- Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
- General Function:
- Succinate dehydrogenase activity
- Specific Function:
- Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
- Gene Name:
- SDHC
- Uniprot ID:
- Q99643
- Molecular Weight:
- 18610.03 Da
References
- Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
- General Function:
- Zinc ion binding
- Specific Function:
- Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
- Gene Name:
- SOD1
- Uniprot ID:
- P00441
- Molecular Weight:
- 15935.685 Da
References
- Lee WG, Hwang JH, Na BK, Cho JH, Lee HW, Cho SH, Kong Y, Song CY, Kim TS: Functional expression of a recombinant copper/zinc superoxide dismutase of filarial nematode, Brugia malayi. J Parasitol. 2005 Feb;91(1):205-8. [15856906 ]
- General Function:
- Protein homodimerization activity
- Specific Function:
- This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.
- Gene Name:
- TYR
- Uniprot ID:
- P14679
- Molecular Weight:
- 60392.69 Da
References
- Laufer Z, Beckett RP, Minibayeva FV: Co-occurrence of the multicopper oxidases tyrosinase and laccase in lichens in sub-order peltigerineae. Ann Bot. 2006 Nov;98(5):1035-42. Epub 2006 Sep 1. [16950829 ]