Lotaustralin (T3D0860)

IdentificationTaxonomyBiological PropertiesPhysical PropertiesToxicity ProfileSpectraConcentrationsLinksReferencesGene RegulationTargets (38)XML
Targets (38)
Record Information
Version2.0
Creation Date2009-06-10 21:44:10 UTC
Update Date2014-12-24 20:22:53 UTC
Accession NumberT3D0860
Identification
Common NameLotaustralin
ClassSmall Molecule
DescriptionEpilotaustralin is found in cereals and cereal products. Epilotaustralin is isolated from Triticum monococcum (wheat).
Compound Type
  • Cyanide Compound
  • Cyanogenic Glycoside
  • Food Toxin
  • Metabolite
  • Natural Compound
  • Nitrile
  • Organic Compound
  • Plant Toxin
Chemical Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
Synonym
2(R)-Hydroxy-2-methylbutyronitrile-beta-D-glucopyranoside
2-(beta-D-Glucopyranosyloxy)-2-methyl-(R)-Butanenitrile
Chemical FormulaC11H19NO6
Average Molecular Mass261.272 g/mol
Monoisotopic Mass261.121 g/mol
CAS Registry Number534-67-8
IUPAC Name(2R)-2-methyl-2-{[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}butanenitrile
Traditional Namelotaustralin
SMILES[H][C@]1(O)[C@]([H])(O)[C@@]([H])(CO)O[C@@]([H])(O[C@](C)(CC)C#N)[C@]1([H])O
InChI IdentifierInChI=1S/C11H19NO6/c1-3-11(2,5-12)18-10-9(16)8(15)7(14)6(4-13)17-10/h6-10,13-16H,3-4H2,1-2H3/t6-,7-,8+,9-,10+,11-/m1/s1
InChI KeyInChIKey=WEWBWVMTOYUPHH-QHAQEBJBSA-N
Chemical Taxonomy
Description belongs to the class of organic compounds known as cyanogenic glycosides. These are glycosides in which the aglycone moiety contains a cyanide group.
KingdomOrganic compounds
Super ClassOrganic oxygen compounds
ClassOrganooxygen compounds
Sub ClassCarbohydrates and carbohydrate conjugates
Direct ParentCyanogenic glycosides
Alternative Parents
Substituents
  • Cyanogenic glycoside
  • Hexose monosaccharide
  • O-glycosyl compound
  • Monosaccharide
  • Oxane
  • Secondary alcohol
  • Polyol
  • Organoheterocyclic compound
  • Oxacycle
  • Nitrile
  • Carbonitrile
  • Acetal
  • Primary alcohol
  • Organonitrogen compound
  • Hydrocarbon derivative
  • Organopnictogen compound
  • Organic nitrogen compound
  • Alcohol
  • Aliphatic heteromonocyclic compound
Molecular FrameworkAliphatic heteromonocyclic compounds
External Descriptors
  • cyanogenic glycoside (CHEBI:6542 )
  • Cyanogenic glucosides derived from valine or isoleucine (C08334 )
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceWhite powder.
Experimental Properties
PropertyValue
Melting Point139°C
Boiling PointNot Available
SolubilityNot Available
LogPNot Available
Predicted Properties
PropertyValueSource
Water Solubility62.3 g/LALOGPS
logP-0.88ALOGPS
logP-1.2ChemAxon
logS-0.62ALOGPS
pKa (Strongest Acidic)12.21ChemAxon
pKa (Strongest Basic)-3ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count7ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area123.17 ŲChemAxon
Rotatable Bond Count4ChemAxon
Refractivity59.47 m³·mol⁻¹ChemAxon
Polarizability25.22 ųChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyDeposition DateView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-06sl-9550000000-23b4f6c3304e8812d4562017-07-27View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0w30-7980000000-3a978648b67dd80be4fb2016-08-03View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0f89-9500000000-3e356cb2d2384f50f2ef2016-08-03View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-001i-9200000000-c8516406b94ec22f08412016-08-03View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03dj-9360000000-1ef57a95ad4f5883749b2016-08-03View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0002-9210000000-7218f7d717d10cb05f562016-08-03View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-00sj-9000000000-ddd71bad6904decc411d2016-08-03View Spectrum
Toxicity Profile
Route of ExposureOral
Mechanism of ToxicityOrganic nitriles decompose into cyanide ions both in vivo and in vitro. Consequently the primary mechanism of toxicity for organic nitriles is their production of toxic cyanide ions or hydrogen cyanide. 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)
MetabolismUpon exposure to enzymes and gut flora in the human intestine, lotaustralin can decompose to the toxic chemical hydrogen cyanide. This occurs via the enzyme linamarase, which is found in the cell wall of the plant. Chewing of the plant allows the enzyme to contact the lotaustralin converting it into acetone cyanohydrin, which then spontaneously decomposes to hydrogen cyanide. (4, 5) Organic nitriles are converted into cyanide ions through the action of cytochrome P450 enzymes in the liver. Cyanide is rapidly absorbed 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 ValuesNot Available
Lethal DoseNot Available
Carcinogenicity (IARC Classification)No indication of carcinogenicity to humans (not listed by IARC).
Uses/SourcesLotaustralin is a plant toxin found in the roots and leaves of plants such as cassava (Manihot esculenta), lima bean (Phaseolus lunatus), roseroot (Rhodiola rosea) and white clover (Trifolium repens). (5)
Minimum Risk LevelNot Available
Health EffectsDietary exposure to lotaustralin has been reported as a risk factor in developing glucose intolerance and diabetes. It may also cause the upper motor neuron disease known as konzo. (4, 5)
SymptomsCyanide 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)
TreatmentNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDHMDB33865
PubChem Compound ID4626626
ChEMBL IDNot Available
ChemSpider ID3817241
KEGG IDC08334
UniProt IDNot Available
OMIM ID
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDC001556
Stitch IDLotaustralin
PDB IDNot Available
ACToR IDNot Available
Wikipedia LinkLotaustralin
References
Synthesis ReferenceNot Available
MSDSNot Available
General References
  1. Yannai, Shmuel. (2004) Dictionary of food compounds with CD-ROM: Additives, flavors, and ingredients. Boca Raton: Chapman & Hall/CRC.
  2. ATSDR - Agency for Toxic Substances and Disease Registry (2006). Toxicological profile for cyanide. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  3. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
  4. Wikipedia. Linamarin. Last Updated 11 May 2009. [Link]
  5. Wikipedia. Lotaustralin. Last Updated 14 May 2009. [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

Target Details
1. Alkaline phosphatase, placental-like
General Function:
Metal ion binding
Specific Function:
Not Available
Gene Name:
ALPPL2
Uniprot ID:
P10696
Molecular Weight:
57376.515 Da
References
  1. 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 ]
Target Details
2. Alkaline phosphatase, tissue-nonspecific isozyme
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
  1. 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 ]
Target Details
3. Catalase
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
  1. 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 ]
Target Details
4. Cytochrome c oxidase subunit 1
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
5. Cytochrome c oxidase subunit 2
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
6. Cytochrome c oxidase subunit 3
General Function:
Cytochrome-c oxidase activity
Specific Function:
Subunits I, II and III form the functional core of the enzyme complex.
Gene Name:
MT-CO3
Uniprot ID:
P00414
Molecular Weight:
29950.6 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
7. Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
8. Cytochrome c oxidase subunit 4 isoform 2, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
9. Cytochrome c oxidase subunit 5A, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
10. Cytochrome c oxidase subunit 5B, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
11. Cytochrome c oxidase subunit 6A1, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
12. Cytochrome c oxidase subunit 6A2, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
13. Cytochrome c oxidase subunit 6B1
General Function:
Cytochrome-c oxidase activity
Specific Function:
Connects the two COX monomers into the physiological dimeric form.
Gene Name:
COX6B1
Uniprot ID:
P14854
Molecular Weight:
10192.345 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
14. Cytochrome c oxidase subunit 6B2
General Function:
Cytochrome-c oxidase activity
Specific Function:
Connects the two COX monomers into the physiological dimeric form.
Gene Name:
COX6B2
Uniprot ID:
Q6YFQ2
Molecular Weight:
10528.905 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
15. Cytochrome c oxidase subunit 6C
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
16. Cytochrome c oxidase subunit 7A1, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
17. Cytochrome c oxidase subunit 7A2, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
18. Cytochrome c oxidase subunit 7B, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
19. Cytochrome c oxidase subunit 7B2, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
20. Cytochrome c oxidase subunit 7C, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
21. Cytochrome c oxidase subunit 8A, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
22. Cytochrome c oxidase subunit 8C, mitochondrial
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
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
23. Epididymal secretory glutathione peroxidase
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
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
24. Extracellular superoxide dismutase [Cu-Zn]
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
  1. 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 ]
Target Details
25. Glutathione peroxidase 1
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
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
26. Glutathione peroxidase 2
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
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
27. Glutathione peroxidase 3
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
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
28. Glutathione peroxidase 6
General Function:
Glutathione peroxidase activity
Specific Function:
Not Available
Gene Name:
GPX6
Uniprot ID:
P59796
Molecular Weight:
24970.46 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
29. Glutathione peroxidase 7
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
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
30. Glutathione reductase, mitochondrial
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
  1. 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 ]
Target Details
31. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
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
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
32. Probable glutathione peroxidase 8
General Function:
Peroxidase activity
Specific Function:
Not Available
Gene Name:
GPX8
Uniprot ID:
Q8TED1
Molecular Weight:
23880.83 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
33. Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
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
  1. 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 ]
Target Details
34. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
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
  1. 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 ]
Target Details
35. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
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
  1. 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 ]
Target Details
36. Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
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
  1. 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 ]
Target Details
37. Superoxide dismutase [Cu-Zn]
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
  1. 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 ]
Target Details
38. Tyrosinase
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
  1. 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 ]