| 词条 | Trypanothione |
| 释义 |
| Verifiedfields = changed | verifiedrevid = 470618372 | Name=Trypanothione | ImageFile=Trypanothione(red).svg | ImageSize=280px | ImageFile1=Trypanothione(ox).svg | ImageSize1=270px | ImageName1=Trypanthione (oxidized) | ImageCaption1 = Reduced form (top) and oxidized form (bottom) | IUPACName= | OtherNames=N1,N8-Bis(glutathionyl)spermidine |Section1={{Chembox Identifiers | InChI = 1/C27H47N9O10S2/c28-16(26(43)44)4-6-20(37)35-18-14-47-48-15-19(36-21(38)7-5-17(29)27(45)46)25(42)34-13-23(40)32-11-3-9-30-8-1-2-10-31-22(39)12-33-24(18)41/h16-19,30H,1-15,28-29H2,(H,31,39)(H,32,40)(H,33,41)(H,34,42)(H,35,37)(H,36,38)(H,43,44)(H,45,46)/t16-,17-,18-,19-/m0/s1 | InChIKey = LZMSXDHGHZKXJD-VJANTYMQBI | StdInChI_Ref = {{stdinchicite|correct|chemspider}} | StdInChI = 1S/C27H47N9O10S2/c28-16(26(43)44)4-6-20(37)35-18-14-47-48-15-19(36-21(38)7-5-17(29)27(45)46)25(42)34-13-23(40)32-11-3-9-30-8-1-2-10-31-22(39)12-33-24(18)41/h16-19,30H,1-15,28-29H2,(H,31,39)(H,32,40)(H,33,41)(H,34,42)(H,35,37)(H,36,38)(H,43,44)(H,45,46)/t16-,17-,18-,19-/m0/s1 | StdInChIKey_Ref = {{stdinchicite|correct|chemspider}} | StdInChIKey = LZMSXDHGHZKXJD-VJANTYMQSA-N | CASNo_Ref = {{cascite|correct|CAS}} | CASNo=96304-42-6 | CASNo_Comment = (oxidized) | PubChem=115098 | PubChem_Comment = (oxidized) | ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} | ChemSpiderID = 102998 | ChemSpiderID_Comment = (oxidized) | ChemSpiderID1_Ref = {{chemspidercite|correct|chemspider}} | ChemSpiderID1 = 396023 | ChemSpiderID1_Comment = (reduced) | ChEBI_Ref = {{ebicite|correct|EBI}} | ChEBI = 35490 | SMILES = O=C(O)[C@@H](N)CCC(=O)N[C@@H]1C(=O)NCC(=O)NCCCNCCCCNC(=O)CNC(=O)[C@@H](NC(=O)CC[C@@H](C(=O)O)N)CSSC1 }} |Section2={{Chembox Properties | Formula=C27H47N9O10S2 (oxidized) C27H49N9O10S2 (reduced) | MolarMass=721.84 g/mol (oxidized) 723.86 g/mol (reduced) | Appearance= | Density= | MeltingPt= | BoilingPt= | Solubility= |Section3={{Chembox Hazards | MainHazards= | FlashPt= | AutoignitionPt = }}Trypanothione is an unusual form of glutathione containing two molecules of glutathione joined by a spermidine (polyamine) linker. It is found in parasitic protozoa such as leishmania and trypanosomes.[1] These protozoal parasites are the cause of leishmaniasis, sleeping sickness and Chagas' disease. Trypanothione was discovered by Alan Fairlamb. Its structure was proven by chemical synthesis.[2] It is unique to the Kinetoplastida and not found in other parasitic protozoa such as Entamoeba histolytica.[3] Since this thiol is absent from humans and is essential for the survival of the parasites, the enzymes that make and use this molecule are targets for the development of new drugs to treat these diseases.[4] Trypanothione-dependent enzymes include reductases, peroxidases, glyoxalases and transferases. Trypanothione-disulfide reductase (TryR) was the first trypanothione-dependent enzyme to be discovered (EC 1.8.1.12). It is an NADPH-dependent flavoenzyme that reduces trypanothione disulfide. TryR is essential for survival of these parasites both in vitro and in the human host.[5][6] A major function of trypanothione is in the defence against oxidative stress.[7] Here, trypanothione-dependent enzymes such as tryparedoxin peroxidase (TryP) reduce peroxides using electrons donated either directly from trypanothione, or via the redox intermediate tryparedoxin (TryX). Trypanothione-dependent hydrogen peroxide metabolism is particularly important in these organisms because they lack catalase. Since the trypanosomatids also lack an equivalent of thioredoxin reductase, trypanothione reductase is the sole path that electrons can take from NADPH to these antioxidant enzymes. References1. ^{{cite journal |vauthors=Fairlamb AH, Cerami A |title=Metabolism and functions of trypanothione in the Kinetoplastida |journal=Annu. Rev. Microbiol. |volume=46 |issue= |pages=695–729 |year=1992 |pmid=1444271 |doi=10.1146/annurev.mi.46.100192.003403 |url=http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.mi.46.100192.003403?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%3dncbi.nlm.nih.gov}} 2. ^{{Cite journal | pmid = 3883489 | date=Mar 1985 | last1 = Fairlamb | first1 = A. H. | last2 = Blackburn | first2 = P. | last3 = Ulrich | first3 = P. | last4 = Chait | first4 = B. T. | last5 = Cerami | first5 = A. | title = Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids | volume = 227 | issue = 4693 | pages = 1485–1487 | issn = 0036-8075 | journal = Science | doi = 10.1126/science.3883489|bibcode = 1985Sci...227.1485F }} 3. ^{{cite journal |vauthors=Ariyanayagam MR, Fairlamb AH |title=Entamoeba histolytica lacks trypanothione metabolism |journal=Mol. Biochem. Parasitol. |volume=103 |issue=1 |pages=61–9 |date=September 1999 |pmid=10514081 |url=http://linkinghub.elsevier.com/retrieve/pii/S0166-6851(99)00118-8 |doi=10.1016/S0166-6851(99)00118-8}} 4. ^{{cite journal |vauthors=Schmidt A, Krauth-Siegel RL |title=Enzymes of the trypanothione metabolism as targets for antitrypanosomal drug development |journal=Curr Top Med Chem |volume=2 |issue=11 |pages=1239–59 |date=November 2002 |pmid=12171583 |url=http://www.bentham-direct.org/pages/content.php?CTMC/2002/00000002/00000011/0005R.SGM |doi=10.2174/1568026023393048}} 5. ^{{cite journal |vauthors=Tovar J, Wilkinson S, Mottram JC, Fairlamb AH |title=Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus |journal=Mol. Microbiol. |volume=29 |issue=2 |pages=653–60 |date=July 1998 |pmid=9720880 |url=http://www3.interscience.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0950-382X&date=1998&volume=29&issue=2&spage=653 |archive-url=https://archive.today/20130105064851/http://www3.interscience.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0950-382X&date=1998&volume=29&issue=2&spage=653 |dead-url=yes |archive-date=2013-01-05 |doi=10.1046/j.1365-2958.1998.00968.x}} 6. ^{{cite journal |vauthors=Krieger S, Schwarz W, Ariyanayagam MR, Fairlamb AH, Krauth-Siegel RL, Clayton C |title=Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress |journal=Mol. Microbiol. |volume=35 |issue=3 |pages=542–52 |date=February 2000 |pmid=10672177 |url=http://www3.interscience.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0950-382X&date=2000&volume=35&issue=3&spage=542 |archive-url=https://archive.today/20130105144742/http://www3.interscience.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0950-382X&date=2000&volume=35&issue=3&spage=542 |dead-url=yes |archive-date=2013-01-05 |doi=10.1046/j.1365-2958.2000.01721.x}} 7. ^{{cite journal |vauthors=Krauth-Siegel RL, Meiering SK, Schmidt H |title=The parasite-specific trypanothione metabolism of trypanosoma and leishmania |journal=Biol. Chem. |volume=384 |issue=4 |pages=539–49 |date=April 2003 |pmid=12751784 |doi=10.1515/BC.2003.062 |url=http://www.reference-global.com/doi/abs/10.1515/BC.2003.062}} 2 : Thiols|Peptides |
| 随便看 |
|
开放百科全书收录14589846条英语、德语、日语等多语种百科知识，基本涵盖了大多数领域的百科知识，是一部内容自由、开放的电子版国际百科全书。