| 词条 | Antipain |
| 释义 |
| Verifiedfields = changed | Watchedfields = changed | verifiedrevid = 457811721 | ImageFile = antipain.svg | ImageSize = 250px | IUPACName = N2[(1S)-1-carboxy-2-phenylethyl]carbamoylN5-(diaminomethylidene)-L-ornithyl-N(2S)-5-[(diaminomethylidene)amino]-1-oxopentan-2-ylL-valinamide | OtherNames = |Section1={{Chembox Identifiers | CASNo = 37691-11-5 | CASNo_Ref = {{cascite|changed|??}} | PubChem = 37817 | ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} | ChemSpiderID = 34678 | UNII_Ref = {{fdacite|changed|FDA}} | UNII = 47V479BE6L | SMILES = O=C[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)N[C@H](C(=O)O)Cc1ccccc1)CCC/N=C(\)N)C(C)C)CCC/N=C(\)N | InChI = 1/C27H44N10O6/c1-16(2)21(23(40)34-18(15-38)10-6-12-32-25(28)29)37-22(39)19(11-7-13-33-26(30)31)35-27(43)36-20(24(41)42)14-17-8-4-3-5-9-17/h3-5,8-9,15-16,18-21H,6-7,10-14H2,1-2H3,(H,34,40)(H,37,39)(H,41,42)(H4,28,29,32)(H4,30,31,33)(H2,35,36,43)/t18-,19-,20-,21-/m0/s1 | InChIKey = SDNYTAYICBFYFH-TUFLPTIABE | StdInChI_Ref = {{stdinchicite|correct|chemspider}} | StdInChI = 1S/C27H44N10O6/c1-16(2)21(23(40)34-18(15-38)10-6-12-32-25(28)29)37-22(39)19(11-7-13-33-26(30)31)35-27(43)36-20(24(41)42)14-17-8-4-3-5-9-17/h3-5,8-9,15-16,18-21H,6-7,10-14H2,1-2H3,(H,34,40)(H,37,39)(H,41,42)(H4,28,29,32)(H4,30,31,33)(H2,35,36,43)/t18-,19-,20-,21-/m0/s1 | StdInChIKey_Ref = {{stdinchicite|correct|chemspider}} | StdInChIKey = SDNYTAYICBFYFH-TUFLPTIASA-N |Section2={{Chembox Properties | C=27 | H=44 | N=10 | O=6 | Appearance = | Density = | MeltingPt = | BoilingPt = | Solubility = |Section3={{Chembox Hazards | MainHazards = | FlashPt = | AutoignitionPt = }}Antipain is an oligopeptide isolated from actinomycetes and used in biochemical research as a protease inhibitor, reported in 1972 as the first natural peptide containing a ureylene group.[1] Specifically, it is an inhibitor of trypsin and papain.[2] It has been crystallised in complex with carboxypeptidase from wheat[3] and Leishmania major oligopeptidase B.[4] In both cases the backbone carbonyl of the terminal arginine of antipain forms a covalent bond to the active site serine in the protease. References1. ^{{cite journal| pmid = 5052959| year = 1972| last1 = Umezawa| first1 = S| last2 = Tatsuta| first2 = K| last3 = Fujimoto| first3 = K| last4 = Tsuchiya| first4 = T| last5 = Umezawa| first5 = H| title = Structure of antipain, a new Sakaguchi-positive product of streptomyces| volume = 25| issue = 4| pages = 267–70| journal = The Journal of Antibiotics| doi=10.7164/antibiotics.25.267}} {{biochem-stub}}2. ^{{cite journal | pmid = 4559651 | year = 1972 | last1 = Suda | first1 = H | last2 = Aoyagi | first2 = T | last3 = Hamada | first3 = M | last4 = Takeuchi | first4 = T | last5 = Umezawa | first5 = H | title = Antipain, a new protease inhibitor isolated from actinomycetes | volume = 25 | issue = 4 | pages = 263–6 | journal = The Journal of Antibiotics | doi=10.7164/antibiotics.25.263}} 3. ^PDB ENTRY {{PDBe|1bcr}} {{cite journal | pmid = 8636973 | year = 1996 | title = Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. | volume = 255| pages = 714–25 | journal = J. Mol. Biol. | issue=5 | last1 = Bullock | first1 = TL | last2 = Breddam | first2 = K | last3 = Remington | first3 = SJ | doi=10.1006/jmbi.1996.0058}} 4. ^PDB ENTRY {{PDBe|2xe4}} {{cite journal | pmid = 20926390 | year = 2010 | title = Crystal Structure of Leishmania Major Oligopeptidase B Gives Insight Into the Enzymatic Properties of a Trypanosomatid Virulence Factor. | volume = 285 | pages = 39249–59 | journal = J. Biol. Chem. | doi=10.1074/jbc.M110.156679 | issue=50 | pmc=2998157 | last1 = McLuskey | first1 = K | last2 = Paterson | first2 = NG | last3 = Bland | first3 = ND | last4 = Isaacs | first4 = NW | last5 = Mottram | first5 = JC}} 2 : Peptides|Aldehydes |
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