Cypemycin
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| Category | Antibiotics |
| Catalog number | BBF-01128 |
| CAS | 154277-21-1 |
| Molecular Weight | 2096.49 |
| Molecular Formula | C99H154N24O24S |
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Description
It is produced by the strain of Streptomyces sp. OH-4156. It can inhibit cancer cell activity, inhibits P388 leukemia cells with IC50 of 1.3 μg/mL, It can inhibit human tumor cells such as HeLa S3, HHCC-1, HCCS-M and Slex with IC50 of >25 μg/mL.
Specification
| IUPAC Name | N-[1-[[1-[[1-[[5-amino-1-[[2-[[3-hydroxy-1-[[(E)-1-[[3-methyl-1-[[(2Z)-9-(2-methylpropyl)-5,8,11-trioxo-6-propan-2-yl-1-thia-4,7,10-triazacyclotridec-2-en-12-yl]amino]-1-oxopentan-2-yl]amino]-1-oxobut-2-en-2-yl]amino]-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1,5-dioxopentan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]-2-[2-[[2-[[(E)-2-[[1-[(E)-2-[2-[[1-[(E)-2-[2-(dimethylamino)propanoylamino]but-2-enoyl]pyrrolidine-2-carbonyl]amino]propanoylamino]but-2-enoyl]pyrrolidine-2-carbonyl]amino]but-2-enoyl]amino]-3-methylbutanoyl]amino]propanoylamino]pentanediamide |
| Canonical SMILES | CCC(C)C(C(=O)NC(CCC(=O)N)C(=O)NCC(=O)NC(CO)C(=O)NC(=CC)C(=O)NC(C(C)CC)C(=O)NC1CSC=CNC(=O)C(NC(=O)C(NC1=O)CC(C)C)C(C)C)NC(=O)C(C(C)C)NC(=O)C(CC2=CC=CC=C2)NC(=O)C(CCC(=O)N)NC(=O)C(C)NC(=O)C(C(C)C)NC(=O)C(=CC)NC(=O)C3CCCN3C(=O)C(=CC)NC(=O)C(C)NC(=O)C4CCCN4C(=O)C(=CC)NC(=O)C(C)N(C)C |
| InChI | InChI=1S/C99H154N24O24S/c1-22-54(15)78(97(145)115-69-49-148-44-41-102-93(141)75(51(9)10)116-87(135)66(45-50(7)8)113-90(69)138)119-85(133)60(24-3)107-89(137)68(48-124)106-74(127)47-103-83(131)64(37-39-72(100)125)112-96(144)79(55(16)23-2)120-95(143)77(53(13)14)118-88(136)67(46-59-33-29-28-30-34-59)114-86(134)65(38-40-73(101)126)111-81(129)57(18)105-94(142)76(52(11)12)117-84(132)61(25-4)108-92(140)71-36-32-43-123(71)98(146)62(26-5)109-80(128)56(17)104-91(139)70-35-31-42-122(70)99(147)63(27-6)110-82(130)58(19)121(20)21/h24-30,33-34,41,44,50-58,64-71,75-79,124H,22-23,31-32,35-40,42-43,45-49H2,1-21H3,(H2,100,125)(H2,101,126)(H,102,141)(H,103,131)(H,104,139)(H,105,142)(H,106,127)(H,107,137)(H,108,140)(H,109,128)(H,110,130)(H,111,129)(H,112,144)(H,113,138)(H,114,134)(H,115,145)(H,116,135)(H,117,132)(H,118,136)(H,119,133)(H,120,143)/b44-41-,60-24+,61-25+,62-26+,63-27+ |
| InChI Key | TYVRUMCYJWCOOO-TVEJMLEISA-N |
Properties
| Appearance | White Powder |
| Antibiotic Activity Spectrum | Neoplastics (Tumor) |
| Melting Point | 188-193 °C |
| Solubility | Soluble in Methanol, Benzene, Chloroform, Ethanol |
Reference Reading
1. Hijacking a Linaridin Biosynthetic Intermediate for Lanthipeptide Production
Leixia Chu, Jinduo Cheng, Chengzeng Zhou, Tianlu Mo, Xinjian Ji, Taoting Zhu, Jie Chen, Suze Ma, Jiangtao Gao, Qi Zhang ACS Chem Biol. 2022 Nov 18;17(11):3198-3206. doi: 10.1021/acschembio.2c00657. Epub 2022 Oct 26.
Linaridins and lanthipeptides are two classes of natural products belonging to the ribosomally synthesized and posttranslationally modified peptide (RiPP) superfamily. Although these two RiPP classes share similar structural motifs such as dehydroamino acids and thioether-based cross-links, the biosynthesis of linaridins and lanthipeptides involved distinct sets of enzymes. Here, we report the identification of a novel lanthipeptide cypepeptin from a recombinant strain of Streptomyces lividans, which harbors most of the cypemycin (a prototypic linaridin) biosynthetic gene cluster but lacks the decarboxylase gene cypD. In contrast to the generally believed structure of cypemycin, multiple d-amino acids and Z-dehydrobutyrines were observed in both cypepeptin and cypemycin, and the stereochemistry of each amino acid was established by the extensive structural analysis in combination with genetic knockout and mutagenesis studies. Comparative analysis of cypemycin and cypepeptin showed that the aminovinyl-cysteine (AviCys) moiety of cypemycin plays an essential role in disrupting the cell integrity of M. luteus, which cannot be functionally substituted by the structurally similar lanthionine moiety.
2. Movements of the Substrate-Binding Clamp of Cypemycin Decarboxylase CypD
Lei Liu, Stephen Chan, Tianlu Mo, Wei Ding, Shaoning Yu, Qi Zhang, Shuguang Yuan J Chem Inf Model. 2019 Jun 24;59(6):2924-2929. doi: 10.1021/acs.jcim.9b00156. Epub 2019 Apr 29.
Linaridins are a small but growing class of natural products belonging to the ribosomally synthesized and post-translationally modified peptide (RiPP) superfamily. The class A linaridins, exemplified by cypemycin, possess an unusual S-[( Z)-2-aminovinyl]-d-cysteine (AviCys) residue. Formation of the AviCys in cypemycin requires an oxidative decarboxylation of the precursor peptide C-terminal Cys, and this reaction is catalyzed by a flavin-dependent decarboxylase CypD. In this work, we investigate the molecular recognition processes of CypD by a combination of computational and biochemical analysis. We show that the substrate binding clamp of CypD undergoes dramatic fluctuation, mediating both the substrate entrance into and product release from the catalytic pocket. Extensive molecular dynamic simulations and Fourier transform IR analyses indicated that binding of the substrate induces substantial structural change of the enzyme, converting the substrate-binding clamp from a random loop to a more ordered structure comprising two β sheets and a β turn. The salt bridge between Arg159 guanine and the Cys carboxylate of substrate plays an important role in mediating substrate binding, while hydrophobic interactions are also important in this process. These results provide important mechanistic insights into CypD and other flavin-dependent Cys decarboxylases, and could facilitate future biosynthetic and bioengineering efforts in studying AviCys-containing RiPPs.
3. Biosynthetic Gene Cluster of Linaridin Peptides Contains Epimerase Gene
Wanlu Xiao, Yasuharu Satoh, Yasushi Ogasawara, Tohru Dairi Chembiochem. 2022 Jun 20;23(12):e202100705. doi: 10.1002/cbic.202100705. Epub 2022 May 12.
Salinipeptins belong to the type-A linaridin class of ribosomally synthesized and post-translationally modified peptides (RiPPs) comprising 22 amino acid residues with multiple D-amino acids. Although chirality of other type-A linaridins, such as grisemycin and cypemycin, has not been reported, the biosynthetic gene clusters of type-A linaridins have identical gene organization. Here, we report heterologous expression of grisemycin biosynthetic gene cluster (grm) and show that grisemycin contains multiple D-amino acids, similar to salinipeptins. The heterologous expression experiments also confirm the involvement of a novel peptide epimerase in grisemycin biosynthesis. Gene-deletion experiments indicate that grmL, a single gene with unknown function, is indispensable for grisemycin production. We also show that the presence of D-amino acids is likely a common feature of linaridin natural products by analyzing two other type-A linaridin clusters.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
