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Ebelactone A

(Synonyms: (-)-Ebelactone A, NSC 335650) 目录号 : GC40277

An esterase inhibitor

Ebelactone A Chemical Structure

Cas No.:76808-16-7

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500μg
¥839.00
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1mg
¥1,336.00
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产品描述

Ebelactone A is a β-lactone enzyme inhibitor that was first isolated from a cultured strain of soil actinomycetes. It can inhibit esterases, lipases, and N-formylmethionine aminopeptidases (IC50s = 0.056, 0.003, and 0.08 µg/ml, respectively) found on cell surfaces, which has been shown to stimulate host defense in immune cells. Ebelactone A is also reported to inhibit cutinases produced by fungal pathogens, thus demonstrating a plant-protective function.

Chemical Properties

Cas No. 76808-16-7 SDF
别名 (-)-Ebelactone A, NSC 335650
Canonical SMILES C/C(C[C@H](C)[C@]1([H])OC([C@H]1C)=O)=C\[C@@H](C)C([C@@H](C)[C@H](O)[C@H](C)CC)=O
分子式 C20H34O4 分子量 338.5
溶解度 DMF: 25 mg/ml,DMF:PBS(pH 7.2)(1:1): 0.5 mg/ml,DMSO: 25 mg/ml,Ethanol: 20 mg/ml 储存条件 Store at -20°C
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1 mM 2.9542 mL 14.771 mL 29.5421 mL
5 mM 0.5908 mL 2.9542 mL 5.9084 mL
10 mM 0.2954 mL 1.4771 mL 2.9542 mL
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Research Update

Biosynthesis of Ebelactone A: isotopic tracer, advanced precursor and genetic studies reveal a thioesterase-independent cyclization to give a polyketide β-lactone

J Antibiot (Tokyo) 2013 Jul;66(7):421-30.PMID:23801186DOI:10.1038/ja.2013.48.

Macrocyclization of polyketides generates arrays of molecular architectures that are directly linked to biological activities. The four-membered ring in oxetanones (β-lactones) is found in a variety of bioactive polyketides (for example, lipstatin, hymeglusin and ebelactone), yet details of its molecular assembly have not been extensively elucidated. Using ebelactone as a model system, and its producer Streptomyces aburaviensis ATCC 31860, labeling with sodium [1-(13)C,(18)O2]propionate afforded Ebelactone A that contains (18)O at all oxygen sites. The pattern of (13)C-(18)O bond retention defines the steps for ebelactone biosynthesis, and demonstrates that β-lactone ring formation occurs by attack of a β-hydroxy group onto the carbonyl moiety of an acyclic precursor. Reaction of Ebelactone A with N-acetylcysteamine (NAC) gives the β-hydroxyacyl thioester, which cyclizes quantitatively to give Ebelactone A in aqueous ethanol. The putative gene cluster encoding the polyketide synthase (PKS) for biosynthesis of 1 was also identified; notably the ebelactone PKS lacks a terminal thioesterase (TE) domain and no stand alone TE was found. Thus the formation of ebelactone is not TE dependent, supporting the hypothesis that cyclization occurs on the PKS surface in a process that is modeled by the chemical cyclization of the NAC thioester.

Biosynthetic studies of Ebelactone A and B by 13C NMR spectrometry

J Antibiot (Tokyo) 1982 Dec;35(12):1670-4.PMID:7166532DOI:10.7164/antibiotics.35.1670.

Biosynthetic pathways of Ebelactone A and B were studied by 13C NMR spectroscopy. By using 13C labeled compounds as precursors it was determined that Ebelactone A was derived from one molecule of acetic acid and six propionic acids and ebelactone B from one molecule of acetic acid, five propionic acids and one butyric acid.

Stereocontrol in organic synthesis using silicon-containing compounds. Studies directed towards the synthesis of Ebelactone A

Org Biomol Chem 2004 Apr 7;2(7):1051-64.PMID:15034629DOI:10.1039/b316899a.

Several approaches to the synthesis of Ebelactone A 2 are described, culminating in the synthesis of the benzenesulfonate of 2-epi-ebelactone A 161. All the approaches were based on three fragments A, B and C, originally defined in general terms in, but eventually used as the aldehyde 72, the allenylsilane 3 and the aldehyde 139, respectively. They were joined, first B with C, and then B+C with A. In the main routes to fragments A and C, the relative stereochemistry was controlled by highly stereoselective enolate methylations 67-->67, 68-->69, and 135-->136, in each case anti to an adjacent silyl group, and by a highly stereoselective hydroboration of an allylsilane 137-->138, also anti to the silyl group. The hydroxyl groups destined to be on C-3 and C-11 were unmasked by silyl-to-hydroxy conversions 69-->70 and 138-->139 with retention of configuration. The stereochemistry created in the coupling of fragment B to C was controlled by the stereospecifically anti S(E)2' reaction between the enantiomerically enriched allenylsilane 3 and the aldehyde 139. The double bond geometry was controlled by syn stereospecific silylcupration 148-->151, and preserved by iododesilylation 151-->152 of the vinylsilane with retention of configuration, and Nozaki-Hiyama-Kishi coupling with the aldehyde 72 gave the whole carbon skeleton 153 of Ebelactone A with the correct relative configuration, all of which had been controlled by organosilicon chemistry. In the steps to remove the superfluous allylic hydroxyl, an intermediate allyllithium species 156 abstracted the proton on C-2, and its reprotonation inverted the configuration at that atom. Other routes to the fragments A and C were also explored, both successful and unsuccessful, both silicon-based and conventional, and a number of unexpected side reactions were investigated.

β-Lactone natural products and derivatives inactivate homoserine transacetylase, a target for antimicrobial agents

J Antibiot (Tokyo) 2011 Jul;64(7):483-7.PMID:21522158DOI:10.1038/ja.2011.37.

Homoserine transacetylase (HTA) catalyzes the transfer of an acetyl group from acetyl-CoA to the hydroxyl group of homoserine. This is the first committed step in the biosynthesis of methionine (Met) from aspartic acid in many fungi, Gram-positive and some Gram-negative bacteria. The enzyme is absent in higher eukaryotes and is important for microorganism growth in Met-poor environments, such as blood serum, making HTA an attractive target for new antimicrobial agents. HTA catalyzes acetyl transfer via a double displacement mechanism facilitated by a classic Ser-His-Asp catalytic triad located at the bottom of a narrow actives site tunnel. We explored the inhibitory activity of several β-lactones to block the activity of HTA. In particular, the natural product Ebelactone A, a β-lactone with a hydrophobic tail was found to be a potent inactivator of HTA from Haemophilus influenzae. Synthetic analogs of Ebelactone A demonstrated improved inactivation characteristics. Covalent modification of HTA was confirmed by mass spectrometry, and peptide mapping identified Ser143 as the modified residue, consistent with the known structure and mechanism of the enzyme. These results demonstrate that β-lactone inhibitors are excellent biochemical probes of HTA and potential leads for new antimicrobial agents.

Purification and characterization of a rat liver enzyme that hydrolyzes valaciclovir, the L-valyl ester prodrug of acyclovir

J Biol Chem 1995 Jun 30;270(26):15827-31.PMID:7797586DOI:10.1074/jbc.270.26.15827.

Valaciclovir is an oral prodrug of the antiherpetic agent acyclovir. An enzyme that hydrolyzes valaciclovir to acyclovir, valaciclovir hydrolase (VACVase), was purified from rat liver and characterized. VACVase was a basic (pI 9.4) protein associated with mitochondria. It was monomeric and had a molecular mass of 29 kDa. Amino acid sequences of six VACVase peptides, including its NH2 terminus (13 amino acids) and accounting for approximately 20% of its complete sequence, were not found in the SwissProt protein data base. VACVase hydrolyzed other amino acid esters of acyclovir in addition to valaciclovir (kcat/Km = 58 mM-1 s-1), with a preference for the L-alanyl (kcat/Km = 226 mM-1 s-1) and L-methionyl (kcat/Km = 200 mM-1 s-1) esters. It did not hydrolyze other types of esters or numerous di- and tripeptides and aminoacyl-beta-naphthylamides. Hydrolysis of valaciclovir by VACVase was not inhibited by amastatin, antipain, aprotinin, bestatin, chymostatin, E-64, EDTA, Ebelactone A, ebelactone B, elastatinal, leupeptin, pepstatin, or phosphoramidon. It was neither inhibited nor activated by Ca2+, Co2+, Mg2+, Mn2+, or Zn2+. Therefore, this enzyme is not a typical esterase or peptidase and, to our knowledge, it has not been described previously. Its physiological function is not known; however, it may play a significant role in the biotransformation of valaciclovir to acyclovir.