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Echinocandin B Sale

(Synonyms: 棘白菌素B) 目录号 : GC40059

An echinocandin antifungal

Echinocandin B Chemical Structure

Cas No.:54651-05-7

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产品描述

Echinocandin B is an echinocandin antifungal originally isolated from Aspergillus. Echinocandin B is an inhibitor of 1,3-β glucan synthase, and it inhibits incorporation of radiolabeled glucose into alkali-insoluble glucan by S. cerevisiae spheroplasts in a dose-dependent manner. It inhibits growth of C. albicans in vitro with an MIC value of 3.9 µg/ml after 2 days.

Chemical Properties

Cas No. 54651-05-7 SDF
别名 棘白菌素B
分子式 C52H81N7O16 分子量 1060.2
溶解度 DMF: Soluble,DMSO: Soluble,Ethanol: Soluble,Methanol: Soluble 储存条件 Store at -20°C
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1 mM 0.9432 mL 4.7161 mL 9.4322 mL
5 mM 0.1886 mL 0.9432 mL 1.8864 mL
10 mM 0.0943 mL 0.4716 mL 0.9432 mL
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Research Update

Mutagenesis of Echinocandin B overproducing Aspergillus nidulans capable of using starch as main carbon source

Prep Biochem Biotechnol 2020;50(8):745-752.PMID:32125248DOI:10.1080/10826068.2020.1734940.

Echinocandin B, a kind of antimycotic with cyclic lipo-hexapeptides, was produced by fermentation with Aspergillus nidulans using fructose as main carbon source. The objective of this study was to screen a high-yield mutant capable of using cheap starch as main carbon source by atmospheric and room temperature plasma (ARTP) treatment in order to decrease the production cost of Echinocandin B. A stable mutant A. nidulans ZJB19033, which can use starch as optimal carbon source instead of expensive fructose, was selected from two thousands isolates after several cycles of ARTP mutagenesis. To further increase the production of Echinocandin B, the optimization of fermentation medium was performed by response surface methodology (RSM), employing Plackett-Burman design (PBD) followed by Box-Behnken design (BBD). The optimized fermentation medium provided the optimal yield of Echinocandin B, 2425.9 ± 43.8 mg/L, 1.3-fold compared to unoptimized medium. The results indicated that the mutant could achieve high Echinocandin B production using cheap starch as main carbon source, and the cost of carbon sources in fermentation medium reduced dramatically by about 45%.

Cryptic Production of trans-3-Hydroxyproline in Echinocandin B Biosynthesis

Appl Environ Microbiol 2018 Mar 19;84(7):e02370-17.PMID:29352089DOI:10.1128/AEM.02370-17.

Echinocandins are antifungal nonribosomal hexapeptides produced by fungi. Two of the amino acids are hydroxy-l-prolines: trans-4-hydroxy-l-proline and, in most echinocandin structures, (trans-2,3)-3-hydroxy-(trans-2,4)-4-methyl-l-proline. In the case of echinocandin biosynthesis by Glarea lozoyensis, both amino acids are found in pneumocandin A0, while in pneumocandin B0 the latter residue is replaced by trans-3-hydroxy-l-proline (3-Hyp). We have recently reported that all three amino acids are generated by the 2-oxoglutarate-dependent proline hydroxylase GloF. In Echinocandin B biosynthesis by Aspergillus species, 3-Hyp derivatives have not been reported. Here we describe the heterologous production and kinetic characterization of HtyE, the 2-oxoglutarate-dependent proline hydroxylase from the Echinocandin B biosynthetic cluster in Aspergillus pachycristatus Surprisingly, l-proline hydroxylation with HtyE resulted in an even higher proportion (?30%) of 3-Hyp than that with GloF. This suggests that the selectivity for methylated 3-Hyp in Echinocandin B biosynthesis is due solely to a substrate-specific adenylation domain of the nonribosomal peptide synthetase. Moreover, we observed that one product of HtyE catalysis, 3-hydroxy-4-methyl-l-proline, is slowly further oxidized at the methyl group, giving 3-hydroxy-4-hydroxymethyl-l-proline, upon prolonged incubation with HtyE. This dihydroxylated amino acid has been reported as a building block of cryptocandin, an echinocandin produced by CryptosporiopsisIMPORTANCE Secondary metabolites from bacteria and fungi are often produced by sets of biosynthetic enzymes encoded in distinct gene clusters. Usually, each enzyme catalyzes one biosynthetic step, but multiple reactions are also possible. Pneumocandins A0 and B0 are produced by the fungus Glarea lozoyensis They belong to the echinocandin family, a group of nonribosomal cyclic lipopeptides that exhibit a strong antifungal activity. Chemical derivatives are important drugs for the treatment of systemic fungal infections. We have recently shown that in the biosynthesis of pneumocandins A0 and B0, three hydroxyproline building blocks are provided by one proline hydroxylase. Here we demonstrate that the proline hydroxylase from Echinocandin B biosynthesis in Aspergillus pachycristatus produces the same hydroxyprolines, with an increased proportion of trans-3-hydroxyproline. However, Echinocandin B biosynthesis does not require trans-3-hydroxyproline; its formation remains cryptic. While one can only speculate on the evolutionary background of this unexpected finding, proline hydroxylation in G. lozoyensis and A. pachycristatus provides an unusual insight into peptide antibiotic biosynthesis-namely, the complex interplay between the selectivity of a hydroxylase and the substrate specificity of a nonribosomal peptide synthetase.

Functional expression of an Echinocandin B deacylase from Actinoplanes utahensis in Escherichia coli

Int J Biol Macromol 2021 Sep 30;187:850-857.PMID:34339787DOI:10.1016/j.ijbiomac.2021.07.146.

Echinocandin B deacylase (ECBD) from Actinoplanes utahensis can be applied to produce Echinocandin B nucleus (ECBN), an essential intermediate of the echinocandins antifungal drugs such as anidulafungin. To date, the expression of ECBD has been limited to Streptomyces. To achieve the active expression of ECBD in Escherichia coli (E. coli), we constructed a plasmid carrying two subunits of ECBD for T7 RNA polymerase driven transcription of dicistron messenger after codon optimization. Subsequently, the introduction of peptide tags in the recombinant ECBD was adopted to reduce the formation of inclusion bodies and enhance the ECBD solubility. The peptide tags with the opposite electrostatic charge, hexa-lysine (6K) and GEGEG (GE), exhibited the best positive effect, which was verified by activity assay and structural simulation. After that, optimization of culture conditions and characterization of ECBD were conducted, the optimal pH and temperature were 7.0 and 60 °C. It is the first report concerning the functional expression of ECBD in the host E. coli. Our results reported here can provide a reference for the high-level expression of other deacylases with respect to a possible industrial application.

Deacylation of Echinocandin B by Streptomyces species: a novel method for the production of Echinocandin B nucleus

3 Biotech 2019 Nov;9(11):412.PMID:31696017DOI:10.1007/s13205-019-1946-7.

Anidulafungin, a new class of antifungal agent used for the treatment of chronic fungal infections, is derived from Echinocandin B nucleus, an intermediate metabolite of Echinocandin B produced by Aspergillus nidulans. The enzyme acylase plays a key role in the bioconversion of Echinocandin B to Echinocandin B nucleus. In the present study, a rapid screening method was used to select an actinomycete capable of producing Echinocandin B acylase. Out of 140 actinomycetes screened for the production of acylase by preliminary qualitative plate assay, 53 were selected. The selected isolates were subjected to quantitative assay under submerged fermentation for the bioconversion of Echinocandin B to Echinocandin B nucleus. Among 53 strains of actinomycetes, two strains (BICC-8848 and BICC-8547) exhibited higher degree of acylase activity. Various physico-chemical parameters were optimised for maximum bioconversion of ECB to ECB nucleus. It was found that the conditions viz. pH 7.0, temperature 26 °C and substrate concentration of about 4 g/L supported higher degree of bioconversion. It was also observed that, as the medium volume increased to 500 mL, the conversion rate was also increased by more than two-folds.

Echinocandin B biosynthesis: a biosynthetic cluster from Aspergillus nidulans NRRL 8112 and reassembly of the subclusters Ecd and Hty from Aspergillus pachycristatus NRRL 11440 reveals a single coherent gene cluster

BMC Genomics 2016 Aug 8;17:570.PMID:27502607DOI:10.1186/s12864-016-2885-x.

Background: Echinocandins are nonribosomal lipopeptides produced by ascommycete fungi. Due to their strong inhibitory effect on fungal cell wall biosynthesis and lack of human toxicity, they have been developed to an important class of antifungal drugs. Since 2012, the biosynthetic gene clusters of most of the main echinocandin variants have been characterized. Especially the comparison of the clusters allows a deeper insight for the biosynthesis of these complex structures. Results: In the genome of the Echinocandin B producer Aspergillus nidulans NRRL 8112 we have identified a gene cluster (Ani) that encodes echinocandin biosynthesis. Sequence analyses showed that Ani is clearly delimited from the genomic context and forms a monophyletic lineage with the other echinocandin gene clusters. Importantly, we found that the disjunct genomic location of the Echinocandin B gene cluster in A. pachycristatus NRRL 11440 on two separate subclusters, Ecd and Hty, at two loci was likely an artifact of genome misassembly in the absence of a reference sequence. We show that both sequences can be aligned resulting a single cluster with a gene arrangement collinear compared to other clusters of Aspergillus section Nidulantes. The reassembled gene cluster (Ecd/Hty) is identical to a putative gene cluster (AE) that was previously deposited at the NCBI as a sequence from A. delacroxii NRRL 3860. PCR amplification of a part of the gene cluster resulted a sequence that was very similar (97 % identity), but not identical to that of AE. Conclusions: The Echinocandin B biosynthetic cluster from A. nidulans NRRL 8112 (Ani) is particularly similar to that of A. pachycristatus NRRL 11440 (Ecd/Hty). Ecd/Hty was originally reported as two disjunct sub-clusters Ecd and Hty, but is in fact a continuous sequence with the same gene order as in Ani. According to sequences of PCR products amplified from genomic DNA, the Echinocandin B producer A. delacroxii NRRL 3860 is closely related to A. pachycristatus NRRL 11440. A PCR-product from the gene cluster was very similar, but clearly distinct from the sequence published for A. delacroxii NRRL 3860 at the NCBI (No. AB720074). As the NCBI entry is virtually identical with the re-assembled Ecd/Hty cluster, it is likely that it originates from A. pachycristatus NRRL 11440 rather than A. delacroxii NRRL 3860.