1. A gene cluster encoding a nonribosomal peptide synthetase-like enzyme catalyzes γ-aromatic butenolides.
- Author
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Meng QZ, Wang XZ, Dai HQ, Assani I, Zhang MT, Zhao PP, Li LF, Yin X, Qi J, Pan Y, Zhang LX, and Xia XK
- Subjects
- Molecular Structure, Animals, Zebrafish, Peptide Synthases genetics, Multigene Family, 4-Butyrolactone analogs & derivatives, 4-Butyrolactone pharmacology, 4-Butyrolactone chemistry, Aspergillus enzymology, Aspergillus chemistry, Aspergillus genetics
- Abstract
Sea cucumber-derived fungi have attracted much attention due to their capacity to produce an incredible variety of secondary metabolites. Genome-wide information on Aspergillus micronesiensis H39 obtained using third-generation sequencing technology (PacBio-SMRT) showed that the strain contains nonribosomal peptide synthetase (NRPS)-like gene clusters, which aroused our interest in mining its secondary metabolites. 11 known compounds ( 1 - 11 ), including two γ -aromatic butenolides ( γ -AB) and five cytochalasans, were isolated from A. micronesiensis H39. The structures of the compounds were determined by NMR and ESIMS, and comparison with those reported in the literature. From the perspective of biogenetic origins, the γ -butyrolactone core of compounds 1 and 2 was assembled by NRPS-like enzyme. All of the obtained compounds showed no inhibitory activity against drug-resistant bacteria and fungi, as well as compounds 1 and 2 had no anti-angiogenic activity against zebrafish.
- Published
- 2024
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