Covering: up to 2017Cytochalasans are a class of natural products possessing a wide range of important biological activities, yet the full biosynthetic steps towards the formation of their characteristic chemical features remain unknown. This highlight provides an overview of the recent advances made in understanding the biosynthesis of this fascinating class of compounds, complementing and extending a previous comprehensive review of this topic (K. Scherlach, D. Boettger, N. Remme and C. Hertweck, Nat. Prod. Rep., 2010, 27, 869-886).

Isolation and sequencing of a PKS gene isolated from xenovulene-producing cultures of Acremonium strictum indicated the presence of NT-, KS-, AT-, PT-, C-MeT- and R-domains; heterologous expression in Aspergillus oryzae resulted in the production of 3-methylorcinaldehyde, demonstrating the role of the terminal reductase domain in product release.

Heterologous expression of key components of the Magnaporthe grisea ACE1 gene cluster produces a potential precursor of cryptic avirulence signalling compounds that induce resistance to M. grisea in rice.

The sorbicillinoids are a class of biologically active and structurally diverse fungal polyketides arising from sorbicillin. Through co‐expression of sorA, sorB, sorC, and sorD from Trichoderma reesei QM6a, the biosynthetic pathway to epoxysorbicillinol and dimeric sorbicillinoids, which resemble Diels–Alder‐like and Michael‐addition‐like products, was reconstituted in Aspergillus oryzae NSAR1. Expression and feeding experiments demonstrated the crucial requirement of the flavin‐dependent monooxygenase SorD for the formation of dimeric sorbicillinoids, hybrid sorbicillinoids, and epoxysorbicillinol in vivo. In contrast to prior reports, SorD catalyses neither the oxidation of 2′,3′‐dihydrosorbicillin to sorbicillin nor the oxidation of sorbicillinol to oxosorbicillinol. This is the first report that both the intermolecular Diels–Alder and Michael dimerization reactions, as well as the epoxidation of sorbicillinol are catalysed in vivo by SorD.