TTh he e p pl la an nt t c ce el ll l w wa al ll l d de ec co om mp po os si in ng g m ma ac ch hi in ne er ry y u un nd de er rl li ie es s t th he e f fu un nc ct ti io on na al l d di iv ve er rs si it ty y o of f f fo or re es st t f fu un ng gi i T Th he e p pl la an nt t c ce el ll l w wa al ll l d de ec co om mp po os si in ng g m ma ac ch hi in ne er ry y u un nd de er rl li ie es s t th he e f fu un nc ct ti io on na al l d di iv ve er rs si it ty y o of f f fo or re es st t f fu un ng gi i

IMPORTANCEIt remains unknown whether SARS-CoV-2 infection specifically increases the risk of serious obstetric morbidity.OBJECTIVE To evaluate the association of SARS-CoV-2 infection with serious maternal morbidity or mortality from common obstetric complications.

Bis-indolylquinones represent a class of fungal natural products that display antiretroviral, antidiabetes, or cytotoxic bioactivities. Recent advances in Aspergillus genomic mining efforts have led to the discovery of the tdiA-E-gene cluster, which is the first genetic locus dedicated to bis-indolylquinone biosynthesis. We have now genetically and biochemically characterized the enzymes TdiA (bis-indolylquinone synthetase) and TdiD (L-tryptophan:phenylpyruvate aminotransferase), which, together, confer biosynthetic abilities for didemethylasterriquinone D to Aspergillus nidulans. This compound is the universal intermediate for all bis-indolylquinones. In this biochemical study of a bis-indolylquinone synthetase and a fungal natural product transaminase, we present a one-pot chemoenzymatic protocol to generate didemethylasterriquinone D in vitro. As TdiA resembles a nonribosomal peptide synthetase, yet catalyzes carbon-carbon-bond formation, we discuss the implications for peptide synthetase chemistry.

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