Feifei Qi

TL;DR: This work elucidate the full biosynthetic pathway of the fungal natural product mycophenolic acid (MPA) and reveals that the MPA biosynthesis enzymes are elegantly compartmentalized; the oxygenase MpaB′ is the long-sought enzyme responsible for initiating the oxidative cleavage of the farnesyl side chain; and the subcellular localization of the acyl-coenzyme A hydrolase MPAH′ in peroxisomes is required

TL;DR: Steady-state kinetic parameters for each catabolic step were determined, and these results suggest that kinetic controls serve a key role in directing the metabolic flux to the most energy effective route.

TL;DR: In this paper, a revised questin ring-opening mechanism was elucidated by in vivo gene disruption, in vitro enzymatic analysis, and 18O chasing experiments, and it has been confirmed that the reductase GedF is responsible for the reduction of the keto group at C-10 in questin to a hydroxyl group with the aid of NADPH.

TL;DR: A catalase‐deficient Escherichia coli host strain is devised and an HTS approach based on colorimetric detection of H2O2‐consumption activity of FADCs is reported, leading to effective identification for the first time of improved FADC variants for medium‐chain 1‐alkene production from both DNA shuffling and random mutagenesis libraries.