Themed collection Biocatalysis

The classes of compounds accessible via biocatalysis are as diverse as the concepts to make them, as presented at the Faraday Discussion on biocatalysis.

It is challenging to identify enzyme mutations that enhance specific conformational changes.We develop the shortest path map method to address this challenge.

This study provides the first evidence of hydrolysis of PET microplastics in human serum by esterases, to combat the microplastic contamination in humans.

We combine the selection and engineering of a carbonyl reductase enzyme with process development, to enable efficient and economically viable bioreduction of ethyl secodione to (13R,17S)-secol, the key chirality introducing intermediate en route to contraceptives etonogestrel and levonorgestrel.

A 1 pot, 2 step deprotection biocatalytic cascade.

This work exemplifies the use of machine-learned 3D structure predictors combined with molecular docking to generate poses for atomistic study via molecular dynamics, ultimately enabling rapid insight into a novel biosynthetic cascade.

By changing an active site tyrosine in FNR (the enzyme central to the e-Leaf) its exclusivity for NADP(H) swaps to NAD(H). Here, an electrochemical study of this variant reveals that the reduction potential of its active site flavin has been retuned.

A highly efficient aminoacyl tRNA synthetase (G1PylRS^MIFAF) has been developed to produce MeHis-containing proteins. High protein titres can be achieved with low ncAA concentrations (0.1 mM) enabling more economical production of MeHis-containing enzymes.

The study identified promising protein scaffolds for artificial enzyme development in iminium-ion catalysis, demonstrating activity and enantioselectivity in abiological Michael addition reactions.

We have developed novel tools to characterize evolutionarily conserved non-covalent interactions in proteins. We showcase their application to understanding substrate specificity in class A β-lactamases, with potential impact for protein engineering.

H/D exchange between substrate and solvent D₂O provides a sensitive test for substrate activation in prenylated-flavin dependent enzymes. We show that a remarkably diverse range of molecules can be activated by one enzyme, ferulic acid decarboxylase.

In silico prediction of distal hotspots was used to introduce distal mutations in an artificial enzyme that improved its reactivity and thermostability by shifting its conformational distribution.

Boosting the biosynthesis of essential cofactors by addition of xylose reductase and lactose to enhance product synthesis using synthetic biology.

We investigate the possible molecular mechanism of polyurethane esterase A, previously identified as responsible for degradation of a polyester polyurethane sample in Pseudomonas chlororaphis.

Engineering redox-sensitive residues dramatically increases the peroxidase activity of P450BM3 monooxygenase, providing new insights and a strategy for regulating P450s' promiscuous functionality.

A game-changer [FeFe]hydrogenase was studied to dissect the mechanism of oxygen resistance and learn how to protect biocatalysts for hydrogen-driven reactions.

We have engineered a novel RNA polymerase, T7-68, that improves co-transcriptional incorporation of selected cap analogs and reduces dsRNA content, addressing manufacturing challenges and facilitating large-scale mRNA production.

We aim to compartmentalize a representative peptide asparaginyl ligase, OaAEP1-C247A, within protein containers to create artificial organelles with substrate sorting capability.

A biocatalytic approach for polydimethylsiloxane synthesis is demonstrated using silicatein-α, an enzyme from marine sponges that catalyses the hydrolysis and condensation of Si–O bonds.

Epoxide hydrolase StEH1 was subjected to targeted randomized mutagenesis at five active-site amino acid residues and the resulting protein library was challenged for reactivity towards a bait chloride substrate.

We investigate the influence of the switchable thermal stability of a fusion partner on the activity of PETases demonstrating a range of optimal reaction temperatures.