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Biology subjects

Speight, R. E.

Publications and source records attributed to Speight, R. E..

3 recordsLinked to original sources

Ultrahigh throughput screening to train generative protein models for engineering specificity into unspecific peroxygenases

Enzyme engineering plays a vital role in tailoring biocatalyst performance to meet the needs of target applications. However, the number of sequence trajectories possible from a single wildtype enzyme sequence is too vast to traverse experimentally. Here we present a novel approach that first expands the experimentally accessible sequence space using ultrahigh throughput screening (uHTS), and then uses indirect and low fidelity assay data to create a "fingerprint" for a target enzyme class. Experimental data from microfluidic uHTS are extracted and used to engineer specificity into an unspecific peroxygenase (UPO) from Aspergillus brasiliensis (AbrUPO). We created a library with more than 5 million different variants expressed in Komagataella phaffii (Pichia pastoris). Microfluidic droplet sorting was then used to generate a dataset of >30,000 unique sequences paired with function data. This dataset was then used to train a task-specific generative model using the Variational Search Distributions (VSD) framework. We compared the variants selected by rank aggregation from the screening data (R series) with novel sequences generated by the refined generative model (G series). While the wildtype enzyme produces nearly equal amounts of both the desired styrene oxide and undesired phenylacetaldehyde products, three out of five of the highest scoring G series variants produced product mixtures more enriched in the desired compound. In comparison, only one of the five highest scoring R series variants showed this improvement. Overall, the variant most enriched in desired product, G929, produced 2.4x more styrene oxide than phenylacetaldehyde, while G3 and G167, produced the highest quantities of desired product at 2.3x enrichment over the undesired product. Further analysis confirmed that our task-specific generative model outperforms existing models pre-trained on large publicly available datasets. This unique combination of uHTS and generative protein modelling provides an intelligent exploration mechanism which not only enables efficient enzyme discovery, but also accelerates optimization and enables predictive insights that are difficult to achieve with either approach alone.

bioengineering↗

Reconstitution of human cytochrome P450 activity using a Leishmania cell-free protein expression system

Cytochrome P450 enzymes (P450s) are ubiquitous in drug metabolism and natural product biosynthesis. Studying eukaryotic P450s has been limited by their dependence on membrane association and requirement for partner reductases. Here, we demonstrate cell-free synthesis and assay of human P450s 3A4 and 2D6 using Leishmania tarentolae translational extract. These P450s were co-expressed with various NADPH-cytochrome P450 reductases (CPRs), and activity was assayed directly using unpurified reactions. P450s 3A4 and 2D6 showed distinct preferences in reductase coupling: P450 3A4 activity was greatest when coupled to the human CPR, whereas P450 2D6 performed better when co-expressed with CPRs from Arabidopsis thaliana. Inhibition assays with chloramphenicol, terbinafine, and erythromycin yielded results consistent with known P450-drug interactions. We conclude that Leishmania-based cell-free protein synthesis resolves previous challenges in eukaryotic P450 expression, allowing for rapid and convenient functional studies of unmodified eukaryotic P450 systems, offering a practical tool for drug metabolism studies and biocatalyst discovery.

synthetic biology↗

Cellulase secretion by engineered Pseudomonas putida enables growth on cellulose oligomers.

Pseudomonas putida is an attractive synthetic biology platform organism for chemical synthesis from low-grade feedstocks due to its high tolerance to chemical solvents and lignin-derived small molecules that are often inhibitory to other biotechnologically relevant microorganisms. However, there are few molecular tools available for engineering P. putida and other gram-negative bacteria to secrete non-native enzymes for extracellular feedstock depolymerisation. In this study P. putida was transformed to secrete cellulase enzymes and evaluated for growth on polymeric or oligomeric cellulose substrates. Active exo- and endocellulase enzymes were secreted into the culture supernatant, and a preferred set of twin-arginine translocase secretion signal peptides were identified. Extracellular cellulase activity was sufficient to support growth of P. putida using cellotriose or cellotetraose as the sole source of carbon and energy. This work supports progress towards consolidated bioprocessing of cellulosic materials using P. putida, and advances the state of engineered protein secretion in gram negative bacteria. Key PointsO_LIEngineered Pseudomonas putida secreted cellulase enzymes into the culture medium C_LIO_LICellulase activity was sufficient to support growth on cellulose oligomers C_LI

synthetic biology↗