PubMed · 5880952
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K Kácl. 1965. [Current problems in enzymology].. https://pubmed.ncbi.nlm.nih.gov/5880952/
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MOTIVATION: Predicting enzyme function from its sequence is still an unsolved problem in the life sciences. Moreover, with the explosion of annotated genome data, we are inundated with potential enzymatic sequences that have not yet been biochemically characterized. While it is not possible to assign a not-yet-existing label to such a sequence, there is high value in placing the sequence as accurately as possible in known function space. Doing so can help provide more accurate falsifiable hypotheses for experimentalists wishing to characterize enzymes from specific functional families. RESULTS: Here we present a contrastive learning algorithm for predicting enzyme function from sequence. Our method, EnzPlacer, predicts the third, second, and first EC numbers for a protein whose fourth EC number is not in the training corpus. This novel prediction mechanism accurately places a protein sequence within a narrowed-down functional context, even if the precise function remains unknown. AVAILABILITY AND IMPLEMENTATION: EnzPlacer and data is available at https://github.com/drxiangma/EnzPlacer under a GPL3 license.
Monoliths are considered as a novel generation of stationary phases. They were applied for capillary electrochromatography and liquid chromatography exploiting every action principle such as ion-exchange, affinity recognition, reversed-phase, and hydrophobic interaction. The fast separation was explained by convective transport of the solutes through the bed. The contribution of this mode of transport is similarly explained as done for the beds packed with particles with gigapores. For monolithic beds, the concept of an ultrashort bed was frequently used. This mode of operation allows very short separation time. In many cases a gradient elution is necessary to achieve separation. Examples of applications for protein and polynucleotide separation performed on monoliths are given. Enzymatic conversion was described showing the examples of several immobilzed enzymes.
Enzyme engineering is undergoing the most profound and exciting transformation in its history (1). It promises unprecedented expansion in the scope and applications of modified or improved enzymes with desired physical and catalytic properties. Two complementary strategies are currently available: rational redesign (2-5) and directed evolution (6,7). Although both approaches have met with great success, each has limitations. In this article, the perspectives for these enzyme-engineering strategies are discussed briefly.