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Demonstrates enhanced enzyme kinetics in engineered enzymes, indicating a new predictive modeling approach.
Predicting enzyme kinetic parameters is vital for enzyme engineering, yet modeling these relationships remains challenging due to catalytic complexity. While Large Language Model (LLM)-based methods perform well by encoding sequences, their accuracy is often limited by neglecting explicit substrate-binding interactions. Here, we present GraphKcat, a deep learning framework integrating 3D enzyme−substrate conformations for kinetic prediction. GraphKcat demonstrates strong predictive performance across multiple sequence-identity-based evaluation settings, outperforming existing models. Using GraphKcat, we identified an L-glutaminase and a raspberry zingerone synthase with significantly enhanced catalytic efficiencies. Model interpretation analyses and in silico mutation studies suggest that the model captures functionally relevant residue−substrate interactions and catalytic regions. Further molecular dynamics and electric field analyses indicate that these enhancements are associated with strengthened substrate binding and a more favorable electrostatic environment. Overall, our results suggest that GraphKcat captures biologically relevant structure−function relationships, providing a structure-informed framework for rational enzyme engineering and industrial biocatalysis.
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Luo et al. (2026) studied this question.
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