Yoshiki Ochiai 落合 佳樹
@y0shiki-2025.bsky.social
Ph.D. candidate at Okinawa Institute of Science and Technology. Research Interests: Protein Engineering/Synthetic biology/modification systems
Reposted by Yoshiki Ochiai 落合 佳樹
The take-home message? Distal residues actively shape enzyme catalysis. Optimizing them can remove bottlenecks in substrate binding & product release—boosting activity. Want to dive deeper? Read our full study here: www.biorxiv.org/content/10.1...
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Distal mutations enhance catalysis in designed enzymes by facilitating substrate binding and product release
The role of amino-acid residues distant from an enzyme's active site in facilitating the complete catalytic cycle—including substrate binding, chemical transformation, and product release—remains poor...
www.biorxiv.org
February 28, 2025 at 5:17 PM
The take-home message? Distal residues actively shape enzyme catalysis. Optimizing them can remove bottlenecks in substrate binding & product release—boosting activity. Want to dive deeper? Read our full study here: www.biorxiv.org/content/10.1...
(6/6)
(6/6)
March 22, 2025 at 9:34 AM