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...
(6/6)
(6/6)
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)
Reposted by Yoshiki Ochiai 落合 佳樹
Our latest work has been published! Our additional implementation for Boltz-1 largely improves the stereochemical accuracy of predicted ligand molecule without retraining the model.
We also developed a notebook on Google Colaboratory, colab.research.google.com/github/cddla... .
We also developed a notebook on Google Colaboratory, colab.research.google.com/github/cddla... .
March 29, 2025 at 11:26 AM
Our latest work has been published! Our additional implementation for Boltz-1 largely improves the stereochemical accuracy of predicted ligand molecule without retraining the model.
We also developed a notebook on Google Colaboratory, colab.research.google.com/github/cddla... .
We also developed a notebook on Google Colaboratory, colab.research.google.com/github/cddla... .
Reposted by Yoshiki Ochiai 落合 佳樹
I could not be more excited to have our lab's first story online where we report our discovery that HDACs ~reverse~ their activity to ADD acyl groups to lysine! We found this for our favorite ketone body, BHB, but this pathway controls other lysine modifications too!🧵
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Reversible histone deacetylase activity catalyzes lysine acylation - Nature Chemical Biology
Tsusaka et al. discover that histone deacetylases, which are well known to remove protein modifications, such as lysine acetylation and β-hydroxybutyrylation, can also reverse their chemical activity ...
www.nature.com
March 26, 2025 at 2:02 PM
I could not be more excited to have our lab's first story online where we report our discovery that HDACs ~reverse~ their activity to ADD acyl groups to lysine! We found this for our favorite ketone body, BHB, but this pathway controls other lysine modifications too!🧵
www.nature.com/articles/s41...
www.nature.com/articles/s41...
I am honored to be selected as a participant of the 74th Lindau Nobel Laureate Meeting #LINO2025 🙌 and look forward to meeting talented chemists.
第74回リンダウ・ノーベル賞受賞者会議の参加者に選出されました！世界各国から集った化学者と交流できるのが楽しみです
第74回リンダウ・ノーベル賞受賞者会議の参加者に選出されました！世界各国から集った化学者と交流できるのが楽しみです
March 19, 2025 at 5:12 AM
I am honored to be selected as a participant of the 74th Lindau Nobel Laureate Meeting #LINO2025 🙌 and look forward to meeting talented chemists.
第74回リンダウ・ノーベル賞受賞者会議の参加者に選出されました！世界各国から集った化学者と交流できるのが楽しみです
第74回リンダウ・ノーベル賞受賞者会議の参加者に選出されました！世界各国から集った化学者と交流できるのが楽しみです
I am attending the Biophysical Society 2025 #BPS2025 in LA and will be presenting my part of the PhD project at the platform session!
Enzyme Function, Cofactors, and Post-Translational Modifications
Tuesday 4 pm, Room 502B, 1762-Plat
Paper: doi.org/10.1093/nar/...
Enzyme Function, Cofactors, and Post-Translational Modifications
Tuesday 4 pm, Room 502B, 1762-Plat
Paper: doi.org/10.1093/nar/...
SUPREM: an engineered non-site-specific m6A RNA methyltransferase with highly improved efficiency
Abstract. N6-Methyladenine (m6A) RNA methylation plays a key role in RNA processing and translational regulation, influencing both normal physiological and
doi.org
February 17, 2025 at 8:49 PM
I am attending the Biophysical Society 2025 #BPS2025 in LA and will be presenting my part of the PhD project at the platform session!
Enzyme Function, Cofactors, and Post-Translational Modifications
Tuesday 4 pm, Room 502B, 1762-Plat
Paper: doi.org/10.1093/nar/...
Enzyme Function, Cofactors, and Post-Translational Modifications
Tuesday 4 pm, Room 502B, 1762-Plat
Paper: doi.org/10.1093/nar/...