Still obsessed with histidine (and its mimics)! Our latest work from Benjamin 🎉 uses genetic code expansion—tuning the primary coordination sphere of a dizinc metallohydrolase—lowering the catalytic pKa and boosting activity up to 5x at acidic pH. Check it out! doi.org/10.1021/acs.biochem.5c00768

Catalytic pKa Attenuation in a Hydrolytic Metalloenzyme by Genetic Code Expansion

Hydrolytic metalloenzymes employ Lewis-acidic metal cofactors to activate water molecules, generating nucleophilic hydroxide species that facilitate catalysis. Their catalytic efficiency across a wide...

doi.org

They say the sincerest form of flattery is mimicry, and we really love histidine! ❤️ Check out our most recent work on histidine mimics: Genetic incorporation of diverse non-canonical amino acids for histidine substitution. www.biorxiv.org/content/10.1...

🚨 PhD Opportunity! Passionate about enzyme engineering or genetic code expansion? 🧬 Our lab is hiring a PhD student! 🔬 Exciting interdisciplinary research 🤝 Engaging environment 🌱 📄 Does this sound like you, apply now! ⏳🔗 📢 Know someone? Share this! 🔄 jobs.uzh.ch/job-vacancie...

Exciting news from the lab! Our first preprint, “Hydrophobic Tuning with Non-Canonical Amino Acids in a Copper Metalloenzyme” is now available. In this study, we rewrite the rules of enzyme engineering with a cyclic, hydrophobic twist that’s anything but ordinary. 🔍: www.biorxiv.org/content/10.1...

Hydrophobic tuning with non-canonical amino acids in a copper metalloenzyme

Hydrophobicity controls many aspects of protein and enzyme function. Although hydrophobic tuning can be achieved to a limited extent with canonical amino acids, the incorporation of non- canonical ami...

biorxiv.org