Shina Caroline Lynn Kamerlin

Ancestral sequence reconstruction of a bacterial decarboxylase gave enzymes with up to 294-fold longer half-life at 45 °C, higher activity, and 99.7% ee on a vinyl malonate substrate.

The paper investigates how natural evolution creates enantioselectivity in plant borneol dehydrogenases through ancestral sequence reconstruction and simulations.

This study investigates the emergence of two key cofactor-binding protein folds by analyzing their metabolic roles, structural organization, and folding mechanisms.

The paper uses FAMPNN to redesign SrBDH1 for increased thermostability while maintaining stereoselectivity.

This study investigates how disease-causing mutations in SHP-1 and SHP-2 affect WPD-loop dynamics and catalysis, revealing their role in altering enzyme function and providing insights for targeted therapy.

This paper describes an engineered archaeal PTP with enhanced thermostability and unique biochemical properties, revealing insights into enzyme evolution and biotechnological potential.

The paper identifies a triple-deletion mutant of SRC kinase that alters activation loop dynamics, leading to changes in substrate preference and signaling outcomes.

This paper presents a computational design of high-efficiency Kemp eliminases with unprecedented catalytic efficiency and stability through de novo enzyme design.

This paper challenges the evolutionary model that the Walker A motif was a seed for early P-loop NTPases by showing that disembodied Walker A peptides do not form stable phosphate-binding nests.

This study investigates the catalytic mechanisms and substrate specificity of the lactonase GcL, revealing its promiscuity in reaction mechanisms and broad substrate acceptance.

This study investigates how conformational changes in a mobile loop of the HisF enzyme regulate catalytic steps in histidine biosynthesis.

This study identifies the N-terminal helix of MarA as critical for DNA binding, showing its role in recognizing marboxes and suggesting it as a target for antibiotic resistance inhibitors.

This study identifies five mutations that enable the evolution of a xenobiotic-degrading enzyme and shows that higher-order epistasis shapes its adaptive landscape and substrate specificity.