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Coagulation of blood is a multifaceted, carefully coordinated process that includes numerous molecular stages and countless biomolecules to facilitate them, notably vitamin K. Although the healthcare industry has taken advantage of this insight to create medications that regulate vitamin K levels—either amplifying or diminishing clotting, as needed—the precise workings of the essential membrane enzyme that employs vitamin K, vitamin K-dependent gamma carboxylase (VKGC), were not fully comprehended.

Now, a research article in Nature spearheaded by Weikai Li, the Roy and Diana Vagelos Professor of Biochemistry & Molecular Biophysics at WashU Medicine, unveils the molecular intricacies of VKGC’s functionality. In particular, the investigators detail how VKGC manages gamma carboxylation, a sophisticated and chemically intricate process vital for effective blood clotting. Malfunctions in this process can result in clotting abnormalities.

Initially identified in blood clot formation, gamma carboxylation is now acknowledged as a crucial mechanism in various important facets of human health, including inflammation, apoptosis, immune reaction, maintaining vascular stability, sperm development, and insulin release. Cone snails also utilize gamma carboxylation to generate a diverse range of toxic peptides that target the nerve receptors of their prey, presenting a valuable reservoir of highly specific and rapid-acting drug candidates. The insights from this research may pave the way for innovative therapeutic strategies centered around this mechanism.

Li’s team presented a collection of cryo-electron microscopy structures of human VKGC in multiple functional states and in conjunction with substrate proteins that facilitate hemostasis, accompanied by biochemical evaluations of the multistep catalytic reactions conducted by VKGC. These discoveries mark a significant advancement in our understanding of how enzymes execute intricate reactions with unmatched chemical requirements within a membrane-bound setting.

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