Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1

Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1

Abstract During collagen biosynthesis, lysine residues undergo extensive post-translational modifications through the alternate action of two distinct metal ion-dependent enzyme families (i.e., LH/PLODs and GLT25D/COLGALT), ultimately producing the highly conserved α-(1,2)-glucosyl-β-(1,O)-galactosy...

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Main Authors: Matteo De Marco, Sristi Raj Rai, Luigi Scietti, Daiana Mattoteia, Stefano Liberi, Elisabetta Moroni, Alberta Pinnola, Alice Vetrano, Claudio Iacobucci, Carlo Santambrogio, Giorgio Colombo, Federico Forneris
Format: Article
Language:English
Published: Nature Portfolio 2025-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-59017-5
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https://doi.org/10.1038/s41467-025-59017-5

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