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Peptide Hydroxylation

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Background

Peptide hydroxylation is a post-translational modification catalyzed by 2-oxoglutarate-dependent dioxygenases. The hydroxylation modification can take place on various amino acids, including but not limited to proline, lysine, asparagine, aspartate and histidine. Hydroxylation of proline or lysine residues in peptides are common post-translational modification event, and such modifications are found in many physiological and pathological processes.
Hydroxylation of proline or lysine residues are found in many physiological and pathological processes, and the pattern of these modifications influences many biological functions. Hydroxyproline and hydroxylysine have been found to be implicated in metabolic disorder, connective tissue disorders, lung cancer and stomach cancer. And annotation of hydroxylation in proteomes is a first-critical step toward decoding protein function and understanding their physiological roles that have been implicated in the pathological processes and providing useful information for drug development.

Modification Strategies

The proline hydroxylation catalyzed by prolyl-4-hydroxylases and prolyl-3-hydroxylase results in a hydroxyproline and is critical for the stabilization of the triple helix conformation.

The hydroxylation of the lysine residue is catalyzed by lysyl hydroxylase, forming hydroxylysine. Some of the hydroxylysine residues are further modified by the sequential steps of O-linked glycosylation producing galactosylhydroxylysine and glucosylgalactosyl-hydroxylysine

Available services:

Creative Peptides is specialized in the peptide modification services, providing a confidential and efficient service at competitive prices. Every step of peptide synthesis is subject to Creative Peptides' stringent quality control. Typical delivery specifications include:

Reference

  1. Shi, S. P., Chen, X., Xu, H. D., & Qiu, J. D. (2015). PredHydroxy: computational prediction of protein hydroxylation site locations based on the primary structure. Molecular BioSystems, 11(3), 819-825.
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