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.
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
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:
Peptide hydroxylation is a post-translational modification where a hydroxyl group is added to amino acids like proline or lysine. It is catalyzed by dioxygenases and affects peptide stability and function.
Proline hydroxylation stabilizes the triple helix structure of proteins, such as collagen, and plays a role in protein integrity and biological functions.
Lysine hydroxylation adds a hydroxyl group to lysine, forming hydroxylysine, which is crucial in protein stability and collagen formation.
Hydroxylation is key for studying protein function, stability, and involvement in diseases, including metabolic and connective tissue disorders.
Hydroxylation sites can be predicted by analyzing the physicochemical properties of the peptide's amino acids using computational tools.
Mass spectrometry and electrophoresis are used to confirm the amount of hydroxylated peptides by identifying and quantifying modified products.
Yes, hydroxylation can be applied to peptides with various amino acids, including proline, lysine, and others, depending on the modification requirements.
Creative Peptides provides custom hydroxylation services, including site prediction, synthesis, and verification via mass spectrometry and electrophoresis, ensuring high-quality peptides.
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