Hydroxyproline
You don't need to be Editor-In-Chief to add or edit content to WikiDoc. You can begin to add to or edit text on this WikiDoc page by clicking on the edit button at the top of this page. Next enter or edit the information that you would like to appear here. Once you are done editing, scroll down and click the Save page button at the bottom of the page.
| Hydroxyproline | |
|---|---|
| Image:Hydroxyproline structure.svg | |
| IUPAC name | 4-hydroxypyrrolidine- 2-carboxylic acid |
| Identifiers | |
| CAS number | |
| PubChem | |
| MeSH | |
| SMILES | OC1CNC(C1)C(O)=O |
| Properties | |
| Molecular formula | C5H9NO3 |
| Molar mass | 131.13 |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox disclaimer and references | |
4-Hydroxyproline, or hydroxyproline (C5H9O3N), is an uncommon amino acid, abbreviated as HYP, e.g., in Protein Data Bank.
Structure
Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the C (gamma) atom.
Other hydroxyprolines also exist in nature, notably 2,3-cis-3,4-trans-3,4-dihydroxyproline which occurs in diatom cell walls[1], and is postulated to have a role in silica deposition. Hydroxyproline is also found in the walls of oomycetes, fungus-like protists related to diatoms.[1]
Production and function
Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification).
Hydroxyproline is a major component of the protein collagen. Hydroxyproline and proline play key roles for collagen stability.[1] They permit the sharp twisting of the collagen helix.[1] It helps provide stability to the triple-helical structure of collagen by forming hydrogen bonds. Hydroxyproline is found in few proteins other than collagen. The only other mammalian protein which includes hydroxyproline is elastin.[1] For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount.
Clinical significance
Proline hydroxylation requires ascorbic acid. The most obvious, first effects (gum and hair problems) of absence of ascorbic acid in humans come from the resulting defect in hydroxylation of proline residues of collagen, with reduced stability of the collagen molecule causing scurvy.
See also
References
Additional images
fr:Hydroxyproline ja:ヒドロキシプロリン
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
