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....is an α-amino acid, one of the twenty DNA-encoded amino acids. It is not an essential amino acid, which means that humans can not synthesize it... |
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The Best Current Available Price ! L-Proline is an amino acid involved in the production of collagen and cartilage and may help support healthy joints and a healthy musculoskeletal system. L-Proline can be made in the body, but low protein/vegetarian diets may not always promote optimal production.... |
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L-Proline is an amino acid involved in the production of collagen and cartilage and may help support healthy joints and a healthy musculoskeletal system. L-Proline can be made in the body, but low protein/vegetarian diets may not always promote optimal production.... |
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L-Lysine and L-Proline amino acids are the precursors of hydroxylysine and hydroxyproline, two constituents of collagen, an essential component of arterial linings.... |
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L-Lysine and L-Proline amino acids are the precursors of hydroxylysine and hydroxyproline, two constituents of collagen, an essential component of arterial linings. Vitamin C, a strong antioxidant, is also essential for collagen production. Hawthorn berry and grape seed extract are potent antioxidants due to their high levels of proanthocyanidin....
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L-Lysine and L-Proline amino acids are the precursors of hydroxylysine and hydroxyproline, two constituents of collagen, an essential component of arterial linings. Vitamin C, a strong antioxidant, is also essential for collagen production. Hawthorn berry and grape seed extract are potent antioxidants due to their high levels of proanthocyanidin.... |
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L-Proline is an amino acid involved in the production of collagen and cartilage and may help support healthy joints and a healthy musculoskeletal system. L-Proline can be made in the body, but low protein/vegetarian diets may not always promote optimal production....
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L-Proline
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Proline
Proline (abbreviated as Pro or P) is an α-amino acid, one of the twenty DNA-encoded amino acids.
Its codons are CCU, CCC, CCA, and CCG.
It is not an essential amino acid, which means that humans can not synthesize it.
It is unique among the 20 protein-forming amino acids because the α-amino group is secondary.
Cis-trans isomerization
Peptide bonds to proline, and to other N-substituted amino acids (such as sarcosine), are able to populate both the cis and trans isomers.
Most peptide bonds overwhelmingly adopt the trans isomer (typically 99.9% under unstrained conditions), chiefly because the amide hydrogen (trans isomer) offers less steric repulsion to the preceding Cα atom than does the following Cα atom (cis isomer).
By contrast, the cis and trans isomers of the X-Pro peptide bond (where X represents any amino acid) both experience steric clashes with the neighboring substitution and are nearly equal energetically.
Hence, the fraction of X-Pro peptide bonds in the cis isomer under unstrained conditions ranges from 10-40%; the fraction depends slightly on the preceding amino acid, with aromatic residues favoring the cis isomer slightly.
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From a kinetic standpoint, Cis-trans proline isomerization is a very slow process that can impede the progress of protein folding by trapping one or more proline residues crucial for folding in the non-native isomer, especially when the native protein requires the cis isomer.
This is because proline residues are exclusively synthesized in the ribosome as the trans isomer form.
All organisms possess prolyl isomerase enzymes to catalyze this isomerization, and some bacteria have specialized prolyl isomerases associated with the ribosome.
However, not all prolines are essential for folding, and protein folding may proceed at a normal rate despite having non-native conformers of many X-Pro peptide bonds.
Uses
Proline and its derivatives are often used as asymmetric catalysts in organic reactions.
The CBS reduction and proline catalysed aldol condensation are prominent examples.
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L-Proline is an osmoprotectant and therefore is used in many pharmaceutical, biotechnological applications.
Specialities
Proline is one of the two amino acids that do not follow along with the typical Ramachandran plot, along with glycine.
Due to the ring formation connected to the Beta-carbon, the ψ and φ angles about the peptide bond have less allowable degrees of rotation. *
| Proline | |
|---|---|
 |
 |
 |
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| IUPAC name | |
Systematic name
|
|
| Identifiers | |
| CAS number | 147-85-3 |
| PubChem | 614 |
| ChemSpider | 594 128566 (2S)-carboxylic acid |
| UNII | DCS9E77JPQ  |
| EC number | 210-189-3 |
| DrugBank | DB02853 |
| KEGG | C16435 |
| MeSH | Proline |
| ChEBI | CHEBI:26271 |
| ChEMBL | CHEMBL72275 |
| RTECS number | TW3584000 |
| Beilstein Reference | 80812 |
| Gmelin Reference | 26927 |
| Jmol-3D images | Image 1 Image 2 |
InChl
|
|
| Properties | |
| Molecular formula | C5H9NO2 |
| Molar mass | 115.13 g mol−1 |
| Exact mass | 115.063328537 g mol-1 |
| Appearance | Transparent crystals |
| Melting point | 205-228 °C, 478-501 K, 401-442 °F (decomposes) |
| log P | -0.06 |
| Acidity (pKa) | 2.351 |
| Hazards | |
| MSDS | External MSDS |
| S-phrases | S22, S24/25 |
| Supplementary data page | |
| Structure and properties |
n, εr, etc. |
| Thermodynamic data |
Phase behaviour Solid, liquid, gas |
| Spectral data | UV, IR, NMR, MS |
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox references |
|
**
Read The complete Article in Wikipedia, Mar 6, 2009
* Proline. (2009, March 5). In Wikipedia, The Free Encyclopedia.
Retrieved 07:25, March 6, 2009, from
http://en.wikipedia.org/w/index.php?title=
Proline&oldid=275110646
____________________
Read The complete Article in Wikipedia June 19 2011
** Proline. (2011, April 13). In Wikipedia, The Free Encyclopedia.
Retrieved 17:42, June 19, 2011, from
http://en.wikipedia.org/w/index.php?title=
____________________Hyperprolinemia
Hypeprolinemia, also referred to as prolinemia or prolinuria, is a condition which occurs when the amino acid proline is not broken down properly by the enzymes proline oxidase or pyrroline-5-carboxylate dehydrogense, causing a build up of proline in the body.
| Hyperprolinemia | |
|---|---|
Classification and external resources |
|
 Proline |
|
| ICD-10 | E72.5 |
| ICD-9 | 270.8 |
| OMIM | 239500 |
| DiseasesDB | 29674 |
**
Types
Hyperprolinemia type I
It is difficult to determine the prevalence of hyperprolinemia type I, as many people with the condition are asymptomatic.
People with hyperprolinemia type I have proline levels in their blood between 3 and 10 times the normal level.
Some individuals with type I exhibit seizures, mental retardation or other neurological problems.
Hyperprolinemia type II
Hyperprolinemia type II results in proline levels in the blood between 10 and 15 times higher than normal, and high levels of a related compound called pyrroline-5-carboxylate.
This rare form of the disorder may appear benign at times, but often involves seizures, convulsions, and mental retardation.
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Hyperprolinemia can also occur with other conditions, such as malnutrition or liver disease.
In particular, individuals with conditions that cause elevated levels of lactic acid in the blood, such as lactic acidemia, are likely to have elevated proline levels, because lactic acid inhibits the breakdown of proline.
Genetics
Mutations in the ALDH4A1 and PRODH genes cause hyperprolinemia.
Read The complete Article in Wikipedia, Mar 6, 2009
* Hyperprolinemia. (2008, December 22). In Wikipedia,The Free Encyclopedia.
Retrieved 07:31, March 6, 2009, from
http://en.wikipedia.org/w/index.php?title=
Hyperprolinemia&oldid=259436924
____________________
Read The complete Article in Wikipedia June 19 2011
** Hyperprolinemia. (2010, October 26). In Wikipedia, The Free Encyclopedia.
Retrieved 17:48, June 19, 2011, from
http://en.wikipedia.org/w/index.php?title=
Hyperprolinemia&oldid=392946361
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____________________Disclaimer :
In accordance with FDA regulation, we do not make any therapeutic claims for any Dietary Supplements in accordance with the Dietary Supplement Health and Education Act.
Information on this website is provided for informational purposes only and is not intended as a substitute for the advice provided by your physicians, health care professional or other professional. You should not use the information on this website for diagnosing or treating any health problem, symptom or disease, prescribing any medication or other treatment, or in place of any other professional advice. This information is not intended to diagnose, treat, cure or prevent any diseases. You should consult with a healthcare professional before starting any diet, exercise or supplementation program, before taking any medication, or if you have or suspect you might have a health problem. Your discretion is advised.
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