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{{chembox
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| ImageFileL1 = L-proline-skeletal.png
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| ImageSizeL1 = 120px
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| ImageFileR1 = L-proline-zwitterion-from-xtal-3D-balls-A.png
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| ImageSizeR1 = 120px
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| IUPACName = (''S'')-Pyrrolidine-2-carboxylic acid
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| OtherNames =
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| Section1 = {{Chembox Identifiers
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| CASNo = 147-85-3
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| PubChem = 614
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| SMILES = OC(=O)[C@@H]1CCCN1
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}}
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| Section2 = {{Chembox Properties
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| C=5 | H=9 | N=1 | O=2
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| Appearance =
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| Density =
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| MeltingPt =
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| BoilingPt =
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| Solubility = }}
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| Section3 = {{Chembox Hazards
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| MainHazards =
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| FlashPt =
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| Autoignition = }}
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}}
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'''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 synthesize it. It is unique among the 20 protein-forming amino acids because the α-amino group is [[secondary amine|secondary]].
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== Biosynthesis ==
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Proline is [[Biosynthesis|biosynthetically]] derived from the amino acid <small>L</small>-[[glutamate]] and its immediate precursor is the [[imino acid]] [[1-Pyrroline-5-carboxylic acid|(''S'')-1-pyrroline-5-carboxylate]] (P5C). Enzymes involved in a typical biosynthesis include:<ref>Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. ISNB 1-57259-153-6.</ref>
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# [[Glutamate kinase]] (ATP-dependent)
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# [[Glutamate dehydrogenase]] (requires NADH or NADPH)
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# [[Pyrroline-5-carboxylate reductase]] (requires NADH or NADPH)
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==Structural properties==
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The distinctive cyclic structure of proline's side chain locks its <math>\phi</math> backbone [[dihedral angle]] at approximately -75°, giving proline an exceptional conformational rigidity compared to other amino acids. Hence, proline loses less conformational [[Introduction to entropy|entropy]] upon folding, which may account for its higher prevalence in the proteins of thermophilic organisms. Proline acts as a structural disruptor in the middle of regular [[secondary structure]] elements such as [[alpha helix|alpha helices]] and [[beta sheet]]s; however, proline is commonly found as the first residue of an [[alpha helix]] and also in the edge strands of [[beta sheet]]s. Proline is also commonly found in [[turn (biochemistry)|turns]], which may account for the curious fact that proline is usually solvent-exposed, despite having a completely [[aliphatic]] side chain. Because proline lacks a hydrogen on the amide group, it cannot act as a [[hydrogen bond]] donor, only as a [[hydrogen bond]] acceptor.
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Multiple prolines and/or [[hydroxyproline]]s in a row can create a [[polyproline helix]], the predominant [[secondary structure]] in [[collagen]]. The hydroxylation of proline by [[prolyl hydroxylase]] (or other additions of electron-withdrawing substituents such as [[fluorine]]) increases the conformational stability of [[collagen]] significantly. Hence, the hydroxylation of proline is a critical biochemical process for maintaining the [[connective tissue]] of higher organisms. Severe diseases such as [[scurvy]] can result from defects in this hydroxylation, e.g., mutations in the enzyme [[hydroxylation|prolyl hydroxylase]] or lack of the necessary [[vitamin C|ascorbate (vitamin C)]] cofactor.
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Sequences of proline and [[2-Aminoisobutyric acid|2-aminoisobutyric acid]] (Aib) also form a helical turn structure{{Fact|date=February 2007}}.
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In 2006, scientists at [[Arizona State University|ASU]] discovered that solutions of [[Titanium dioxide|TiO<sub>2</sub>]] illuminated with [[ultraviolet]] radiation can serve as an extremely cost-effective and accurate protein cleavage catalyst. The TiO<sub>2</sub> catalyst preferentially and rapidly cleaves protein at sites where proline is present, while taking much longer to degrade the protein from its endpoints.<ref>{{cite journal | author = B. J. Jones, M. J. Vergne, D. M. Bunk, L. E. Locascio and M. A. Hayes | title = Cleavage of Peptides and Proteins Using Light-Generated Radicals from Titanium Dioxide | year = 2007 | journal = [[Anal. Chem.]] | volume = 79 | issue = 4 | pages = 1327–1332 | doi = 10.1021/ac0613737}}</ref>
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==Cis-trans isomerization==
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[[Peptide bond]]s 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 <math>\mathrm{C}^{\alpha}</math> atom than does the following <math>\mathrm{C}^{\alpha}</math> 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 [[isomer]]ization 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]] [[enzyme]]s 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.
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==Uses==
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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.
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==Specialities==
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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.
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==History==
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[[Hermann Emil Fischer]] discovered Proline between 1899 and 1908.
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==See also==
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* [[Collagen]]
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* [[Polyproline helix]]
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* [[Peptide bond]] (for more discussion of cis-trans isomerization)
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*[[Hyperprolinemia]]
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== External links ==
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* [http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/Pro.html Proline biosynthesis]
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* [http://www.compchemwiki.org/index.php?title=Proline Computational Chemistry Wiki]
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* [http://www.biocarta.com/pathfiles/prolinePathway.asp Proline biosynthesis]
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==Notes==
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{{reflist}}
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== References ==
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* Balbach J, Schmid FX. (2000). Proline isomerization and its catalysis in protein folding. In ''Mechanisms of Protein Folding'' 2nd ed. Editor RH Pain. Oxford University Press.
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* For a thorough scientific overview of disorders of proline and hydroxyproline metabolism, one can consult chapter 81 of OMMBID [[Charles Scriver]], Beaudet, A.L., Valle, D., Sly, W.S., Vogelstein, B., Childs, B., Kinzler, K.W. (Accessed 2007). [http://www.ommbid.com The Online Metabolic and Molecular Bases of Inherited Disease]. New York: McGraw-Hill. - Summaries of 255 chapters, full text through many universities. There is also the [http://books.mcgraw-hill.com/medical/ommbid/blog/ OMMBID blog].
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* For more online resources and references, see [[inborn errors of metabolism]].
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{{AminoAcids}}
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[[Category:Proteinogenic amino acids]]
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[[Category:Glucogenic amino acids]]
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[[Category:Cyclic amino acids]]
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Latest revision as of 16:55, 22 April 2009

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Proline
Proline
General
Systematic name ?
Other names ?
Molecular formula ?
SMILES ?
Molar mass ?.?? g/mol
Appearance ?
CAS number [?-?-?]
Properties
Density and phase ? g/cm³, ?
Solubility in water ? g/100 ml (?°C)
Melting point ?°C (? K)
Boiling point ?°C (? K)
Acidity (pKa) ?
Basicity (pKb) ?
Chiral rotation [α]D ?°
Viscosity ? cP at ?°C
Structure
Molecular shape ?
Coordination
geometry 		?
Crystal structure ?
Dipole moment ? D
Hazards
MSDS External MSDS
Main hazards ?
NFPA 704
Flash point ?°C
R/S statement R: ?
S: ?
RTECS number ?
Supplementary data page
Structure and
properties 		n, εr, etc.
Thermodynamic
data 		Phase behaviour
Solid, liquid, gas
Spectral data UV, IR, NMR, MS
Related compounds
Other anions ?
Other cations ?
Related ? ?
Related compounds ?
Except where noted otherwise, data are given for
materials in their standard state (at 25 °C, 100 kPa)
Infobox disclaimer and references


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 synthesize it. It is unique among the 20 protein-forming amino acids because the α-amino group is secondary.

Biosynthesis

Proline is biosynthetically derived from the amino acid L-glutamate and its immediate precursor is the imino acid (S)-1-pyrroline-5-carboxylate (P5C). Enzymes involved in a typical biosynthesis include:[1]

  1. Glutamate kinase (ATP-dependent)
  2. Glutamate dehydrogenase (requires NADH or NADPH)
  3. Pyrroline-5-carboxylate reductase (requires NADH or NADPH)

Structural properties

The distinctive cyclic structure of proline's side chain locks its backbone dihedral angle at approximately -75°, giving proline an exceptional conformational rigidity compared to other amino acids. Hence, proline loses less conformational entropy upon folding, which may account for its higher prevalence in the proteins of thermophilic organisms. Proline acts as a structural disruptor in the middle of regular secondary structure elements such as alpha helices and beta sheets; however, proline is commonly found as the first residue of an alpha helix and also in the edge strands of beta sheets. Proline is also commonly found in turns, which may account for the curious fact that proline is usually solvent-exposed, despite having a completely aliphatic side chain. Because proline lacks a hydrogen on the amide group, it cannot act as a hydrogen bond donor, only as a hydrogen bond acceptor.

Multiple prolines and/or hydroxyprolines in a row can create a polyproline helix, the predominant secondary structure in collagen. The hydroxylation of proline by prolyl hydroxylase (or other additions of electron-withdrawing substituents such as fluorine) increases the conformational stability of collagen significantly. Hence, the hydroxylation of proline is a critical biochemical process for maintaining the connective tissue of higher organisms. Severe diseases such as scurvy can result from defects in this hydroxylation, e.g., mutations in the enzyme prolyl hydroxylase or lack of the necessary ascorbate (vitamin C) cofactor.

Sequences of proline and 2-aminoisobutyric acid (Aib) also form a helical turn structure[How to reference and link to summary or text].

In 2006, scientists at ASU discovered that solutions of TiO2 illuminated with ultraviolet radiation can serve as an extremely cost-effective and accurate protein cleavage catalyst. The TiO2 catalyst preferentially and rapidly cleaves protein at sites where proline is present, while taking much longer to degrade the protein from its endpoints.[2]

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 atom than does the following 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.

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.

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.

History

Hermann Emil Fischer discovered Proline between 1899 and 1908.

See also

  • Collagen
  • Polyproline helix
  • Peptide bond (for more discussion of cis-trans isomerization)
  • Hyperprolinemia

External links

Notes

  1. ↑ Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. ISNB 1-57259-153-6.
  2. ↑ B. J. Jones, M. J. Vergne, D. M. Bunk, L. E. Locascio and M. A. Hayes (2007). Cleavage of Peptides and Proteins Using Light-Generated Radicals from Titanium Dioxide. Anal. Chem. 79 (4): 1327–1332.

References

  • Balbach J, Schmid FX. (2000). Proline isomerization and its catalysis in protein folding. In Mechanisms of Protein Folding 2nd ed. Editor RH Pain. Oxford University Press.
  • For a thorough scientific overview of disorders of proline and hydroxyproline metabolism, one can consult chapter 81 of OMMBID Charles Scriver, Beaudet, A.L., Valle, D., Sly, W.S., Vogelstein, B., Childs, B., Kinzler, K.W. (Accessed 2007). The Online Metabolic and Molecular Bases of Inherited Disease. New York: McGraw-Hill. - Summaries of 255 chapters, full text through many universities. There is also the OMMBID blog.
  • For more online resources and references, see inborn errors of metabolism.


Amino acids

Alanine | Arginine | Asparagine | Aspartic acid | Cysteine | Glutamic acid | Glutamine | Glycine | Histidine | Isoleucine | Leucine | Lysine | Methionine | Phenylalanine | Proline | Serine | Threonine | Tryptophan | Tyrosine | Valine
Essential amino acid | Protein | Peptide | Genetic code
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