Record Information
Version2.0
Creation Date2012-05-31 10:22:27 -0600
Update Date2015-09-13 12:56:06 -0600
Secondary Accession Numbers
  • ECMDB00162
Identification
Name:L-Proline
DescriptionL-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins. Proline is sometimes called an imino acid, although the IUPAC definition of an imine requires a carbon-nitrogen double bond. Proline is a non-essential amino acid that is synthesized from glutamic acid. It is an essential component of collagen and is important for proper functioning of joints and tendons.
Structure
Thumb
Synonyms:
  • (-)-(S)-Proline
  • (-)-2-Pyrrolidinecarboxylate
  • (-)-2-Pyrrolidinecarboxylic acid
  • (-)-Proline
  • (S)-(-)-Proline
  • (S)-(-)-Pyrrolidine-2-carboxylate
  • (S)-(-)-Pyrrolidine-2-carboxylic acid
  • (S)-2-Carboxypyrrolidine
  • (S)-2-Pyrralidinecarboxylate
  • (S)-2-Pyrralidinecarboxylic acid
  • (S)-2-Pyrrolidinecarboxylate
  • (S)-2-Pyrrolidinecarboxylic acid
  • (S)-Proline
  • 2-Pyrrolidinecarboxylate
  • 2-Pyrrolidinecarboxylic acid
  • P
  • Pro
  • Prol
  • Proline
Chemical Formula:C5H9NO2
Weight:Average: 115.1305
Monoisotopic: 115.063328537
InChI Key:ONIBWKKTOPOVIA-BYPYZUCNSA-N
InChI:InChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1
CAS number:147-85-3
IUPAC Name:(2S)-pyrrolidine-2-carboxylic acid
Traditional IUPAC Name:L-proline
SMILES:OC(=O)[C@@H]1CCCN1
Chemical Taxonomy
Description belongs to the class of organic compounds known as proline and derivatives. Proline and derivatives are compounds containing proline or a derivative thereof resulting from reaction of proline at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentProline and derivatives
Alternative Parents
Substituents
  • Proline or derivatives
  • Alpha-amino acid
  • L-alpha-amino acid
  • Pyrrolidine carboxylic acid
  • Pyrrolidine carboxylic acid or derivatives
  • Pyrrolidine
  • Amino acid
  • Carboxylic acid
  • Secondary aliphatic amine
  • Monocarboxylic acid or derivatives
  • Secondary amine
  • Organoheterocyclic compound
  • Azacycle
  • Organic oxygen compound
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Organopnictogen compound
  • Organic oxide
  • Carbonyl group
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Aliphatic heteromonocyclic compound
Molecular FrameworkAliphatic heteromonocyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:0
Melting point:221 °C
Experimental Properties:
PropertyValueSource
Water Solubility:162.0 mg/mL [MERCK INDEX (1996)]PhysProp
LogP:-2.54 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility365 g/LALOGPS
logP-2.7ALOGPS
logP-2.6ChemAxon
logS0.5ALOGPS
pKa (Strongest Acidic)1.94ChemAxon
pKa (Strongest Basic)11.33ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area49.33 ŲChemAxon
Rotatable Bond Count1ChemAxon
Refractivity28.06 m³·mol⁻¹ChemAxon
Polarizability11.5 ųChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Adenosine triphosphate + Water + L-Proline > ADP + Hydrogen ion + Phosphate + L-Proline
Adenosine triphosphate + Water + L-Proline > ADP + Hydrogen ion + Phosphate + L-Proline
Water + L-Prolinylglycine > Glycine + L-Proline
Adenosine triphosphate + L-Proline + tRNA(Pro) + tRNA(Pro) <> Adenosine monophosphate + Pyrophosphate + L-Prolyl-tRNA(Pro) + L-Prolyl-tRNA(Pro)
L-D-1-Pyrroline-5-carboxylic acid + 2 Hydrogen ion + NADPH > NADP + L-Proline
FAD + L-Proline > L-D-1-Pyrroline-5-carboxylic acid + FADH2 + Hydrogen ion
L-Proline + NAD <> L-D-1-Pyrroline-5-carboxylic acid + NADH + Hydrogen ion
L-Proline + NADP <> L-D-1-Pyrroline-5-carboxylic acid + NADPH + Hydrogen ion
L-Proline + Acceptor + Quinone <> L-D-1-Pyrroline-5-carboxylic acid + Reduced acceptor + (S)-1-pyrroline-5-carboxylate + Hydroquinone
Adenosine triphosphate + L-Proline + tRNA(Pro) <> Adenosine monophosphate + Pyrophosphate + L-Prolyl-tRNA(Pro)
a dipeptide with proline at carboxy terminal + Water L-Proline + a standard &alpha; amino acid
Adenosine triphosphate + L-Proline + Water > ADP + Phosphate + L-Proline + Hydrogen ion
Adenosine triphosphate + L-Proline + Water > ADP + Phosphate + L-Proline + Hydrogen ion
NAD(P)<sup>+</sup> + L-Proline < NAD(P)H + L-D-1-Pyrroline-5-carboxylic acid + Hydrogen ion
L-Proline + an oxidized electron acceptor > L-D-1-Pyrroline-5-carboxylic acid + a reduced electron acceptor + Hydrogen ion
glycylproline + Water > Glycine + L-Proline
L-Proline + NAD(P)(+) > L-D-1-Pyrroline-5-carboxylic acid + NAD(P)H
L-Proline + acceptor > (S)-1-pyrroline-5-carboxylate + reduced acceptor
Adenosine triphosphate + L-Proline + tRNA(Pro) > Adenosine monophosphate + Pyrophosphate + L-prolyl-tRNA(Pro)
L-Proline + NAD + NADP <> (S)-1-pyrroline-5-carboxylate + NADH + NADPH + Hydrogen ion
1-Pyrroline-5-carboxylic acid + Hydrogen ion + NADPH + L-D-1-Pyrroline-5-carboxylic acid + NADPH > NADP + L-Proline + L-Proline
L-Proline + Ubiquinone-1 + L-Proline > Hydrogen ion + Ubiquinol-1 + 1-Pyrroline-5-carboxylic acid + L-D-1-Pyrroline-5-carboxylic acid
L-Proline + Adenosine triphosphate + Hydrogen ion + tRNA(Pro) + L-Proline > Adenosine monophosphate + Pyrophosphate + L-prolyl-tRNA(Pro)
L-Proline + Adenosine triphosphate + Water + L-Proline > L-Proline + Adenosine diphosphate + Phosphate + Hydrogen ion + ADP
L-D-1-Pyrroline-5-carboxylic acid + 2 Hydrogen ion + NADPH > NADP + L-Proline

SMPDB Pathways:
proline metabolismPW000794 ThumbThumb?image type=greyscaleThumb?image type=simple
tRNA Charging 2PW000803 ThumbThumb?image type=greyscaleThumb?image type=simple
tRNA chargingPW000799 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
385± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
451± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
361± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
143± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
550± 45 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
Download Details
532± 11 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
Download Details
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-0006-0910000000-a9127c0e370afb80259bView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-000f-0910000000-3195f21e625520d51316View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-0006-0900000000-119af746c347969e8ae7View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-006x-8900000000-b31beabb1ed6235e7145View in MoNA
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-00di-9100000000-c1c67bc521741ee891cbView in MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0006-1900000000-84e6fb318323fd0261b1View in MoNA
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-00xs-8910000000-74b0c34ca5fd7c85f1d9View in MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-00fu-9000000000-716c3d01b301162863b6View in MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-0006-0900000000-0d7354201ed866c87b13View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0006-0910000000-a9127c0e370afb80259bView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-000f-0910000000-3195f21e625520d51316View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0006-0900000000-119af746c347969e8ae7View in MoNA
GC-MSGC-MS Spectrum - GC-EI-QQ (Non-derivatized)splash10-001i-1920000000-09006ee4e7a137d8a45aView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-006x-8900000000-b31beabb1ed6235e7145View in MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0006-1900000000-84e6fb318323fd0261b1View in MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-00xs-8910000000-74b0c34ca5fd7c85f1d9View in MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-00di-9100000000-c1c67bc521741ee891cbView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-00fu-9000000000-d203e3dfb0701403a75bView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-00di-9000000000-56471980a375d26046caView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-03di-0900000000-2c23774af5f6a0c217d5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-03di-0900000000-d89c1e626ef24a79c89fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-03di-1900000000-fc27094f2eb75e65b438View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Negativesplash10-03di-0900000000-e1d0a4b20419dc7bae92View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-03di-0900000000-2c23774af5f6a0c217d5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-03di-0900000000-d89c1e626ef24a79c89fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-03di-1900000000-fc27094f2eb75e65b438View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , negativesplash10-03di-0900000000-e1d0a4b20419dc7bae92View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-00xr-9600000000-ba51a901e786b1a4663eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-00di-9000000000-f72e2f3812225708fc56View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-00di-9000000000-59887da6580f63bcc1c5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - EI-B (HITACHI M-80) , Positivesplash10-00fu-9000000000-c69dcaf7cb2d1e9d285eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-0930000000-984f9a23ebfe28f95017View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-9000000000-f75575cac28a54aa923dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-9000000000-221cfb8c82f3df76eb51View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-0900000000-e5741fd9870218d57cafView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-0900000000-6bc9b4e775be37fa18d9View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-9000000000-a8eb419b26655a6a1dabView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-9000000000-873ee03b61d1ffcae70fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-0900000000-61d583960651669fb9e6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Positivesplash10-014i-1900000000-3221c23504b8847abf8dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Positivesplash10-00di-9100000000-8169367f5127c57fae12View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Positivesplash10-00di-9000000000-f704eb8402fcacfccd18View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Positivesplash10-00di-9000000000-ccd74eea36efab2cbab8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Positivesplash10-00di-9000000000-9f214692cd39a6581813View in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,1H] 2D NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Azizi M, Ezan E, Reny JL, Wdzieczak-Bakala J, Gerineau V, Menard J: Renal and metabolic clearance of N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) during angiotensin-converting enzyme inhibition in humans. Hypertension. 1999 Mar;33(3):879-86. Pubmed: 10082503
  • Azizi M, Junot C, Ezan E, Menard J: Angiotensin I-converting enzyme and metabolism of the haematological peptide N-acetyl-seryl-aspartyl-lysyl-proline. Clin Exp Pharmacol Physiol. 2001 Dec;28(12):1066-9. Pubmed: 11903317
  • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. Pubmed: 19561621
  • Boden G, Rezvani I, Owen OE: Effects of glucagon on plasma amino acids. J Clin Invest. 1984 Mar;73(3):785-93. Pubmed: 6142902
  • Chambers, S. T., Kunin, C. M. (1987). "Osmoprotective activity for Escherichia coli in mammalian renal inner medulla and urine. Correlation of glycine and proline betaines and sorbitol with response to osmotic loads." J Clin Invest 80:1255-1260. Pubmed: 3316273
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. Pubmed: 12297216
  • Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. Pubmed: 12101068
  • Feldman JM, Plonk JW, Admiraal J, Sidbury, JB: Plasma amino acids in patients with the carcinoid syndrome. Cancer. 1976 Nov;38(5):2127-31. Pubmed: 136295
  • Hart W, van den Hamer CJ, van der Sluys Veer J: The use of hydroxy-DL-proline-2-(14)C in the investigation of hydroxyproline metabolism in normal subjects and in patients with renal insufficiency. Clin Nephrol. 1976 Sep;6(3):379-87. Pubmed: 991465
  • Hausmann D: [Post-traumatic imbalances of plasma amino acids--interference factors or defense mechanisms? A study of protein metabolism in severe craniocerebral trauma] Anasth Intensivther Notfallmed. 1988 Feb;23(1):14-21. Pubmed: 3364629
  • Humbertclaude V, Rivier F, Roubertie A, Echenne B, Bellet H, Vallat C, Morin D: Is hyperprolinemia type I actually a benign trait? Report of a case with severe neurologic involvement and vigabatrin intolerance. J Child Neurol. 2001 Aug;16(8):622-3. Pubmed: 11510941
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Kanwar YS, Krakower CA, Manaligod JR, Justice P, Wong PW: Biochemical, morphological and hybrid studies in hyperprolinemic mice. Biomedicine. 1975 May;22(3):209-16. Pubmed: 240452
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Lu SH, Ohshima H, Fu HM, Tian Y, Li FM, Blettner M, Wahrendorf J, Bartsch H: Urinary excretion of N-nitrosamino acids and nitrate by inhabitants of high- and low-risk areas for esophageal cancer in Northern China: endogenous formation of nitrosoproline and its inhibition by vitamin C. Cancer Res. 1986 Mar;46(3):1485-91. Pubmed: 3943105
  • Roesel RA, Blankenship PR, Mobley EB, Coryell ME: Increased excretion of histidyl-L-proline diketopiperazine by infants receiving Pregestimil and Nutramigen formulas. Clin Chem. 1986 May;32(5):865-7. Pubmed: 3698278
  • Scriver CR, McInnes RR, Mohyuddin F: Role of epithelial architecture and intracellular metabolism in proline uptake and transtubular reclamation in PRO/re mouse kidney. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1431-5. Pubmed: 1055415
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. Pubmed: 12097436
  • Simila S: Hydroxyproline metabolism in type II hyperprolinaemia. Ann Clin Biochem. 1979 Jul;16(4):177-81. Pubmed: 533224
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. Pubmed: 18402659
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference: Itoh, Tamio. Synthesis of L-proline from L-glutamine. Bulletin of the Chemical Society of Japan (1963), 36(1), 25-9
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID17203
HMDB IDHMDB00162
Pubchem Compound ID145742
Kegg IDC00148
ChemSpider ID128566
WikipediaL-Proline
BioCyc IDPRO
EcoCyc IDPRO
Ligand ExpoPRO_LFZW

Enzymes

General function:
Involved in proteolysis
Specific function:
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation
Gene Name:
pepN
Uniprot ID:
P04825
Molecular weight:
98918
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
General function:
Involved in oxidoreductase activity
Specific function:
Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon
Gene Name:
putA
Uniprot ID:
P09546
Molecular weight:
143814
Reactions
L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
(S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 H(2)O = L-glutamate + NAD(P)H.
General function:
Involved in oxidation-reduction process
Specific function:
L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H
Gene Name:
proC
Uniprot ID:
P0A9L8
Molecular weight:
28145
Reactions
L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H.
General function:
Involved in nucleotide binding
Specific function:
Involved in a multicomponent binding-protein-dependent transport system for glycine betaine/L-proline
Gene Name:
proV
Uniprot ID:
P14175
Molecular weight:
44162
General function:
Involved in hydrolase activity
Specific function:
Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source
Gene Name:
pepD
Uniprot ID:
P15288
Molecular weight:
52915
Reactions
Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
General function:
Involved in nucleotide binding
Specific function:
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction:proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by ybaK
Gene Name:
proS
Uniprot ID:
P16659
Molecular weight:
63692
Reactions
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
General function:
Involved in cellular process
Specific function:
Splits dipeptides with a prolyl residue in the C- terminal position and a polar or nonpolar amino acid at the N- terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX
Gene Name:
pepQ
Uniprot ID:
P21165
Molecular weight:
50176
Reactions
Hydrolysis of Xaa-|-Pro dipeptides
also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
General function:
Involved in aminopeptidase activity
Specific function:
Probably plays an important role in intracellular peptide degradation
Gene Name:
pepB
Uniprot ID:
P37095
Molecular weight:
46180
Reactions
Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln.
General function:
Involved in aminopeptidase activity
Specific function:
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place
Gene Name:
pepA
Uniprot ID:
P68767
Molecular weight:
54879
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
General function:
Involved in transporter activity
Specific function:
Involved in a multicomponent binding-protein-dependent transport system for glycine betaine/L-proline
Gene Name:
proW
Uniprot ID:
P14176
Molecular weight:
37619
General function:
Involved in transporter activity
Specific function:
Member of a multicomponent binding-protein-dependent transport system (the proU transporter) which serves as the glycine betaine/L-proline transporter
Gene Name:
proX
Uniprot ID:
P0AFM2
Molecular weight:
36022

Transporters

General function:
Involved in proteolysis
Specific function:
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation
Gene Name:
pepN
Uniprot ID:
P04825
Molecular weight:
98918
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
General function:
Involved in proline:sodium symporter activity
Specific function:
Catalyzes the sodium-dependent uptake of extracellular L-proline. This protein is also capable of using lithium as the transport cation. Also catalyzes the uptake of propionate
Gene Name:
putP
Uniprot ID:
P07117
Molecular weight:
54344
General function:
Involved in nucleotide binding
Specific function:
Probably part of a binding-protein-dependent transport system yecCS for an amino acid. Probably responsible for energy coupling to the transport system
Gene Name:
yecC
Uniprot ID:
P37774
Molecular weight:
27677
General function:
Involved in transporter activity
Specific function:
Probably part of the binding-protein-dependent transport system yecCS for an amino acid; probably responsible for the translocation of the substrate across the membrane
Gene Name:
yecS
Uniprot ID:
P0AFT2
Molecular weight:
24801
General function:
Involved in transport
Specific function:
Permease that is involved in the transport across the cytoplasmic membrane of proline
Gene Name:
proY
Uniprot ID:
P0AAE2
Molecular weight:
50215
General function:
Involved in transporter activity
Specific function:
Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response
Gene Name:
proP
Uniprot ID:
P0C0L7
Molecular weight:
54845
General function:
Involved in transporter activity
Specific function:
Involved in a multicomponent binding-protein-dependent transport system for glycine betaine/L-proline
Gene Name:
proW
Uniprot ID:
P14176
Molecular weight:
37619
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368