L-Proline (ECMDB00162) (M2MDB000064)
| Record Information | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Version | 2.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Creation Date | 2012-05-31 10:22:27 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Update Date | 2015-09-13 12:56:06 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Secondary Accession Numbers |
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| Identification | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Name: | L-Proline | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Description | L-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 |  | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Synonyms: |
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| 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. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Organic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Super Class | Organic acids and derivatives | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Class | Carboxylic acids and derivatives | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sub Class | Amino acids, peptides, and analogues | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Direct Parent | Proline and derivatives | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative Parents | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Substituents |
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| Molecular Framework | Aliphatic heteromonocyclic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| External Descriptors |
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| Physical Properties | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| State: | Solid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Charge: | 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Melting point: | 221 °C | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties: |
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| Predicted Properties |
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| 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 α 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 Adenosine triphosphate + L-Proline + tRNA(Pro) <> Adenosine monophosphate + Pyrophosphate + L-Prolyl-tRNA(Pro) More...Adenosine triphosphate + L-Proline + tRNA(Pro) <> Adenosine monophosphate + Pyrophosphate + L-Prolyl-tRNA(Pro) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SMPDB Pathways: |
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| KEGG Pathways: | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| EcoCyc Pathways: |
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| Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Find out more about how we convert literature concentrations. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Spectra | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Spectra: | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| References | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| References: |
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| 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) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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