L-Glutamyl-L-Proline
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| Category | Others |
| Catalog number | BBF-05385 |
| CAS | 41745-47-5 |
| Molecular Weight | 244.24 |
| Molecular Formula | C10H16N2O5 |
| Purity | ≥98% |
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Description
L-Glutamyl-L-Proline is a dipeptide composed of glutamate and proline. It is an incomplete breakdown product of protein digestion or protein catabolism.
Specification
| Synonyms | L-Proline, L-a-glutamyl-; L-α-Glutamyl-L-proline; Glutamyl-proline; L-Proline, L-alpha-glutamyl-; Glu-Pro; glutamylproline; H-EP-OH |
| Sequence | H-Glu-Pro-OH |
| IUPAC Name | (2S)-1-[(2S)-2-amino-4-carboxybutanoyl]pyrrolidine-2-carboxylic acid |
| Canonical SMILES | C1CC(N(C1)C(=O)C(CCC(=O)O)N)C(=O)O |
| InChI | InChI=1S/C10H16N2O5/c11-6(3-4-8(13)14)9(15)12-5-1-2-7(12)10(16)17/h6-7H,1-5,11H2,(H,13,14)(H,16,17)/t6-,7-/m0/s1 |
| InChI Key | YBTCBQBIJKGSJP-BQBZGAKWSA-N |
Properties
| Appearance | Solid |
| Boiling Point | 558.1±50.0°C at 760 mmHg |
| Density | 1.4±0.1 g/cm3 |
| Solubility | Soluble in Water |
Reference Reading
1. Roles of cathepsins in reperfusion-induced apoptosis in cultured astrocytes
Kazuhiro Takuma, Makiko Kiriu, Koichi Mori, Eibai Lee, Riyo Enomoto, Akemichi Baba, Toshio Matsuda Neurochem Int. 2003 Jan;42(2):153-9. doi: 10.1016/s0197-0186(02)00077-3.
Astrocytic apoptosis may play a role in the central nervous system injury. We previously showed that reperfusion of cultured astrocytes with normal medium after exposure to hydrogen peroxide (H(2)O(2))-containing medium causes apoptosis. This study examines the involvement of the lysosomal enzymes cathepsins B and D in the astrocytic apoptosis. Reperfusion after exposure to H(2)O(2) caused a marked increase in caspase-3 and cathepsin D activities and a marked decrease in cathepsin B activity. Pepstatin A, an inhibitor of cathepsin D, and acetyl-L-aspartyl-L-methionyl-L-glutaminyl-L-aspart-1-aldehyde (Ac-DMQD-CHO), a specific inhibitor of caspase-3, blocked the H(2)O(2)-induced decrease in cell viability and DNA ladder formation in cultured rat astrocytes. The (L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester (CA074 Me), a specific inhibitor of cathepsin B, did not affect the H(2)O(2)-induced cell injury. On the other hand, CA074 Me decreased cell viability with DNA ladder formation when cultured in the presence of Ac-DMQD-CHO. This caspase-independent apoptosis was attenuated by the addition of the cathepsin D inhibitor pepstatin A. Caspase-3 like activity was markedly inhibited by Ac-DMQD-CHO and partially by pepstatin A. Pepstatin A and CA074 Me inhibited cathepsin B and cathepsin D activities, respectively, in the presence and absence of Ac-DMQD-CHO. These results suggest that cathepsins B and D are involved in astrocytic apoptosis: cathepsin D acts as a death-inducing factor upstream of caspase-3 and the caspase-independent apoptosis is regulated antagonistically by cathepsins B and D.
2. L-amino acid ligase from Pseudomonas syringae producing tabtoxin can be used for enzymatic synthesis of various functional peptides
Toshinobu Arai, Yasuhiro Arimura, Shun Ishikura, Kuniki Kino Appl Environ Microbiol. 2013 Aug;79(16):5023-9. doi: 10.1128/AEM.01003-13. Epub 2013 Jun 14.
Functional peptides are expected to be beneficial compounds that improve our quality of life. To address the growing need for functional peptides, we have examined peptide synthesis by using microbial enzymes. l-Amino acid ligase (Lal) catalyzes the condensation of unprotected amino acids in an ATP-dependent manner and is applicable to fermentative production. Hence, Lal is a promising enzyme to achieve cost-effective synthesis. To obtain a Lal with novel substrate specificity, we focused on the putative Lal involved in the biosynthesis of the dipeptidic phytotoxin designated tabtoxin. The tabS gene was cloned from Pseudomonas syringae NBRC14081 and overexpressed in Escherichia coli cells. The recombinant TabS protein produced showed the broadest substrate specificity of any known Lal; it detected 136 of 231 combinations of amino acid substrates when dipeptide synthesis was examined. In addition, some new substrate specificities were identified and unusual amino acids, e.g., l-pipecolic acid, hydroxy-l-proline, and β-alanine, were found to be acceptable substrates. Furthermore, kinetic analysis and monitoring of the reactions over a short time revealed that TabS showed distinct substrate selectivity at the N and C termini, which made it possible to specifically synthesize a peptide without by-products such as homopeptides and heteropeptides with the reverse sequence. TabS specifically synthesized the following functional peptides, including their precursors: l-arginyl-l-phenylalanine (antihypertensive effect; yield, 62%), l-leucyl-l-isoleucine (antidepressive effect; yield, 77%), l-glutaminyl-l-tryptophan (precursor of l-glutamyl-l-tryptophan, which has antiangiogenic activity; yield, 54%), l-leucyl-l-serine (enhances saltiness; yield, 83%), and l-glutaminyl-l-threonine (precursor of l-glutamyl-l-threonine, which enhances saltiness; yield, 96%). Furthermore, our results also provide new insights into tabtoxin biosynthesis.
3. Phosphate ions and glutaminyl cyclases catalyze the cyclization of glutaminyl residues by facilitating synchronized proton transfers
Franziska Seifert, Hans-Ulrich Demuth, Teresa Weichler, Hans-Henning Ludwig, Kai Tittmann, Stephan Schilling Bioorg Chem. 2015 Jun;60:98-101. doi: 10.1016/j.bioorg.2015.04.005. Epub 2015 Apr 24.
Phosphate ions and glutaminyl cyclase (QC) both catalyze the formation of pyroglutamate (pE, pGlu) from N-terminal glutamine residues of peptides and proteins. Here, we studied the mechanism of glutamine cyclization using kinetic secondary deuterium and solvent isotope effects. The data suggest that proton transfer(s) are rate determining for the spontaneous reaction, and that phosphate and QC are accelerating the reaction by promoting synchronized proton transfers in a concerted mechanism. Thus, non-enzymatic and enzymatic catalysis of pyroglutamate formation exploit a similar mode of transition-state stabilization.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
