74-79-3 Usage
Indications and Usage
Odorless, slightly bitter. Easily soluble in water (solubility in 0℃ water is 83g/L, solubility in 50℃ water is 400g/L), very slightly soluble in ethanol, insoluble in ether; pI6.0; loses its 2-molecule water crystal when heated to 105℃, darkens in color at 230℃, disintegrates at 244℃; its aqueous solution has maximum absorption at 205nm (1gε3.28).
L-Arginine is an encoding amino acid in protein synthesis and is one of the 8 essential amino acids in the human body. The body needs it for many different functions. Taking L-Arginine supplements can treat certain diseases such as congestive heart failure and cystitis. L-Arginine can also act as seasoning for nutrient supplements and food additives. L-Arginine can undergo a heat reaction with sugar (amino-carbonyl reaction) to obtain a unique fragrance, GB 2760-2001, an approved food spice. As an amino acid drug, L-Arginine can be used as pharmaceutical raw material and is an important ingredient in amino acid infusions and integrated amino acid preparations. It is also a crucial amino acid in maintaining infant growth and maturation.
Mechanisms of Action
L-Arginine can stimulate the human body to release certain chemicals such as insulin and human growth hormone. It can also clear ammonia in the body and promote the healing of wounds. The human body also needs it to produce sarcosine. Decomposing L-Arginine produces nitric oxide, which can expand blood vessels and increase blood flow. L-Arginine is an intermediate metabolite in the orthinine cycle and promotes the conversion of ammonia to urea, thus lowering the blood concentration of ammonia. L-Arginine is also an important part of sperm protein and can promote spermatogenesis and provide energy for sperm movement. Additionally, intravenous arginine can stimulate the pituitary to release growth hormone and can be used to test pituitary functions.
Adverse reactions
Abdominal pain, diarrhea, gout and bloating. There may also be increased severity in herpes breakouts and increased effects of antihypertensive drugs, resulting in a lower blood pressure than expected, which may cause hypertensive patients to experience dizziness and fainting.
Toxicity Level
Moderate
Acute Toxicity
Reference data: abdominal cavity – large rat LD50: 3793 mg/kg.
Flammability Characteristics
Flammable. Burning produces toxic nitrogen oxide smoke.
Handling
Store in ventilated, cool and dry area.
Extinguishers
Dry powder, foam, sand, carbon dioxide, water mist.
Chemical Properties
Different sources of media describe the Chemical Properties of 74-79-3 differently. You can refer to the following data:
1. Arginine is a diaminomonocarboxylic acid. The nonessential amino acid, arginine, is a urea cycle amino acid and a
precursor for the neurotransmitter nitric oxide, which plays a role in the regulation of the brain’s system of dilation and constriction
of small blood vessels. It is strongly alkaline and its water solutions absorb carbon dioxide from the air (FCC, 1996). Functionality in
foods includes, but is not limited to, nutrient and dietary supplement
2. White crystalline powder
Occurrence
Reported present in cheese, chocolate, eggs, meat, nuts and other products.
Uses
Different sources of media describe the Uses of 74-79-3 differently. You can refer to the following data:
1. L-Arginine is used for heart and blood vessel conditions which includes congestive heart failure (CHF), chest pain, high blood pressure and coronary artery disease. It plays a vital role in the treatment of cardiovascular disease due to it being antiatherogenic, anti-ischemic, antiplatelet and antithrombotic. It acts as a growth stimulant and is involved in the treatment of erectile dysfunction in men. It is an important ingredient of tooth paste which provides effective relief for sensitive teeth.
2. Amino acid; nutrient.
3. L-Arginine has been used:as a Roswell park memorial institute medium (RPMI) media component in the isolation and culture of peripheral blood mononuclear cells (PBMCs)as a RPMI media component for tissue culturein DMEM medium for the identification and quantification of phosphorylation sites by stable isotope labeling by amino acids in cell culture (SILAC) and LCMS/MS
Definition
ChEBI: An L-alpha-amino acid that is the L-isomer of arginine.
Aroma threshold values
Detection at 100%, faint.
Taste threshold values
Taste characteristics at 1000 ppm: hint of sourness.
General Description
L-Arginine is an amino acid that plays a key role in many physiological processes such as tissue repair and reproduction. It is a key precursor for synthesizing nitric oxide in mammals. Due to these factors, the dietary supplementation with L-arginine may show a range of health benefits.
Biochem/physiol Actions
Substrate of nitric oxide synthase, which is converted to citrulline and nitric oxide (NO). Induces insulin release by a nitric oxide-dependent mechanism.
Safety Profile
Mutation data reported. Whenheated to decomposition it emits toxic fumes of NOx.
Synthesis
Enzymatically, arginine is formed in two reactions from citrulline. The first reaction (citrulline + succinate) is catalyzed
by the enzyme arginosuccinate synthetase. It is ATP dependent and with the formation of a new C–N bond in the gaunidino group of
arginosuccinate, water is removed and ATP is hydrolyzed. The second reaction is catalyzed by arginine synthetase and involves the
scission of arginosuccinate with the formation of arginine and fumaric acid.
Purification Methods
S-Arginine crystallises from H2O as the dihydrate and as plates from EtOH. It also crystallises from 66% EtOH. Its solubility in H2O is 15% at 21o. Its isoelectric point is at pH 10.76. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 p 1841 1961, Beilstein 4 IV 817.]
Check Digit Verification of cas no
The CAS Registry Mumber 74-79-3 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 7 and 4 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 74-79:
(4*7)+(3*4)+(2*7)+(1*9)=63
63 % 10 = 3
So 74-79-3 is a valid CAS Registry Number.
InChI:InChI=1/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/p+1/t4-/m0/s1
74-79-3Relevant articles and documents
Binding Methylarginines and Methyllysines as Free Amino Acids: A Comparative Study of Multiple Host Classes**
Bayer, Peter,Hof, Fraser,Isaacs, Lyle,Kamba, Bianca E.,Le, My-Hue,Schrader, Thomas,Warmerdam, Zoey
, (2021/11/30)
Methylated free amino acids are an important class of targets for host-guest chemistry that have recognition properties distinct from those of methylated peptides and proteins. We present comparative binding studies for three different host classes that are each studied with multiple methylated arginines and lysines to determine fundamental structure-function relationships. The hosts studied are all anionic and include three calixarenes, two acyclic cucurbiturils, and two other cleft-like hosts, a clip and a tweezer. We determined the binding association constants for a panel of methylated amino acids using indicator displacement assays. The acyclic cucurbiturils display stronger binding to the methylated amino acids, and some unique patterns of selectivity. The two other cleft-like hosts follow two different trends, shallow host (clip) following similar trends to the calixarenes, and the other more closed host (tweezer) binding certain less-methylated amino acids stronger than their methylated counterparts. Molecular modelling sheds some light on the different preferences of the various hosts. The results identify hosts with new selectivities and with affinities in a range that could be useful for biomedical applications. The overall selectivity patterns are explained by a common framework that considers the geometry, depth of binding pockets, and functional group participation across all host classes.
Sequence-Selective Protection of Peptides from Proteolysis
Li, Xiaowei,Chen, Kaiqian,Zhao, Yan
supporting information, p. 11092 - 11097 (2021/04/05)
Proteolysis of proteins and peptides is involved in the infection of cells by enveloped viruses and also in the invasion and spread of cancer cells. Shutting down broad-specificity proteases, however, is problematic because normal functions by these proteases will be affected. Herein, nanoparticle receptors were prepared from molecular imprinting for complex biological peptides. Their strong and selective binding enabled them to protect their targeted sequences from proteolysis in aqueous solution at stoichiometric amounts. Generality of the method was demonstrated by the protection of hydrophobic and hydrophilic peptides from different proteases, selective protection of a segment of a long peptide, and selective protection of a targeted peptide in a mixture. Most interestingly, two receptors targeting different parts of a long peptide could work in cooperation to protect the overall sequence, highlighting the versatility of the method.
Mutations of key substrate binding residues of leishmanial peptidase T alter its functional and structural dynamics
Bhat, Saleem Yousuf,Qureshi, Insaf Ahmed
, (2019/11/11)
Background: M20 aminopeptidases, such as Peptidase T (PepT), are implicated in the hydrolysis of oligopeptides during the terminal stages of protein degradation pathway to maintain turnover. Therefore, specific inhibition of PepT bores well for the development of novel next-generation antileishmanials. This work describes the metal dependence, substrate preferences and inhibition of PepT, and demonstrates in detail the role of its two conserved substrate binding residues. Methods: PepT was purified and characterized using a scheme of peptide substrates and peptidomimetic inhibitors. Residues T364 and N378 were mutated and characterized with an array of biochemical, biophysical and structural biology methods. Results: PepT sequence carries conserved motifs typical of M20 peptidases and our work on its biochemistry shows that this cytosolic enzyme carries broad substrate specificity with best cleavage preference for peptides carrying alanine at the P1 position. Peptidomimetics amastatin and actinonin occupied S1 pocket by competing with the substrate for binding to active site and inhibited PepT potently, while arphamenine A and bestatin were less effective inhibitors. We further show that the mutation of conserved substrate binding residues (T364 and N378) to alanine affects structure, reduces substrate binding and alters the amidolytic activity of this dimeric enzyme. Conclusions: PepT preferentially hydrolyzes oligopeptides carrying alanine at P1 position and is potently inhibited by peptidomimetics. Reduced substrate binding after mutations was a key factor involved in amidolytic digressions. General significance: This study provides insights for further exploration of the druggability of PepT and highlights prospective applications of this enzyme along with its mutazyme T364A/N378A.