443-79-8

Basic information

• Product Name: DL-Isoleucine
• Synonyms: Isoleucine, DL- (8CI);DL-Ile;NSC 9958
• CAS NO: 443-79-8
• Molecular Formula: C₆H₁₃NO₂
• Molecular Weight: 131.17292
• EINECS: 207-139-8
• Mol File: 443-79-8.mol

Chemical Properties

• Melting Point: 210℃
• Boiling Point: 225.8 °C at 760 mmHg
• Flash Point: 90.3 °C
• Appearance: white powder
• Density: 1.035 g/cm³
• Vapor Pressure: 0.0309mmHg at 25°C
• Refractive Index: 1.462
• Water Solubility: 22.3 g/L (25℃)
• CAS DataBase Reference: DL-Isoleucine(CAS DataBase Reference)
• NIST Chemistry Reference: DL-Isoleucine(443-79-8)
• EPA Substance Registry System: DL-Isoleucine(443-79-8)

Safety Data

• Safety Statements: S24/25:
• Hazardous Substances Data: 443-79-8(Hazardous Substances Data)

Usage

Uses

Used in Nutritional Supplements:
DL-Isoleucine is used as a nutritional supplement to support protein synthesis, muscle repair, and growth. It helps athletes and fitness enthusiasts to enhance their muscle mass and strength, as well as to promote faster recovery after intense workouts.
Used in Medical Applications:
DL-Isoleucine is used in medical applications to support individuals with certain health conditions that may affect their ability to synthesize or absorb this essential amino acid. It can help in the management of conditions such as liver disease, where the body's ability to produce amino acids may be compromised.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, DL-Isoleucine is used as an active ingredient in various formulations, including injectable solutions and oral medications, to address specific health needs related to amino acid deficiencies or imbalances.
Used in Food and Beverage Industry:
DL-Isoleucine is used in the food and beverage industry as a flavor enhancer and a nutritional additive in protein-rich products, such as sports drinks, meal replacement shakes, and energy bars. It helps to improve the taste and nutritional profile of these products, making them more appealing to consumers seeking high-quality protein sources.
Used in Animal Nutrition:
In animal nutrition, DL-Isoleucine is used as a feed additive to ensure a balanced amino acid profile in livestock diets. It helps to optimize the growth, health, and productivity of animals, particularly in intensive farming systems where the quality of feed can be a critical factor in overall performance.

InChI:InChI=1/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)

Upstream product

• 319-78-8 D-Isoleucine 
• 66277-23-4 D,L-β-methylenenorvaline 
• 1460-34-0 2-oxo-3(RS)-methylvaleric acid 
• 91741-17-2 DL-isoleucyl-leucyl anhydride 
• 7664-93-9 sulfuric acid 
• 61548-98-9 C₉H₉NO₂C₂H₃CHC 
• 96-17-3 2-Methylbutyraldehyde 
• 922-63-4 ethylacrolein 
• 67000-01-5 methyltertbutyl ether 
• 328-39-2 LEUCINE 
• 42880-22-8 2-bromo-3-methylpentanoic acid 
• 69946-40-3 N-hydroxy-2-imino-3-methylpentanoic acid 
• 4372-15-0 sec-butyl-malonic acid 
• 50706-06-4 3-methyl-2-phenylhydrazono-valeric acid 

Downstream Products

• 96-17-3 2-Methylbutyraldehyde 
• 73-32-5 L-isoleucine 
• 921-48-2 1-chloro-2-methylbutanecarboxylic acid 
• 2577-46-0 2-Amino-3-methyl-pentanoic acid methyl ester 
• 4101-35-3 N-formyl-isoleucine 
• 921-74-4 isoleucine ethylester 
• 4427-08-1 2-benzamido-3-methylpentanoic acid 
• 86323-41-3 3-Methyl-2-(4-nitro-benzoylamino)-pentanoic acid isopropyl ester 
• 86323-52-6 3-Methyl-2-(4-nitro-benzoylamino)-pentanoic acid isopropyl ester 
• 3160-59-6 N-benzyloxycarbonyl-isoleucine 
• 73-32-5 D-isoleucine 
• 56-40-6 glycine 

Relevant articles and documents

Rational engineering ofAcinetobacter tandoiiglutamate dehydrogenase for asymmetric synthesis ofl-homoalanine through biocatalytic cascades

l-Homoalanine, a useful building block for the synthesis of several chiral drugs, is generally synthesized through biocascades using natural amino acids as cheap starting reactants. However, the addition of expensive external cofactors and the low efficiency of leucine dehydrogenases towards the intermediate 2-ketobutyric acid are two major challenges in industrial applications. Herein, a dual cofactor-dependent glutamate dehydrogenase fromAcinetobacter tandoii(AtGluDH) was identified to help make full use of the intracellular pool of cofactors when using whole-cell catalysis. Through reconstruction of the hydrophobic network between the enzyme and the terminal methyl group of the substrate 2-ketobutyric acid, the strict substrate specificity ofAtGluDH towards α-ketoglutarate was successfully changed, and the activity obtained by the most effective mutant (K76L/T180C) was 17.2 times higher than that of the wild-type protein. A three-enzyme co-expression system was successfully constructed in order to help release the mass transfer restriction. Using 1 Ml-threonine, which is close to the solubility limit, we obtained a 99.9% yield ofl-homoalanine in only 3.5 h without adding external coenzymes to the cascade, giving 99.9% ee and a 29.2 g L?1h?1space-time yield. Additionally, the activities of the engineeredAtGluDH towards some other hydrophobic amino acids were also improved to 1.1-11.2 fold. Therefore, the engineering design of some dual cofactor-dependent GluDHs could not only eliminate the low catalytic activity of unnatural substrates but also enhance the cofactor utilization efficiency of these enzymes in industrial applications.

Direct Synthesis of Free α-Amino Acids by Telescoping Three-Step Process from 1,2-Diols

A practical telescoping three-step process for the syntheses of α-amino acids from the corresponding 1,2-diols has been developed. This process enables the direct synthesis of free α-amino acids without any protection/deprotection step. This method was also effective for the preparation of a 15N-labeled α-amino acid. 1,2-Diols bearing α,β-unsaturated ester moieties afforded bicyclic α-amino acids through intramolecular [3 + 2] cycloadditions. A preliminary study suggests that the resultant α-amino acids are resolvable by aminoacylases with almost complete selectivity.

Versiquinazolines A-K, Fumiquinazoline-Type Alkaloids from the Gorgonian-Derived Fungus Aspergillus versicolor LZD-14-1

Eleven fumiquinazoline-type alkaloids, namely, versiquinazolines A-K (1-11), along with cottoquinazolines B-D, were isolated from the gorgonian-derived fungus Aspergillus versicolor LZD-14-1. Their structures were determined by extensive analyses of the spectroscopic data (1D and 2D NMR, HRESIMS), in addition to the experimental and calculated ECD data and X-ray single-crystal diffraction analysis for the assignments of the absolute configurations. Versiquinazolines A, B, and F (1, 2, and 6), bearing a methanediamine or an aminomethanol unit and representing a unique subtype of fumiquinazolines, were found from nature for the first time. Possible biogenetic relationships of the versiquinazolines are postulated. In addition, the structures of cottoquinazolines B (12), D (13), and C (14) should be revised to the enantiomers. Compounds 1, 2, 7, and 11 exhibited inhibitory activities against thioredoxin reductase (IC50 values ranging from 12 to 20 μM).

Biocatalytic asymmetric synthesis of unnatural amino acids through the cascade transfer of amino groups from primary amines onto keto acids

Flee to the hills: An unfavorable equilibrium in the amino group transfer between amino acids and keto acids catalyzed by α-transaminases was successfully overcome by coupling with a ω-transaminase reaction as an equilibrium shifter, leading to efficient asymmetric synthesis of diverse unnatural amino acids, including L-tert-leucine and D-phenylglycine. Copyright

Asperterrestide A, a cytotoxic cyclic tetrapeptide from the marine-derived fungus Aspergillus terreus SCSGAF0162

A new cytotoxic and antiviral cyclic tetrapeptide, asperterrestide A (1), a new alkaloid, terremide C (2), and a new aromatic butenolide, aspernolide E (3), together with 10 known compounds were isolated from the fermentation broth of the marine-derived fungus Aspergillus terreus SCSGAF0162. Their structures were elucidated by spectroscopic analysis, and the absolute configuration of 1 was determined by the Mosher ester technique and analysis of the acid hydrolysates using a chiral-phase HPLC column. Compound 1 contains a rare 3-OH-N-CH3-Phe residue and showed cytotoxicity against U937 and MOLT4 human carcinoma cell lines and inhibitory effects on influenza virus strains H1N1 and H3N2.

Compositions, kits, and methods relating to the human FEZ1 gene, a novel tumor suppressor gene

The invention relates to isolated polynucleotides homologous with a portion of one strand of the human tumor suppressor gene, FEZ1, and to the tumor suppressor protein encoded thereby, Fez1. The polynucleotides are useful, for example, as probes, primers, portions of expression vectors, and the like. The invention also includes diagnostic, therapeutic, cell proliferation enhancement, and screening methods which involve these polynucleotides and protein. The invention further includes kits useful for performing the methods of the invention.

Determination of the complete absolute configuration of petriellin A

We report the full structural determination of the depsipeptide petriellin A. The absolute configuration of the amino acid residues, N-methyl isoleucine and N-methyl threonine, have been determined by a combination of HPLC and TLC comparison of synthetic Marfey's derivatives and Marfey's derivatives of the natural product hydrolysate. The configuration of the chiral centres in these two N-methylated residues was found to be the same as those of the common unmethylated l-amino acids. CSIRO 2006.

Direct synthesis of unprotected α-amino acids via allylation of hydroxyglycine

Hydroxyglycine, the ammonia adduct of glyoxylic acid, was found to react with various allylboronates in the presence of triethylamine in methanol to give unprotected α-amino acids directly with high stereoselectivity. For instance, the reactions with (E)- and (Z)-crotylboronates afforded the corresponding anti- and syn-crotylated products (isoleucine and alloisoleucine after hydrogenation) with high diastereoselectivity, respectively. Interestingly, it was found that isomerization of the products (γ-adducts to α-adducts) occurred under the reaction conditions in some cases. Control experiments have suggested that the isomerization took place via 2-aza (or azonia) Cope rearrangement of imines derived from γ-adducts and glyoxylic acid.

pH-Dependent Chemoselective Synthesis of α-Amino Acids. Reductive Amination of α-Keto Acids with Ammonia Catalyzed by Acid-Stable Iridium Hydride Complexes in Water

An acid-stable hydride complex [Cp*IrIII(bpy)H]+ {1, Cp* = η5-C5Me5, bpy = 2,2′-bipyridine} serves as the active catalyst for the highly chemoselective synthesis of α-amino acids by reductive aminatio

T-CELL SELECTIVE INTERLEUKIN-4 AGONISTS

The invention is directed to human IL-4 muteins numbered in accordance with wild-type IL-4 having T-cell activating activity, but having reduced endothelial cell activating activity. In particular, the invention is related to human IL-4 muteins wherein the surface-exposed residues of the D helix of the wild-type IL-4 are mutated whereby the resulting mutein causes T-cell proliferation, and causes reduced IL-6 secretion from HUVECs, relative to wild-type IL-4. This invention realizes a less toxic IL-4 mutant that allows greater therapeutic use of this interleukin. Further, the invention is directed to IL-4 muteins having single, double and triple mutations represented by the designators R121A, R121D, R121E, R121F, R121H, R121I, R121K, R121N, R121P, R121T, R121W; Y124A, Y124Q, Y124R, Y124S, Y124T; Y124A/S125A, T13D/R121E; and R121T/E122F/Y124Q, when numbered in accordance with wild-type IL-4 (His=1). The invention also includes polynucleotides coding for the muteins of the invention, vectors containing the polynucleotides, transformed host cells, pharmaceutical compositions comprising the muteins, and therapeutic methods of treatment.