5250-25-9

Basic information

• Product Name: 1H-Tetrazole-5-aceticacid, 1-methyl-, ethyl ester
• Synonyms: NSC 138011
• CAS NO: 5250-25-9
• Molecular Formula: C₆H₁₀N₄O₂
• Molecular Weight: 170.1692
• Mol File: 5250-25-9.mol
• Article Data: 7

Chemical Properties

• Boiling Point: 342.6°Cat760mmHg
• Flash Point: 161°C
• Density: 1.33g/cm³
• CAS DataBase Reference: 1H-Tetrazole-5-aceticacid, 1-methyl-, ethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: 1H-Tetrazole-5-aceticacid, 1-methyl-, ethyl ester(5250-25-9)
• EPA Substance Registry System: 1H-Tetrazole-5-aceticacid, 1-methyl-, ethyl ester(5250-25-9)

Safety Data

• Hazardous Substances Data: 5250-25-9(Hazardous Substances Data)

Usage

Chemical structure

1H-Tetrazole-5-aceticacid, 1-methyl-, ethyl ester is a heterocyclic compound with a tetrazole ring fused to an acetic acid chain and a methyl group attached to the nitrogen atom. The ethyl ester group is also attached to the carboxylic acid moiety.

Molecular weight

140.14 g/mol

Appearance

White or off-white crystalline solid

Solubility

Slightly soluble in water, soluble in common organic solvents such as ethanol, methanol, and acetone.

Stability

Stable under normal conditions, but may decompose upon heating or exposure to strong acids or bases.

Reactivity

1H-Tetrazole-5-aceticacid, 1-methyl-, ethyl ester can undergo various chemical reactions, such as ester hydrolysis, amide formation, and substitution reactions.

Uses

Commonly used as a starting material in the synthesis of pharmaceuticals, agrochemicals, and specialty chemicals. It is also used as an intermediate in organic synthesis and as a building block in the production of various functional materials.

Biological activity

Has potential applications in the field of medicinal chemistry and drug discovery due to its ability to modulate biological activity.

Other potential properties

Has been studied for its potential properties as a corrosion inhibitor and as a catalyst in chemical reactions.

Upstream product

• 5144-11-6 1,5-dimethyl-1H-tetrazole 
• 541-41-3 chloroformic acid ethyl ester 
• 13616-37-0 ethyl (tetrazol-5-yl)acetate 
• 74-88-4 methyl iodide 
• 87-13-8 diethyl 2-ethoxymethylenemalonate 
• 25724-83-8 ethyl 2-methyl-5-oxo-2,5-dihydroisoxazole-4-carboxylate 

Downstream Products

• 118875-20-0 ethyl 3,3-bis(4-fluorophenyl)-2-(1-methyl-1H-tetrazol-5-yl)-2-propenoate 

Relevant articles and documents

-

-

Substituted enaminones, their derivatives and uses thereof

The present invention is related substituted enaminones represented by a compound of Formula I that are novel allosteric modulators of α7 nAChRs. The invention also discloses the treatment of disorders that are responsive to enhancement of acetylcholine a

Synthesis, biological profile, and quantitative structure - Activity relationship of a series of novel 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors

A series of 9,9-bis(4-fluorophenyl)-3,5-dihydroxy-8-(alkyltetrazol-5-yl)-6,8-nonad ienoic acid derivatives 1 were synthesized and found to inhibit competitively the enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase. The analogues having 1N-methyltetrazol-5-yl attached to the C8-position (3a, 4a, R1 = R2 = F) are the most active in suppressing cholesterol biosynthesis in both in vitro and in vivo models: the IC50 for the chiral form of 3a is 19 nM, K(i) = 4.3 x 10-9 M when K(m) for HMG-CoA is 28 x 10-6 M; the ED50 (oral) value corresponding to the lactone derivative (4a, BMY 22089) is approximately 0.1 mg/kg. Further, BMY 21950 is nearly 2 orders of magnitude more active in parenchymal hepatocytes, from which most of the serum cholesterol originates, than in other cell preparations (such as spleen, testes, ileum, adrenal, and ocular lens epithelial cells; Table III). This apparent tissue specificity may be highly beneficial since the blocking of cholesterol biosynthesis in other vital organs could eventually lead to undesirable side effects. In addition to the chemical synthesis and biological evaluation, a theoretical study aimed at relating the HMG-CoA reductase inhibitory potency to the three-dimensional structure of the inhibitors was undertaken. With a combination of molecular mapping and 3D-QSAR techniques, it was possible to determine a logical candidate for the conformation of the bound inhibitor and to quantitatively relate inhibitory potency to the shape and size of both the binding site and the C8-substituent.