37462-92-3 Usage
Description
H-ILE-PRO-OH, with the molecular formula C11H21NO3, is a unique chemical compound composed of the amino acids isoleucine (ILE) and proline (PRO), along with a hydroxyl group (OH). Isoleucine, an essential amino acid, is crucial for protein synthesis and muscle metabolism, while proline, a non-essential amino acid, is vital for collagen production and maintaining healthy connective tissues. The hydroxyl group contributes a hydrophilic characteristic to the molecule, enhancing its water solubility. The synergistic effect of these components makes H-ILE-PRO-OH essential for a range of physiological processes, including muscle growth and repair, connective tissue maintenance, and overall health.
Uses
Used in Pharmaceutical Industry:
H-ILE-PRO-OH is used as a therapeutic agent for promoting muscle growth and repair due to its role in protein synthesis and muscle metabolism. The presence of isoleucine, an essential amino acid, makes it a valuable component in treatments targeting muscle health and recovery.
Used in Nutritional Supplements:
H-ILE-PRO-OH is used as a dietary supplement to support overall health and well-being. Its composition of essential and non-essential amino acids contributes to the maintenance of healthy connective tissues and the promotion of muscle metabolism, making it a beneficial addition to nutritional programs.
Used in Cosmetics and Skincare:
H-ILE-PRO-OH is used as an ingredient in cosmetic and skincare products for its potential role in collagen production and connective tissue health. The hydroxyl group's hydrophilic property may also contribute to the improved hydration and overall health of the skin.
Used in Research and Development:
H-ILE-PRO-OH serves as a valuable compound in scientific research, particularly in the fields of biochemistry and physiology. Its unique composition allows researchers to study the effects of specific amino acids on various biological processes, such as muscle metabolism and connective tissue maintenance.
Check Digit Verification of cas no
The CAS Registry Mumber 37462-92-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,7,4,6 and 2 respectively; the second part has 2 digits, 9 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 37462-92:
(7*3)+(6*7)+(5*4)+(4*6)+(3*2)+(2*9)+(1*2)=133
133 % 10 = 3
So 37462-92-3 is a valid CAS Registry Number.
37462-92-3Relevant articles and documents
Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily
Xiang, Dao Feng,Patskovsky, Yury,Xu, Chengfu,Fedorov, Alexander A.,Fedorov, Elena V.,Sisco, Abby A.,Sauder, J. Michael,Burley, Stephen K.,Almo, Steven C.,Raushel, Frank M.
experimental part, p. 6791 - 6803 (2011/05/05)
Two uncharacterized enzymes from the amidohydrolase superfamily belonging to cog1228 were cloned, expressed, and purified to homogeneity. The two proteins, Sgx9260c (gi|44242006) and Sgx9260b (gi|44479596), were derived from environmental DNA samples originating from the Sargasso Sea. The catalytic function and substrate profiles for Sgx9260c and Sgx9260b were determined using a comprehensive library of dipeptides and N-acyl derivative of l-amino acids. Sgx9260c catalyzes the hydrolysis of Gly-l-Pro, l-Ala-l-Pro, and N-acyl derivatives of l-Pro. The best substrate identified to date is N-acetyl-l-Pro with a value of kcat/Km of 3 × 105 M -1 s-1. Sgx9260b catalyzes the hydrolysis of l-hydrophobic l-Pro dipeptides and N-acyl derivatives of l-Pro. The best substrate identified to date is N-propionyl-l-Pro with a value of kcat/Km of 1 × 105 M-1 s-1. Three-dimensional structures of both proteins were determined by X-ray diffraction methods (PDB codes 3MKV and 3FEQ). These proteins fold as distorted (β/α) 8-barrels with two divalent cations in the active site. The structure of Sgx9260c was also determined as a complex with the N-methylphosphonate derivative of l-Pro (PDB code 3N2C). In this structure the phosphonate moiety bridges the binuclear metal center, and one oxygen atom interacts with His-140. The α-carboxylate of the inhibitor interacts with Tyr-231. The proline side chain occupies a small substrate binding cavity formed by residues contributed from the loop that follows β-strand 7 within the (β/α)8-barrel. A total of 38 other proteins from cog1228 are predicted to have the same substrate profile based on conservation of the substrate binding residues. The structure of an evolutionarily related protein, Cc2672 from Caulobacter crecentus, was determined as a complex with the N-methylphosphonate derivative of l-arginine (PDB code 3MTW).
