L-Methionine, L-isoleucyl- is a dipeptide composed of the amino acids L-methionine and L-isoleucine. It is classified as a non-essential amino acid, which means that it can be synthesized by the body. This compound is characterized by its role in protein synthesis and its involvement in various metabolic processes. L-methionine serves as a precursor for other important biomolecules, including cysteine and taurine, and plays a crucial role in methylation reactions due to its sulfur-containing side chain. The presence of L-isoleucine contributes to the compound's hydrophobic characteristics, influencing its solubility and interaction with other biomolecules. L-Methionine, L-isoleucyl- is often studied for its potential benefits in nutrition and health, particularly in muscle metabolism and recovery. Additionally, it may have antioxidant properties, helping to protect cells from oxidative stress. As with many peptides, its stability and bioactivity can be influenced by factors such as pH and temperature, making it important to consider these conditions in experimental and therapeutic contexts.

L-Methionine, L-isoleucyl-

42384-14-5: L-Methionine, L-isoleucyl- is a dipeptide composed of the amino acids L-methionine and L-isoleucine. It is classified as a non-essential amino acid, which means that it can be synthesized by the body. This compound is characterized by its role in protein synthesis and its involvement in various metabolic processes. L-methionine serves as a precursor for other important biomolecules, including cysteine and taurine, and plays a crucial role in methylation reactions due to its sulfur-containing side chain. The presence of L-isoleucine contributes to the compound's hydrophobic characteristics, influencing its solubility and interaction with other biomolecules. L-Methionine, L-isoleucyl- is often studied for its potential benefits in nutrition and health, particularly in muscle metabolism and recovery. Additionally, it may have antioxidant properties, helping to protect cells from oxidative stress. As with many peptides, its stability and bioactivity can be influenced by factors such as pH and temperature, making it important to consider these conditions in experimental and therapeutic contexts.

H-Ile-Met-OH is a cytosolic protein that is found in the cytosolic domain of plant cells. H-Ile-Met-OH is an enzyme that catalyzes the conversion of HMBP to Met, which is an intermediate in the biosynthesis of methionine. The frequency and sequence of H-Ile-Met-OH has been analyzed in animals, plants, and fungi. Bioinformatics studies have shown that H-Ile-Met-OH has a vacuolar function, which can be seen by its sequence similarity to other vacuolar proteins.

CAS 42384-14-5

L-Methionine, L-isoleucyl-

H-Ile-Met-OH

Ref: 3D-FI108078