Acylase I is a hydrolase enzyme that plays an important part in the metabolism of a variety of chemical molecules. It hydrolyzes acyl groups from a variety of substrates, including acyl-amino acids, acyl esters, and amides.
Acylase I’s principal purpose is to cleave the acyl group off its substrate, resulting in the creation of an amine and a carboxylic acid. This enzyme activity is required for many biochemical pathways, including the degradation of natural and manufactured chemicals in living organisms.
Acylase I’s substrate specificity enables it to target a wide variety of acyl molecules, making it a significant tool in the pharmaceutical and chemical sectors. Acylase I is used to
Acylase I is involved in environmental bioremediation in addition to its applications in chemical synthesis. It contributes to the detoxification and elimination of environmental toxins by assisting in the breakdown of certain pollutants and hazardous chemicals that contain acyl groups.
Acylase I’s catalytic activity is controlled by a variety of variables, including pH, temperature, and the presence of particular cofactors. The optimal conditions for its activity are determined by the organism or source from which the enzyme is produced.
Acylase I is a versatile enzyme that catalyzes the hydrolysis of acyl groups from a variety of substrates. Because of its substrate selectivity and enzymatic activity, it is useful in chemical synthesis, pharmaceutical manufacturing, and environmental cleanup. The investigation of Acylase I’s capabilities and its applications
Acylase I is a catalytic enzyme that catalyzes the hydrolysis of N-acyl-L-amino acids into L-amino acids and fatty acids. This enzyme is found in a variety of organisms, including bacteria, fungi, and mammals, and it is important in the metabolism of nitrogen-containing compounds. Acylase I degrades a variety of N-acyl-L-amino acids, including N-acyl derivatives of alanine, leucine, phenylalanine, and tryptophan. The activity of the enzyme is greatest at neutral pH and is dependent on the presence of divalent metal ions such as zinc, cobalt, or nickel. Acylase I is found primarily in the liver and kidneys of mammals and is responsible for the metabolism of N-acylated amino acids derived from protein breakdown. Certain drugs, such as valproic acid, which is used to treat epilepsy and bipolar disorder, can also stimulate enzyme activity. Acylase I is essential in the degradation of xenobiotic compounds such as herbicides and pesticides in bacteria. The activity of the enzyme has been harnessed for biotechnological applications such as bioremediation of contaminated soil and water. Acylase I has also been investigated for possible therapeutic applications. According to research, the enzyme can be used to synthesize enantiomerically pure L-amino acids, which are required for the production of pharmaceuticals, food additives, and agrochemicals. Furthermore, because Acylase I is required for bacterial growth and survival, it has been investigated as a target for the development of novel antibiotics.
Related Products
Product Categories
Explore
Get In Touch
- Horizon Flora, Office No. 2A & 2B First Floor, Ghodbunder Road, Bhayandarpada, Thane, Mumbai – 400615
- +91 9158047802
- support@biolaxienzymes.com