Search results
Results from the WOW.Com Content Network
This linkage is an ester bond that chemically binds the carboxyl group of an amino acid to the terminal 3'-OH group of its cognate tRNA. [7] It has been discovered that the amino acid moiety of a given aa-tRNA provides for its structural integrity; the tRNA moiety dictates, for the most part, how and when the amino acid will be incorporated ...
Thioester containing protein 1, often called TEP1 is a key component of the arthropod innate immune system. TEP1 was first identified as a key immunity gene in 2001 through functional studies on Anopheles gambiae mosquitoes.
Acyl-protein thioesterases are enzymes that cleave off lipid modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. [1] Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad . [ 2 ]
Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase , which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid . [ 1 ]
Phosphatidylserine (PS) is the major acidic phospholipid class that accounts for 13–15% of the phospholipids in the human cerebral cortex. [7] In the plasma membrane, PS is localized exclusively in the cytoplasmic leaflet where it forms part of protein docking sites necessary for the activation of several key signaling pathways.
In biochemistry, an esterase is a class of enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis (and as such, it is a type of hydrolase).
Carboxylesterase 1 is a serine esterase and member of a large multigene carboxylesterase family. It is also part of the alpha/beta fold hydrolase family. [7] These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing xenobiotics and drugs such as cocaine and heroin.
Eventually, [these] thioesters could have served to usher in ATP through its ability to support the formation of bonds between phosphate groups. However, due to the high free energy change of thioester's hydrolysis and correspondingly their low equilibrium constants, it is unlikely that these compounds could have accumulated abiotically to any ...