Search results
Results from the WOW.Com Content Network
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
The two enzymes have similar folding patterns and protein domains. In fact, past attempts to produce drugs targeting glucansucrase have not been successful because the drugs also disrupted amylase, which is necessary to break down starches. [12] [13] This occurred because the active sites of the two enzymes are nearly the same. Glucansucrase ...
First, glucose metabolism is faster through ethanol fermentation because it involves fewer enzymes and limits all reactions to the cytoplasm. Second, ethanol has bactericidal activity by causing damage to the cell membrane and protein denaturing , allowing yeast fungus to outcompete environmental bacteria for resources. [ 6 ]
Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human body. These intermediates must be ingested, mostly from eating other organisms. [6]
Glucose-6-phosphate dehydrogenase is the rate-controlling enzyme of this pathway [citation needed]. It is allosterically stimulated by NADP + and strongly inhibited by NADPH. [7] The ratio of NADPH:NADP + is the primary mode of regulation for the enzyme and is normally about 100:1 in liver cytosol [citation needed]. This makes the cytosol a ...
Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids.This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism).
β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. [1] [2] Alternative names for β-fructofuranosidase EC 3.2.1.26 include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase.
It is a spontaneous reaction and a type of post-translational modification of proteins meaning it alters their structure and biological activity. It is the covalent attachment between the carbonil group of a reducing sugar (mainly glucose and fructose) and the amino acid side chain of the protein. In this process the intervention of an enzyme ...