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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]
Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O − 2) anion radical into normal molecular oxygen (O 2) and hydrogen peroxide (H 2 O 2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. [2]
Ubiquitin-activating enzymes, also known as E1 enzymes, catalyze the first step in the ubiquitination reaction, which (among other things) can target a protein for degradation via a proteasome. This covalent bond of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic ...
This article needs attention from an expert in biochemistry.The specific problem is: someone with a solid grasp of the full scope of this subject and of its secondary and advanced teaching literatures needs to address A, the clear structural issues of the article (e.g., general absence of catabolic biosynthetic pathways, insertion of macromolecule anabolic paths before all building blocks ...
Nucleic acid thermodynamics is the study of how temperature affects the nucleic acid structure of double-stranded DNA (dsDNA). The melting temperature (T m) is defined as the temperature at which half of the DNA strands are in the random coil or single-stranded (ssDNA) state.
Two of the sites strongly bind Ca 2+ while the other two coordinate Mg 2+. Little has been published on the number and location of the Mg 2+ binding sites, although it has been proposed that Mg 2+ is located near the catalytic pocket and contributes to hydrolysis. [6] The two Ca 2+ are shown in red in the image. They are bound to DNase I under ...
Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...
Enzymes appear in this category according to the EC number classification: EC 1 Oxidoreductases: catalyze oxidation/reduction reactions; EC 2 Transferases: transfer a functional group (e.g. a methyl or phosphate group) EC 3 Hydrolases: catalyze the hydrolysis of various bonds; EC 4 Lyases: cleave various bonds by means other than hydrolysis and ...