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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]
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 are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a protein loop or unit of secondary structure, or even an entire protein domain.
Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...
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 ...
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]
The RM system was first discovered by Salvatore Luria and Mary Human in 1952 and 1953. [1] [2] They found that a bacteriophage growing within an infected bacterium could be modified, so that upon their release and re-infection of a related bacterium the bacteriophage's growth is restricted (inhibited; also described by Luria in his autobiography on pages 45 and 99 in 1984). [3]
The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme, [3] or between the interfaces of multimeric enzymes. An active site can catalyse a reaction repeatedly as residues are not altered at the end of the reaction (they may change during the reaction, but are regenerated by the end ...