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Kallikrein 13
Kallikrein 13 (, '' KLK13'', ''kallikrein mK13'', ''mGK-13'', ''mK13'', ''mKLK13'', ''prorenin converting enzyme 1'', ''PRECE-1'', ''prorenin-converting enzyme'', ''PRECE'', ''proteinase P'') is an enzyme. This enzyme catalyses hydrolyses mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg- pair in the N-terminus, to yield mature renin Renin ( etymology and pronunciation), also known as an angiotensinogenase, is an aspartic protease protein and enzyme secreted by the kidneys that participates in the body's renin-angiotensin-aldosterone system (RAAS)—also known as the reni .... This enzyme belongs in peptidase family S1A. References External links * {{Portal bar, Biology, border=no EC 3.4.21 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KLK13
Kallikrein-13 is a protein that in humans is encoded by the ''KLK13'' gene. Function Kallikreins are a subgroup of serine proteases having diverse physiological functions. As of 2022, the precise physiological functions of Kallikrein 13 remain unknown. It may play a role in the defense of the upper digestive apparatus, in extracellular matrix degradation, in tissue remodelling, and in the male reproductive organs. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Expression of this gene is regulated by steroid hormones and may be useful as a marker for breast cancer. An additional transcript variant has been identified, but its full length sequence has not been determined. Kallikrein-13 serves as a priming protease during infection by the human coronavirus HKU1. Many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. References Further reading * * * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Catalysis
Catalysis () is the increase in rate of a chemical reaction due to an added substance known as a catalyst (). Catalysts are not consumed by the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. The rate increase occurs because the catalyst allows the reaction to occur by an alternative mechanism which may be much faster than the noncatalyzed mechanism. However the noncatalyzed mechanism does remain possible, so that the total rate (catalyzed plus noncatalyzed) can only increase in the presence of the catalyst and never decrease. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usual ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrolyse
Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution, elimination, and solvation reactions in which water is the nucleophile. Biological hydrolysis is the cleavage of biomolecules where a water molecule is consumed to effect the separation of a larger molecule into component parts. When a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g., sucrose being broken down into glucose and fructose), this is recognized as saccharification. Hydrolysis reactions can be the reverse of a condensation reaction in which two molecules join into a larger one and eject a water molecule. Thus hydrolysis adds water to break down, whereas condensation builds up by removing water. Types Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both the substance and water molecule to split into two parts. In ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prorenin
Prorenin () is a protein that constitutes a precursor for renin, the hormone that activates the renin–angiotensin system, which serves to raise blood pressure. Prorenin is converted into renin by the juxtaglomerular cells, which are specialised smooth muscle cells present mainly in the afferent, but also the efferent, arterioles of the glomerular capillary bed. Prorenin is a relatively large molecule, weighing approximately 46 KDa. History Prorenin was discovered by Eugenie Lumbers in 1971. Synthesis In addition to juxtaglomerular cells, prorenin is also synthesised by other organs, such as the adrenal glands, the ovaries, the testis and the pituitary gland, which is why it is found in the plasma of anephric individuals. Concentration Blood concentration levels of prorenin are between 5 and 10 times higher than those of renin. There is evidence to suggest that, in diabetes mellitus, prorenin levels are even higher. One study using relatively newer technology found that blood ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Submandibular Gland
The paired submandibular glands (historically known as submaxillary glands) are major salivary glands located beneath the floor of the mouth. In adult humans, they each weigh about 15 grams and contribute some 60–67% of unstimulated saliva secretion; on stimulation their contribution decreases in proportion as parotid gland secretion rises to 50%. The average length of the normal adult human submandibular salivary gland is approximately 27 mm, while the average width is approximately 14.3 mm. Structure Each submandibular gland is divided into a superficial lobe and a deep lobe, the two being separated by the mylohyoid muscle: * The superficial lobe comprises most of the gland, with the mylohyoid muscle runs under it * The deep lobe is the smaller part Submandibular duct Secretions are delivered into the submandibular duct on the deep portion after which they hook around the posterior edge of the mylohyoid muscle and proceed on the superior surface laterally. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidinium, guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is Genetic code, encoded by the DNA codon table, codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the Precursor (chemistry), precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. The one-letter symbol R was assigned to arginine for its phonetic similarity. History Arginine was first isolated in 1886 from Lupinus luteus, yellow lupin seedlings by the German chemist Ernst Schulze (chemist), Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Renin
Renin ( etymology and pronunciation), also known as an angiotensinogenase, is an aspartic protease protein and enzyme secreted by the kidneys that participates in the body's renin-angiotensin-aldosterone system (RAAS)—also known as the renin-angiotensin-aldosterone axis—that increases the volume of extracellular fluid (blood plasma, lymph, and interstitial fluid) and causes arterial vasoconstriction. Thus, it increases the body's mean arterial blood pressure. Renin is not commonly referred to as a hormone, although it has a receptor, the (pro)renin receptor, also known as the renin receptor and prorenin receptor (see also below), as well as enzymatic activity with which it hydrolyzes angiotensinogen to angiotensin I. Biochemistry and physiology Structure The primary structure of renin precursor consists of 406 amino acids with a pre- and a pro-segment carrying 20 and 46 amino acids, respectively. Mature renin contains 340 amino acids and has a mass of 37 kDa. Secr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
