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Pacifastin
Pacifastin is a family of serine proteinase inhibitors found in arthropods. Pacifastin inhibits the serine peptidases trypsin and chymotrypsin. All pacifastin members that have been characterized at the molecular level are precursor peptides composed of an N-terminal signal sequence followed by a precursor domain and a variable number of inhibitor domains. Each of these inhibitor domains carries a six-cysteine motif – see below. The first family members to be identified were isolated from ''Locusta migratoria migratoria'' ( migratory locust) which were HI, LMCI-1 (PMP-D2) and LMCI-2 (PMP-C). A further five members, SGPI-1 to 5, were then isolated from ''Schistocerca gregaria'' (desert locust), and a heterodimeric serine protease inhibitor was isolated from the haemolymph of ''Pacifastacus leniusculus'' (Signal crayfish), and named pacifastin. Function Peptide proteinase inhibitors are in many cases synthesised as part of a larger precursor protein, referred to as a propep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine Protease
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. Classification The MEROPS protease classification system counts 16 protein superfamily, superfamilies (as of 2013) each containing many protein family, families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For protein superfamily, superfamilies, P: superfamily, containing a mixture of nucleophile class families, S: purely serine proteases. superfamily. Within each superfamily, protein family, families are designated by their catalytic nucl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Signal Crayfish
The signal crayfish (''Pacifastacus leniusculus'') is a species of crayfish indigenous to North America. Introduced to Europe in the 1960s to supplement the North European ''Astacus astacus'' fisheries, which were being damaged by crayfish plague, it was subsequently discovered that the signal was itself a carrier of that disease. Consequently, the signal crayfish is now considered an invasive species across Europe, Japan, and California, having displaced the native species in these regions. Description and ecology Members of this species are typically long, although sizes up to are possible. A distinctive white to pale blue-green patch is present near the claw hinge, reminiscent of the white flags that signalmen used for directing trains—hence the species' common name. The Biological life cycle, lifecycle of the signal crayfish is typical for the family Astacidae. The mating season occurs in the autumn, during which time the female produces around 200 to 400 egg (biolog ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Insect
Insects (from Latin ') are Hexapoda, hexapod invertebrates of the class (biology), class Insecta. They are the largest group within the arthropod phylum. Insects have a chitinous exoskeleton, a three-part body (Insect morphology#Head, head, Thorax (insect anatomy), thorax and abdomen (insect anatomy), abdomen), three pairs of jointed Arthropod leg, legs, compound eyes, and a pair of antenna (biology), antennae. Insects are the most diverse group of animals, with more than a million described species; they represent more than half of all animal species. The insect nervous system consists of a insect brain, brain and a ventral nerve cord. Most insects reproduce Oviparous, by laying eggs. Insects Respiratory system of insects, breathe air through a system of Spiracle (arthropods), paired openings along their sides, connected to Trachea#Invertebrates, small tubes that take air directly to the tissues. The blood therefore does not carry oxygen; it is only partly contained in ves ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Physiology
Physiology (; ) is the science, scientific study of function (biology), functions and mechanism (biology), mechanisms in a life, living system. As a branches of science, subdiscipline of biology, physiology focuses on how organisms, organ systems, individual organ (biology), organs, cell (biology), cells, and biomolecules carry out chemistry, chemical and physics, physical functions in a living system. According to the classes of organisms, the field can be divided into clinical physiology, medical physiology, Zoology#Physiology, animal physiology, plant physiology, cell physiology, and comparative physiology. Central to physiological functioning are biophysics, biophysical and biochemical processes, homeostasis, homeostatic control mechanisms, and cell signaling, communication between cells. ''Physiological state'' is the condition of normal function. In contrast, ''pathology, pathological state'' refers to abnormality (behavior), abnormal conditions, including human diseases. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Immunity (medical)
In biology, immunity is the state of being insusceptible or resistant to a noxious agent or process, especially a pathogen or infectious disease. Immunity may occur naturally or be produced by prior exposure or immunization. Innate and adaptive The immune system has Innate immune system, innate and Adaptive immune system, adaptive components. Innate immunity is present in all metazoans, immune responses: inflammation, inflammatory responses and phagocytosis. The adaptive component, on the other hand, involves more advanced lymphocyte, lymphatic cells that can distinguish between specific "non-self" substances in the presence of "self". The reaction to foreign substances is etymologically described as inflammation while the non-reaction to self substances is described as immunity. The two components of the immune system create a dynamic biological environment where "health" can be seen as a physical state where the self is immunologically spared, and what is foreign is inflammat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endogenous
Endogeny, in biology, refers to the property of originating or developing from within an organism, tissue, or cell. For example, ''endogenous substances'', and ''endogenous processes'' are those that originate within a living system (e.g. an organism or a cell). For instance, estradiol is an endogenous estrogen hormone A hormone (from the Ancient Greek, Greek participle , "setting in motion") is a class of cell signaling, signaling molecules in multicellular organisms that are sent to distant organs or tissues by complex biological processes to regulate physio ... produced within the body, whereas ethinylestradiol is an exogenous synthetic estrogen, commonly used in birth control pills. In contrast, '' exogenous substances'' and ''exogenous'' ''processes'' are those that originate from outside of an organism. References External links *{{Wiktionary-inline, endogeny Biology ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bond Cleavage
In chemistry, bond cleavage, or bond fission, is the splitting of chemical bonds. This can be generally referred to as dissociation when a molecule is cleaved into two or more fragments. In general, there are two classifications for bond cleavage: ''homo''lytic and ''hetero''lytic, depending on the nature of the process. The triplet and singlet excitation energies of a sigma bond can be used to determine if a bond will follow the homolytic or heterolytic pathway. A metal−metal sigma bond is an exception because the bond's excitation energy is extremely high, thus cannot be used for observation purposes. In some cases, bond cleavage requires catalysts. Due to the high bond-dissociation energy of C−H bonds, around , a large amount of energy is required to cleave the hydrogen atom from the carbon and bond a different atom to the carbon. Homolytic cleavage In homolytic cleavage, or homolysis, the two electrons in a cleaved covalent bond are divided equally betwee ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Autocatalytic
In chemistry, a chemical reaction is said to be autocatalytic if one of the reaction products is also a catalyst for the same reaction. Many forms of autocatalysis are recognized.Steinfeld J.I., Francisco J.S. and Hase W.L. ''Chemical Kinetics and Dynamics'' (2nd ed., Prentice-Hall 1999) pp. 151–2 A ''set'' of chemical reactions can be said to be "collectively autocatalytic" if a number of those reactions produce, as reaction products, catalysts for enough of the other reactions that the entire set of chemical reactions is self-sustaining given an input of energy and food molecules (see autocatalytic set). Examples Acid-catalyzed hydrolysis of esters produces carboxylic acids that also catalyze the same reaction. Indeed, the observation of an accelerating hydrolysis of gamma valerolactone to gamma-hydroxyvaleric acid led to the introduction of the concept of autocatalysis in 1890. The oxidation of hydrocarbons by air or oxygen is the basis of autoxidation. Like many radic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Active Site
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the ''binding site'', and residues that catalyse a reaction of that substrate, the ''catalytic site''. Although the active site occupies only ~10–20% of the volume of an enzyme, it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes. Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their functio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme Substrate
In chemistry, the term substrate is highly context-dependent. Broadly speaking, it can refer either to a chemical species being observed in a chemical reaction, or to a surface on which other chemical reactions or microscopy are performed. In the former sense, a reagent is added to the ''substrate'' to generate a product through a chemical reaction. The term is used in a similar sense in synthetic and organic chemistry, where the substrate is the chemical of interest that is being modified. In biochemistry, an enzyme substrate is the material upon which an enzyme acts. When referring to Le Chatelier's principle, the substrate is the reagent whose concentration is changed. ;Spontaneous reaction : :*Where S is substrate and P is product. ;Catalysed reaction : :*Where S is substrate, P is product and C is catalyst. In the latter sense, it may refer to a surface on which other chemical reactions are performed or play a supporting role in a variety of spectroscopic and micro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lysosome
A lysosome () is a membrane-bound organelle that is found in all mammalian cells, with the exception of red blood cells (erythrocytes). There are normally hundreds of lysosomes in the cytosol, where they function as the cell’s degradation center. Their primary responsibility is catabolic degradation of proteins, polysaccharides and lipids into their respective building-block molecules: amino acids, monosaccharides, and free fatty acids. The breakdown is done by various enzymes, for example proteases, glycosidases and lipases. With an acidic lumen limited by a single-bilayer lipid membrane, the lysosome holds an environment isolated from the rest of the cell. The lower pH creates optimal conditions for the over 60 different Hydrolase, hydrolases inside. Lysosomes receive extracellular particles through endocytosis, and intracellular components through autophagy. They can also fuse with the plasma membrane and secrete their contents, a process called lysosomal exocytosis. After ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Zymogen
In biochemistry, a zymogen (), also called a proenzyme (), is an inactive precursor of an enzyme. A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) to become an active enzyme. The biochemical change usually occurs in Golgi bodies, where a specific part of the precursor enzyme is cleaved in order to activate it. The inactivating piece which is cleaved off can be a peptide unit, or can be independently-folding domains comprising more than 100 residues. Although they limit the enzyme's ability, these N-terminal extensions of the enzyme or a "prosegment" often aid in the stabilization and folding of the enzyme they inhibit. The pancreas secretes zymogens partly to prevent the enzymes from digesting proteins in the cells where they are synthesised. Enzymes like pepsin are created in the form of pepsinogen, an inactive zymogen. Pepsinogen is activated when chief cells release ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
