Peptidase S
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Peptidase S
Leucyl aminopeptidases (, ''leucine aminopeptidase'', ''LAPs'', ''leucyl peptidase'', ''peptidase S'', ''cytosol aminopeptidase'', ''cathepsin III'', ''L-leucine aminopeptidase'', ''leucinaminopeptidase'', ''leucinamide aminopeptidase'', ''FTBL proteins'', ''proteinates FTBL'', ''aminopeptidase II'', ''aminopeptidase III'', ''aminopeptidase I'') are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, ''Escherichia coli'' ('' E. coli'') LAP (also known as PepA or XerB), and the solanaceous-specific acidic LAP (LAP-A) in tomato (''Solanum lycopersicum''). Enzyme description, structure, and active site The active sites in PepA and in bovine lens LAP have been found to be similar. Shown in the picture below is the proposed model for the active site of LA ...
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Enzymes
Enzymes () are proteins that act as biological catalysts 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 are Ribozyme, catalytic RNA molecules, called ribozymes. Enzymes' Chemical specificity, specific ...
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Biochemistry
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Voet (2005), p. 3. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells,Karp (2009), p. 2. in turn relating greatly to the understanding of tissues and organs, as well as organism structure and function.Miller (2012). p. 62. Biochemistry is closely related to molecular biology, which is the study of the molecular mechanisms of biological phenomena.As ...
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Endopeptidase
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. They are usually very specific for certain amino acids. Examples of endopeptidases include: * Trypsin - cuts after Arg or Lys, unless followed by Pro. Very strict. Works best at pH 8. * Chymotrypsin - cuts after Phe, Trp, or Tyr, unless followed by Pro. Cuts more slowly after His, Met or Leu. Works best at pH 8. * Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro. * Thermolysin - cuts ''before'' Ile, Met, Phe, Trp, Tyr, or Val, unless ''preceded'' by Pro. Sometimes cuts after Ala, Asp ...
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Carboxypeptidase
A carboxypeptidase ( EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. At least two mechanisms have been discussed. Functions Initial studies on carboxypeptidases focused on pancreatic carboxypeptidases A1, A2, and B in the digestion of food. Most carboxypeptidases are not, however, involved in catabolism. Instead they help to mature proteins, for example Post-translational modification. They also regulate biological processes, such as the biosynthesis of neuroendocrine peptides such as insulin requires a carboxypeptidase. Carboxypeptidases also function in blood clotting, growth factor production, wound healing, reproduction, ...
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Reaction Mechanism
In chemistry, a reaction mechanism is the step by step sequence of elementary reactions by which overall chemical change occurs. A chemical mechanism is a theoretical conjecture that tries to describe in detail what takes place at each stage of an overall chemical reaction. The detailed steps of a reaction are not observable in most cases. The conjectured mechanism is chosen because it is thermodynamically feasible, and has experimental support in isolated intermediates (see next section) or other quantitative and qualitative characteristics of the reaction. It also describes each reactive intermediate, activated complex, and transition state, and which bonds are broken (and in what order), and which bonds are formed (and in what order). A complete mechanism must also explain the reason for the reactants and catalyst used, the stereochemistry observed in reactants and products, all products formed and the amount of each. The electron or arrow pushing method is often used in i ...
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FEBS Letters
''FEBS Letters'' is a not-for-profit peer-reviewed scientific journal published on behalf of the Federation of European Biochemical Societies (FEBS) by Wiley. It covers all aspects of molecular biosciences, including molecular biology and biochemistry. The aim of the journal is to publish primary research in the form of Research Articles, Research Letters, Communications and Hypotheses, as well as secondary research in the form of Review articles. The journal also publishes a News and Views column calle"The Scientists' Forum" The editorial office of ''FEBS Letters'' is based in Heidelberg, Germany. The journal income is reinvested in science. History The initial idea of ''FEBS Letters'' as a journal for rapid communication of short reports in biochemistry, biophysics and molecular biology was proposed by the Secretary General of FEBS, W.J. Whelan, at the 4th FEBS Meeting held in Oslo in 1967. After further discussions and preparations, the first issue of ''FEBS Letters'' appeare ...
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Protomer
In structural biology, a protomer is the structural unit of an oligomeric protein. It is the smallest unit composed of at least two different protein chains that form a larger hetero-oligomer by association of two or more copies of this unit. The term was introduced by Chetverin to make nomenclature in the Na/K-ATPase enzyme unambiguous. This enzyme is composed of two subunits: a large, catalytic α subunit, and a smaller glycoprotein β subunit (plus a proteolipid, called γ-subunit). At the time it was unclear how many of each work together. In addition, when people spoke of a dimer, it was unclear whether they were referring to αβ or to (αβ)2. Chetverin suggested to call αβ a protomer and (αβ)2 a diprotomer. Protomers usually arrange in cyclic symmetry to form closed point group symmetries. In chemistry, a so-called protomer is a molecule which displays tautomerism due to position of a proton. Examples Hemoglobin is a heterotetramer consisting of four subunits (two α ...
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In Vivo
Studies that are ''in vivo'' (Latin for "within the living"; often not italicized in English) are those in which the effects of various biological entities are tested on whole, living organisms or cells, usually animals, including humans, and plants, as opposed to a tissue extract or dead organism. This is not to be confused with experiments done ''in vitro'' ("within the glass"), i.e., in a laboratory environment using test tubes, Petri dishes, etc. Examples of investigations ''in vivo'' include: the pathogenesis of disease by comparing the effects of bacterial infection with the effects of purified bacterial toxins; the development of non-antibiotics, antiviral drugs, and new drugs generally; and new surgical procedures. Consequently, animal testing and clinical trials are major elements of ''in vivo'' research. ''In vivo'' testing is often employed over ''in vitro'' because it is better suited for observing the overall effects of an experiment on a living subject. In dr ...
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Hexamer
In chemistry and biochemistry, an oligomer () is a molecule that consists of a few repeating units which could be derived, actually or conceptually, from smaller molecules, monomers.Quote: ''Oligomer molecule: A molecule of intermediate relative molecular mass, the structure of which essentially comprises a small plurality of units derived, actually or conceptually, from molecules of lower relative molecular mass.'' The name is composed of Greek elements '' oligo-'', "a few" and '' -mer'', "parts". An adjective form is ''oligomeric''. The oligomer concept is contrasted to that of a polymer, which is usually understood to have a large number of units, possibly thousands or millions. However, there is no sharp distinction between these two concepts. One proposed criterion is whether the molecule's properties vary significantly with the removal of one or a few of the units. An oligomer with a specific number of units is referred to by the Greek prefix denoting that number, wit ...
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Temperature
Temperature is a physical quantity that expresses quantitatively the perceptions of hotness and coldness. Temperature is measured with a thermometer. Thermometers are calibrated in various temperature scales that historically have relied on various reference points and thermometric substances for definition. The most common scales are the Celsius scale with the unit symbol °C (formerly called ''centigrade''), the Fahrenheit scale (°F), and the Kelvin scale (K), the latter being used predominantly for scientific purposes. The kelvin is one of the seven base units in the International System of Units (SI). Absolute zero, i.e., zero kelvin or −273.15 °C, is the lowest point in the thermodynamic temperature scale. Experimentally, it can be approached very closely but not actually reached, as recognized in the third law of thermodynamics. It would be impossible to extract energy as heat from a body at that temperature. Temperature is important in all fields of natur ...
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Metal
A metal (from Greek μέταλλον ''métallon'', "mine, quarry, metal") is a material that, when freshly prepared, polished, or fractured, shows a lustrous appearance, and conducts electricity and heat relatively well. Metals are typically ductile (can be drawn into wires) and malleable (they can be hammered into thin sheets). These properties are the result of the ''metallic bond'' between the atoms or molecules of the metal. A metal may be a chemical element such as iron; an alloy such as stainless steel; or a molecular compound such as polymeric sulfur nitride. In physics, a metal is generally regarded as any substance capable of conducting electricity at a temperature of absolute zero. Many elements and compounds that are not normally classified as metals become metallic under high pressures. For example, the nonmetal iodine gradually becomes a metal at a pressure of between 40 and 170 thousand times atmospheric pressure. Equally, some materials regarded as metals ...
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Divalent
In chemistry, the valence (US spelling) or valency (British spelling) of an element is the measure of its combining capacity with other atoms when it forms chemical compounds or molecules. Description The combining capacity, or affinity of an atom of a given element is determined by the number of hydrogen atoms that it combines with. In methane, carbon has a valence of 4; in ammonia, nitrogen has a valence of 3; in water, oxygen has a valence of 2; and in hydrogen chloride, chlorine has a valence of 1. Chlorine, as it has a valence of one, can be substituted for hydrogen. Phosphorus has a valence of 5 in phosphorus pentachloride, . Valence diagrams of a compound represent the connectivity of the elements, with lines drawn between two elements, sometimes called bonds, representing a saturated valency for each element. The two tables below show some examples of different compounds, their valence diagrams, and the valences for each element of the compound. Modern definitions ...
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