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Substrate Promiscuity
Enzyme promiscuity is the ability of an enzyme to catalyze an unexpected side reaction in addition to its main reaction. Although enzymes are remarkably specific catalysts, they can often perform side reactions in addition to their main, native catalytic activity. These wild activities are usually slow relative to the main activity and are under neutral selection. Despite ordinarily being physiologically irrelevant, under new selective pressures, these activities may confer a fitness benefit therefore prompting the evolution of the formerly promiscuous activity to become the new main activity. An example of this is the atrazine chlorohydrolase (''atzA'' encoded) from '' Pseudomonas sp.'' ADP evolved from melamine deaminase (''triA'' encoded), which has very small promiscuous activity toward atrazine, a man-made chemical. Introduction Enzymes are evolved to catalyze a particular reaction on a particular substrate with high catalytic efficiency (''kcat/KM'', ''cf''. Michaelis–Mente ... [...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] |
Last Universal Common Ancestor
The last universal common ancestor (LUCA) is the hypothesized common ancestral cell from which the three domains of life, the Bacteria, the Archaea, and the Eukarya originated. The cell had a lipid bilayer; it possessed the genetic code and ribosomes which translated from DNA or RNA to proteins. Although the timing of the LUCA is not able to be definitively constrained, most studies suggest that the LUCA existed by or prior to 3.5 billion years ago, and possibly as early as 4.3 billion years ago or earlier. The nature of this point or stage of divergence remains a topic of research. All earlier forms of life preceding this divergence and all extant organisms are generally thought to share common ancestry. On the basis of a formal statistical test, this theory of a universal common ancestry (UCA) is supported versus competing multiple-ancestry hypotheses. The first universal common ancestor (FUCA) is a hypothetical non-cellular ancestor to LUCA and other now-extinct s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transaminase
Transaminases or aminotransferases are enzymes that catalyze a transamination reaction between an amino acid and an α-keto acid. They are important in the synthesis of amino acids, which form proteins. Function and mechanism An amino acid contains an amino (NH2) group. A keto acid contains a ketone, keto (=O) group. In transamination, the NH2 group on one molecule is exchanged with the =O group on the other molecule. The amino acid becomes a keto acid, and the keto acid becomes an amino acid. Transaminases require the coenzyme pyridoxal phosphate, which is converted into pyridoxamine in the first half-reaction, when an amino acid is converted into a keto acid. Enzyme-bound pyridoxamine in turn reacts with pyruvate, oxaloacetate, or alpha-ketoglutarate, giving alanine, aspartic acid, or glutamic acid, respectively. Many transamination reactions occur in tissues, catalysed by transaminases specific for a particular amino/keto acid pair. The reactions are readily reversible, the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rational Design
In chemical biology and biomolecular engineering, rational design (RD) is an umbrella term which invites the strategy of creating new molecules with a certain functionality, based upon the ability to predict how the molecule's structure (specifically derived from structural motif, motifs) will affect its behavior through physical models. This can be done either from scratch or by making mathematical model, calculated variations on a known structure, and usually complements directed evolution. Applications As an example, rational design is used to decipher collagen stability, mapping ligand-receptor interactions, unveiling protein folding and dynamics, and creating extra-biological structures by using fluorinated amino acids. To treat cancer, rational design is used for targeted therapies where proteins are engineered to modify the communication of cells with their environment. There is also the rational design of alfa-alkyl auxin molecules, which are auxin analogs capable of bi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biocatalysis
Biocatalysis refers to the use of living (biological) systems or their parts to speed up ( catalyze) chemical reactions. In biocatalytic processes, natural catalysts, such as enzymes, perform chemical transformations on organic compounds. Both enzymes that have been more or less isolated and enzymes still residing inside living cells are employed for this task. Modern biotechnology, specifically directed evolution, has made the production of modified or non-natural enzymes possible. This has enabled the development of enzymes that can catalyze novel small molecule transformations that may be difficult or impossible using classical synthetic organic chemistry. Utilizing natural or modified enzymes to perform organic synthesis is termed chemoenzymatic synthesis; the reactions performed by the enzyme are classified as chemoenzymatic reactions. History Biocatalysis underpins some of the oldest chemical transformations known to humans, for brewing predates recorded history. The old ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Secondary Metabolites
Secondary metabolites, also called ''specialised metabolites'', ''secondary products'', or ''natural products'', are organic compounds produced by any lifeform, e.g. bacteria, archaea, fungi, animals, or plants, which are not directly involved in the normal growth, development, or reproduction of the organism. Instead, they generally mediate ecological interactions, which may produce a selective advantage for the organism by increasing its survivability or fecundity. Specific secondary metabolites are often restricted to a narrow set of species within a phylogenetic group. Secondary metabolites often play an important role in plant defense against herbivory and other interspecies defenses. Humans use secondary metabolites as medicines, flavourings, pigments, and recreational drugs. The term secondary metabolite was first coined by Albrecht Kossel, the 1910 Nobel Prize laureate for medicine and physiology. 30 years later a Polish botanist Friedrich Czapek described secondary ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Delphinidin
Delphinidin (also delphinidine) is an anthocyanidin, a primary plant pigment, and also an antioxidant. Delphinidin gives blue hues to flowers in the genera ''Viola'' and ''Delphinium''. It also gives the blue-red color of the grape variety Cabernet Sauvignon, and can be found in cranberries and Concord grapes as well as pomegranates, and bilberries. Delphinidin, like nearly all other anthocyanidins, is pH-sensitive, i.e. a natural pH indicator, and changes from blue in basic solution to red in acidic solution. Glycosides Several glycosides derived from delphinidin are known: * Myrtillin (delphinidin-3-''O''-glucoside) and tulipanin (delphinidin-3-''O''-rutinoside) can be found in blackcurrant pomace. * Violdelphin (delphinidin 3-rutinoside-7-''O''-(6-''O''-(4-(6-''O''-(4-hydroxybenzoyl)-β-D-glucosyl)oxybenzoyl)-β-D-glucoside) is responsible for the purplish-blue flower color of '' Aconitum chinense''. * Nasunin (delphinidin-3-(''p''-coumaroylrutinoside)-5-glucosid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Star Activity
A star is a luminous spheroid of plasma held together by self-gravity. The nearest star to Earth is the Sun. Many other stars are visible to the naked eye at night; their immense distances from Earth make them appear as fixed points of light. The most prominent stars have been categorised into constellations and asterisms, and many of the brightest stars have proper names. Astronomers have assembled star catalogues that identify the known stars and provide standardized stellar designations. The observable universe contains an estimated to stars. Only about 4,000 of these stars are visible to the naked eye—all within the Milky Way galaxy. A star's life begins with the gravitational collapse of a gaseous nebula of material largely comprising hydrogen, helium, and traces of heavier elements. Its total mass mainly determines its evolution and eventual fate. A star shines for most of its active life due to the thermonuclear fusion of hydrogen into helium in its core. Thi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Non-proteinogenic Amino Acids
In biochemistry, non-coded or non-proteinogenic amino acids are distinct from the 22 proteinogenic amino acids (21 in eukaryotesplus formylmethionine in eukaryotes with prokaryote organelles like mitochondria), which are naturally encoded in the genome of organisms for the assembly of proteins. However, over 140 non-proteinogenic amino acids occur naturally in proteins and thousands more may occur in nature or be synthesized in the laboratory. Chemically synthesized amino acids can be called unnatural amino acids. Unnatural amino acids can be synthetically prepared from their native analogs via modifications such as amine alkylation, side chain substitution, structural bond extension cyclization, and isosteric replacements within the amino acid backbone. Many non-proteinogenic amino acids are important: * intermediates in biosynthesis, * in post-translational formation of proteins, * in a physiological role (e.g. components of Peptidoglycan, bacterial cell walls, neurotransmitters ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tyrocidine
Tyrocidine is a mixture of cyclic decapeptides produced by the bacteria ''Brevibacillus brevis'' found in soil. It can be composed of 4 different amino acid sequences, giving tyrocidine A–D (See figure 1). Tyrocidine is the major constituent of tyrothricin, which also contains gramicidin.Pubchem: Tyrocidine and Tyrothricin. Tyrocidine was the first commercially available antibiotic, but has been found to be toxic toward human blood and reproductive cells. The function of tyrocidine within its host ''B. brevis'' is thought to be regulation of sporulation. Tyrocidines A, B, and C are cyclic decapeptides. The biosynthesis of tyrocidine involves three enzymes. Parts of its sequence are identical to gramicidin S. History In 1939, the American microbiologist René Dubos discovered the soil microbe ''Bacillus brevis''. He observed the ability of the microbe to decompose the capsule of pneumococcus bacterium, rendering it harmless. From the soil microbe ''B. brevis'', he isola ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacillus Brevis
''Brevibacillus brevis'' (formerly known as ''Bacillus brevis'') is a Gram-positive, aerobic, motile, spore-forming, rod-shaped bacterium commonly found in soil, air, water, and decaying matter. It is rarely associated with infectious diseases. The antibiotics gramicidin and tyrocidine were first isolated from it.Abedon, Stephen. "Bacteria Binomials." 26 Apr 1998. Ohio State University. 17 Jun 2006 . ''Brevibacillus brevis'' is catalase positive, amylase negative, casein negative, gelatinase positive, and indole negative; most strains are citrate users. Some strains are capable of oxidizing carbon monoxide Carbon monoxide (chemical formula CO) is a poisonous, flammable gas that is colorless, odorless, tasteless, and slightly less dense than air. Carbon monoxide consists of one carbon atom and one oxygen atom connected by a triple bond. It is the si ... aerobically. Optimal growth occurs at 35 °C to 55 °C. References Paenibacillaceae Pathogenic bacteria B ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
