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Adenylyl Cyclase
Adenylate cyclase (EC 4.6.1.1, also commonly known as adenyl cyclase and adenylyl cyclase, abbreviated AC) is an enzyme with systematic name ATP diphosphate-lyase (cyclizing; 3′,5′-cyclic-AMP-forming). It catalyzes the following reaction: :ATP = 3′,5′-cyclic AMP + diphosphate It has key regulatory roles in essentially all Cell (biology), cells. It is the most Polyphyly, polyphyletic known enzyme: six distinct classes have been described, all catalysis, catalyzing the same reaction but representing unrelated gene Gene family, families with no known Sequence homology, sequence or structural homology. The best known class of adenylyl cyclases is class III or AC-III (Roman numerals are used for classes). AC-III occurs widely in eukaryotes and has important roles in many human Tissue (biology), tissues. All classes of adenylyl cyclase Catalysis, catalyse the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate, 3',5'-cyclic AMP (cAMP) and pyrophosphate ...
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Trimer (chemistry)
In chemistry, a trimer (; ) is a molecule or polyatomic anion formed by combination or association of three molecules or ions of the same substance. In technical jargon, a trimer is a kind of oligomer derived from three identical Precursor (chemistry), precursors often in competition with polymerization. Examples Alkyne trimerization In 1866, Marcellin Berthelot reported the first example of cyclotrimerization, the conversion of acetylene to benzene. This process was commercialized: : Nitrile trimerization Symmetrical 1,3,5-triazines are prepared by trimerization of certain nitriles such as cyanogen chloride. Cyanogen chloride and cyanogen bromide each trimerize at elevated temperatures over a carbon catalyst. The chloride gives cyanuric chloride: : The bromide has an extended shelflife when refrigerated. Like the chloride, it undergoes ab exothermic trimerization to form cyanuric bromide. This reaction is catalyzed by traces of bromine, metal salts, acids and bases. For th ...
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Adenosine Triphosphate
Adenosine triphosphate (ATP) is a nucleoside triphosphate that provides energy to drive and support many processes in living cell (biology), cells, such as muscle contraction, nerve impulse propagation, and chemical synthesis. Found in all known forms of life, it is often referred to as the "molecular unit of currency" for intracellular energy transfer. When consumed in a Metabolism, metabolic process, ATP converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. It is also a Precursor (chemistry), precursor to DNA and RNA, and is used as a coenzyme. An average adult human processes around 50 kilograms (about 100 mole (unit), moles) daily. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base (adenine), the sugar ribose, and the Polyphosphate, triphosphate. Structure ATP consists of three parts: a sugar, an amine base ...
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Anthrax Toxin
Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, '' Bacillus anthracis''—the causative agent of anthrax. The toxin was first discovered by Harry Smith in 1954. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). These three protein components act together to impart their physiological effects. Assembled complexes containing the toxin components are endocytosed. In the endosome, the enzymatic components of the toxin translocate into the cytoplasm of a target cell. Once in the cytosol, the enzymatic components of the toxin disrupt various immune cell functions, namely cellular signaling and cell migration. The toxin may even induce cell lysis, as is observed for macrophage cells. Anthrax toxin allows the bacteria to evade the immune system, proliferate, and ultimately kill the host animal. Research on anthrax toxin also provi ...
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CyaA
Adenylate cyclase toxin (CyaA) is released from bacterium Bordetella pertussis by the T1SS (Type 1 secretion system) and released in the host’s respiratory tract in order to suppress its early innate and subsequent adaptive immune defense. CyaA plays a particular role in the early phases of airway colonization. It is able to instantly ablate the bactericidal oxidative burst, along with the opsonophagocytic killing capacities of neutrophils and macrophages. As a result, it enables establishment of Bordetella infection of airway mucosa and promotes immune evasion of B. pertussis, by affecting the host’s immune cells. Structure The toxin is a 1706 residue-long polypeptide that consists of an N-terminal ~400 residue-long adenylate cyclase (AC) enzyme that is linked to a characteristic Hemolysin, RTX hemolysin (Hly) moiety of ~1300 residues. This Hly moiety itself consists of four functional subdomains, comprising: (i) a hydrophobic pore-forming domain ; (ii) an activation domain ...
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CCA TRNA Nucleotidyltransferase
CCA tRNA nucleotidyltransferase (, ''CCA-adding enzyme'', ''tRNA adenylyltransferase'', ''tRNA CCA-pyrophosphorylase'', ''tRNA-nucleotidyltransferase'', ''transfer-RNA nucleotidyltransferase'', ''transfer ribonucleic acid nucleotidyl transferase'', ''CTP(ATP):tRNA nucleotidyltransferase'', ''transfer ribonucleate adenylyltransferase'', ''transfer ribonucleate adenyltransferase'', ''transfer RNA adenylyltransferase'', ''transfer ribonucleate nucleotidyltransferase'', ''ATP (CTP):tRNA nucleotidyltransferase'', ''ribonucleic cytidylic cytidylic adenylic pyrophosphorylase'', ''transfer ribonucleic adenylyl (cytidylyl) transferase'', ''transfer ribonucleic-terminal trinucleotide nucleotidyltransferase'', ''transfer ribonucleate cytidylyltransferase'', ''ribonucleic cytidylyltransferase'', ''-C-C-A pyrophosphorylase'', ''ATP(CTP)-tRNA nucleotidyltransferase'', ''tRNA adenylyl(cytidylyl)transferase'', ''CTP:tRNA cytidylyltransferase'') is an enzyme with systematic name ''CTP,CTP,ATP:tRNA cy ...
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DNA Polymerase Beta
DNA polymerase beta, also known as POLB, is an enzyme present in eukaryotes. In humans, it is encoded by the ''POLB'' gene. Function In eukaryotic cells, DNA polymerase beta (POLB) performs base excision repair (BER) required for DNA maintenance, replication, recombination, and drug resistance. The mitochondrial DNA of mammalian cells is constantly under attack from oxygen radicals released during ATP production. Mammalian cell mitochondria contain an efficient base excision repair system employing POLB that removes some frequent oxidative DNA damages. POLB thus has a key role in maintaining the stability of the mitochondrial genome. An analysis of the fidelity of DNA replication by polymerase beta in the neurons from young and very aged mice indicated that aging has no significant effect on the fidelity of DNA synthesis by polymerase beta. This finding was considered to provide evidence against the error catastrophe theory of aging. Base excision repair Cabelof ...
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CAMP Receptor Protein
cAMP receptor protein (CRP; also known as catabolite activator protein, CAP) is a regulatory protein in bacteria. Protein CRP protein binds cyclic adenosine monophosphate (cAMP), which causes a conformational change that allows CRP to bind tightly to a specific DNA site in the promoters of the genes it controls. CRP then activates transcription through direct protein–protein interactions with RNA polymerase. The genes regulated by CRP are mostly involved in energy metabolism, such as galactose, citrate, or the PEP group translocation system. In ''Escherichia coli'', CRP can regulate the transcription of more than 100 genes. The signal to activate CRP is the binding of cyclic AMP. Binding of cAMP to CRP leads to a long-distance signal transduction from the N-terminal cAMP-binding domain to the C-terminal domain of the protein, which is responsible for interaction with specific sequences of DNA. At "Class I" CRP-dependent promoters, CRP binds to a DNA site located upstream of ...
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Adenylate Kinase
Adenylate kinase ( ECbr>2.7.4.3 (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates (ATP, ADP, and AMP). By constantly monitoring phosphate nucleotide levels inside the cell, ADK plays an important role in cellular energy homeostasis. Substrate and products The reaction catalyzed is: ATP + AMP ⇔ 2 ADP The equilibrium constant varies with condition, but it is close to 1. Thus, ΔGo for this reaction is close to zero. In muscle from a variety of species of vertebrates and invertebrates, the concentration of ATP is typically 7-10 times that of ADP, and usually greater than 100 times that of AMP. The rate of oxidative phosphorylation is controlled by the availability of ADP. Thus, the mitochondrion attempts to keep ATP levels high due to the combined action of adenylate kinase and the controls on oxidative phosphorylation. Isozymes To date there have been nine human ADK protein isoforms ...
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Membrane Transport Proteins
A membrane transport protein is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins; that is they exist permanently within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion, active transport, osmosis, or reverse diffusion. The two main types of proteins involved in such transport are broadly categorized as either ''channels'' or ''carriers'' (a.k.a. transporters, or permeases). Examples of channel/carrier proteins include the GLUT 1 uniporter, sodium channels, and potassium channels. The solute carriers and atypical SLCs are secondary active or facilitative transporters in humans. Collectively membrane transporters and channels are known as the transportome. Transportomes govern cellular influx and efflux of not only ions and nutrients but drug ...
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Kinase
In biochemistry, a kinase () is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule. As a result, kinase produces a phosphorylated substrate and ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group (producing a dephosphorylated substrate and the high energy molecule of ATP). These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis. Kinases are part of the larger family of phosphotransferases. Kinases should not be confused with phosphorylases, which catalyze the addition of inorganic phosphate groups to an acceptor, nor with phosphatases, which remove phosphate groups (dephosphorylation). The phosphorylation state of a molecule, whether it ...
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Transcription Factor
In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription (genetics), transcription of genetics, genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The function of TFs is to regulate—turn on and off—genes in order to make sure that they are Gene expression, expressed in the desired Cell (biology), cells at the right time and in the right amount throughout the life of the cell and the organism. Groups of TFs function in a coordinated fashion to direct cell division, cell growth, and cell death throughout life; cell migration and organization (body plan) during embryonic development; and intermittently in response to signals from outside the cell, such as a hormone. There are approximately 1600 TFs in the human genome. Transcription factors are members of the proteome as well as regulome. TFs work alone or with other proteins in a complex, by promoting (a ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ...
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