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Long-chain-fatty-acid—CoA Ligase
The long chain fatty acyl-CoA ligase (or synthetase) is an enzyme () of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylation, adenylated intermediate. The enzyme catalyzes the following reaction, :Fatty acid + coenzyme A, CoA + adenosine triphosphate, ATP ⇌ Acyl-CoA + adenosine monophosphate, AMP + pyrophosphate, PPi It is present in all organisms from bacteria to humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorporated in phospholipids. Function Long chain fatty acyl-CoA synthetase, LC-FACS, plays a role in the physiological regulation of various cellular functions via the production of long chain fatty acyl-CoA esters, which reportedly have affected protein transport, enzyme activation, protein acylation, cell signaling, and transcriptional regulation. The formation of fatty acyl-Co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thermus Thermophilus
''Thermus thermophilus'' is a Gram-negative bacterium used in a range of biotechnological applications, including as a model organism for genetic manipulation, structural genomics, and systems biology. The bacterium is extremely thermophilic, with an optimal growth temperature of about . ''Thermus thermophilus'' was originally isolated from a thermal vent within a hot spring in Izu, Japan by Tairo Oshima and Kazutomo Imahori. The organism has also been found to be important in the degradation of organic materials in the thermogenic phase of composting. ''T. thermophilus'' is classified into several strains, of which HB8 and HB27 are the most commonly used in laboratory environments. Genome analyses of these strains were independently completed in 2004. Cell Structure ''Thermus thermophilus'' is a Gram-negative bacterium with an outer membrane that is composed of phospholipids and lipopolysaccharides. This bacterium also has a thin peptidoglycan (also known as murein) layer, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenosine Triphosphate
Adenosine triphosphate (ATP) is an organic compound that provides energy to drive many processes in living cells, such as muscle contraction, nerve impulse propagation, condensate dissolution, and chemical synthesis. Found in all known forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. The human body recycles its own body weight equivalent in ATP each day. It is also a precursor to DNA and RNA, and is used as a coenzyme. 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 an adenine attached by the 9-nitrogen atom to the 1′ carbon atom of a sugar (ribose), which i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monomer
In chemistry, a monomer ( ; ''mono-'', "one" + '' -mer'', "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or three-dimensional network in a process called polymerization. Classification Monomers can be classified in many ways. They can be subdivided into two broad classes, depending on the kind of the polymer that they form. Monomers that participate in condensation polymerization have a different stoichiometry than monomers that participate in addition polymerization: : Other classifications include: *natural vs synthetic monomers, e.g. glycine vs caprolactam, respectively *polar vs nonpolar monomers, e.g. vinyl acetate vs ethylene, respectively *cyclic vs linear, e.g. ethylene oxide vs ethylene glycol, respectively The polymerization of one kind of monomer gives a homopolymer. Many polymers are copolymers, meaning that they are derived from two different monomers. In the case of condensation polymerizations, the r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Substrate (biochemistry)
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 microscop ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Long Chain Fatty Acyl-CoA Synthetase
Long may refer to: Measurement * Long, characteristic of something of great duration * Long, characteristic of something of great length * Longitude (abbreviation: long.), a geographic coordinate * Longa (music), note value in early music mensural notation Places Asia * Long District, Laos * Long District, Phrae, Thailand * Longjiang (other) or River Long (lit. "dragon river"), one of several rivers in China * Yangtze River or Changjiang (lit. "Long River"), China Elsewhere * Long, Somme, France * Long, Washington, United States People * Long (surname) * Long (surname 龍) (Chinese surname) Fictional characters * Long (''Bloody Roar''), in the video game series Sports * Long, a fielding term in cricket * Long, in tennis and similar games, beyond the service line during a serve and beyond the baseline during play Other uses * , a U.S. Navy ship name * Long (finance), a position in finance, especially stock markets * Lòng, name for a laneway in Shanghai * Long in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thioester
In organic chemistry, thioesters are organosulfur compounds with the functional group . They are analogous to carboxylate esters () with the sulfur in the thioester playing the role of the linking oxygen in the carboxylate ester, as implied by the ''thio-'' prefix. They are the product of esterification between a carboxylic acid () and a thiol (). In biochemistry, the best-known thioesters are derivatives of coenzyme A, e.g., acetyl-CoA.Matthys J. Janssen "Carboxylic Acids and Esters" in PATAI's Chemistry of Functional Groups: Carboxylic Acids and Esters, Saul Patai, Ed. John Wiley, 1969, New York: pp. 705–764. Synthesis The most typical route to thioester involves the reaction of an acid chloride with an alkali metal salt of a thiol: :RSNa + R'COCl -> R'COSR + NaCl Another common route entails the displacement of halides by the alkali metal salt of a thiocarboxylic acid. For example, thioacetate esters are commonly prepared by alkylation of potassium thioacetate: :CH3COSK + ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acyl CoA
Acyl-CoA is a group of coenzymes that metabolize fatty acids. Acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of ATP. In this way, fats are converted to ATP, the universal biochemical energy carrier. Functions Fatty acid activation Fats are broken down by conversion to acyl-CoA. This conversion is one response to high energy demands such as exercise. The oxidative degradation of fatty acids is a two-step process, catalyzed by acyl-CoA synthetase. Fatty acids are converted to their acyl phosphate, the precursor to acyl-CoA. The latter conversion is mediated by acyl-CoA synthase" :acyl-P + HS-CoA → acyl-S-CoA + Pi + H+ Three types of acyl-CoA synthases are employed, depending on the chain length of the fatty acid. For example, the substrates for medium chain acyl-CoA synthase are 4-11 carbon fatty acids. The enzyme acyl-CoA thioesterase takes of the acyl-CoA t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coenzyme A
Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenic acid, pantothenate (vitamin B5), and adenosine triphosphate (ATP). In acetyl-CoA, its acetyl form, coenzyme A is a highly versatile molecule, serving metabolic functions in both the Anabolism, anabolic and Catabolism, catabolic pathways. Acetyl-CoA is utilised in the post-translational regulation and allosteric regulation of pyruvate dehydrogenase and carboxylase to maintain and support the partition of Pyruvic acid, pyruvate synthesis and degradation. Discovery of structure Coenzyme A was identified by Fritz Lipmann in 1946, who also later gave it its name. Its structure was determined during the e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyrophosphate
In chemistry, pyrophosphates are phosphorus oxyanions that contain two phosphorus atoms in a P–O–P linkage. A number of pyrophosphate salts exist, such as disodium pyrophosphate (Na2H2P2O7) and tetrasodium pyrophosphate (Na4P2O7), among others. Often pyrophosphates are called diphosphates. The parent pyrophosphates are derived from partial or complete neutralization of pyrophosphoric acid. The pyrophosphate bond is also sometimes referred to as a phosphoanhydride bond, a naming convention which emphasizes the loss of water that occurs when two phosphates form a new P–O–P bond, and which mirrors the nomenclature for anhydrides of carboxylic acids. Pyrophosphates are found in ATP and other nucleotide triphosphates, which are important in biochemistry. The term pyrophosphate is also the name of esters formed by the condensation of a phosphorylated biological compound with inorganic phosphate, as for dimethylallyl pyrophosphate. This bond is also referred to as a high-energy ... [...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 (binding site) and residues that catalyse a reaction of that substrate (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 function. The active si ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
