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Nα-acetyltransferase 60
Nα-acetyltransferase 60 (NAA60) also known as NatF is a member of the N-terminal acetyltransferase (NAT) family of proteins. NATs bind to acetyl-coenzyme A (Ac-CoA) as well as to the protein N-terminus, and enzymatically transfer the acetyl group from Ac-CoA to the free backbone amino group (NH3+) on the first residue of the protein. NATs are mono- or multisubunit enzymes consisting of one catalytic subunit and up to two auxiliary subunits, however, only a catalytic subunit of NAA60 has been identified so far. Structure The crystal structure of NAA60 was solved in 2016, though it was missing the C-terminal region due to difficulties purifying the whole protein. The structure revealed an overall fold that is similar to the catalytic subunit of ribosome-associated NATs, and the two residues Y164 and Y165 of the β6-β7 loop important for peptide anchoring is conserved in NAA60 as in multiple NATs. Most similarities in the active site of NAA60 were found to NAA50. The two NATs sha ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acetyltransferase
An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation. In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules. Types of acetyltransferases Additional examples of acetyltransferases found in nature include: * Chloramphenicol acetyltransferase Structure The predicted three-dimensional structures of histone, choline, and serotonin acetyltransferases are shown below. As with all enzymes, the structures of acetyltransferases are essential for interactions between them and their substrates; alterations to the structures of these enzymes often result in a loss o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...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] |
Acetyl
In organic chemistry, an acetyl group is a functional group denoted by the chemical formula and the structure . It is sometimes represented by the symbol Ac (not to be confused with the element actinium). In IUPAC nomenclature, an acetyl group is called an ethanoyl group. An acetyl group contains a methyl group () that is single-bonded to a carbonyl (), making it an acyl group. The carbonyl center of an acyl radical has one non-bonded electron with which it forms a chemical bond to the remainder (denoted with the letter ''R'') of the molecule. The acetyl moiety is a component of many organic compounds, including acetic acid, the neurotransmitter acetylcholine, acetyl-CoA, acetylcysteine, acetaminophen (also known as paracetamol), and acetylsalicylic acid (also known as aspirin). Acetylation Acetylation is the chemical reaction known as "ethanoylation" in the IUPAC nomenclature. It depicts a reactionary process that injects an acetyl functional group into a chemical ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Group
In chemistry, amines (, ) are organic compounds that contain carbon-nitrogen bonds. Amines are formed when one or more hydrogen atoms in ammonia are replaced by alkyl or aryl groups. The nitrogen atom in an amine possesses a lone pair of electrons. Amines can also exist as hetero cyclic compounds. Aniline is the simplest aromatic amine, consisting of a benzene ring bonded to an amino group. Amines are classified into three types: primary (1°), secondary (2°), and tertiary (3°) amines. Primary amines (1°) contain one alkyl or aryl substituent and have the general formula RNH2. Secondary amines (2°) have two alkyl or aryl groups attached to the nitrogen atom, with the general formula R2NH. Tertiary amines (3°) contain three substituent groups bonded to the nitrogen atom, and are represented by the formula R3N. The functional group present in primary amines is called the amino group. Classification of amines Amines can be classified according to the nature and number o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (carboxyl g ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Golgi Apparatus
The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic Cell (biology), cells. Part of the endomembrane system in the cytoplasm, it protein targeting, packages proteins into membrane-bound Vesicle (biology and chemistry), vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and Endocytosis, endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus. The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist Camillo Golgi. The organelle was later named after him in the 1910s. Discovery Because of its large size and distinctive structure, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Organelle
In cell biology, an organelle is a specialized subunit, usually within a cell (biology), cell, that has a specific function. The name ''organelle'' comes from the idea that these structures are parts of cells, as Organ (anatomy), organs are to the Human body, body, hence ''organelle,'' the suffix ''-elle'' being a diminutive. Organelles are either separately enclosed within their own lipid bilayers (also called membrane-bounded organelles) or are spatially distinct functional units without a surrounding lipid bilayer (non-membrane bounded organelles). Although most organelles are functional units within cells, some functional units that extend outside of cells are often termed organelles, such as cilia, the flagellum and archaellum, and the trichocyst (these could be referred to as membrane bound in the sense that they are attached to (or bound to) the membrane). Organelles are identified by microscopy, and can also be purified by cell fractionation. There are many types of organe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endosome
Endosomes are a collection of intracellular sorting organelles in eukaryotic cells. They are parts of the endocytic membrane transport pathway originating from the trans Golgi network. Molecules or ligands internalized from the plasma membrane can follow this pathway all the way to lysosomes for degradation or can be recycled back to the cell membrane in the endocytic cycle. Molecules are also transported to endosomes from the trans Golgi network and either continue to lysosomes or recycle back to the Golgi apparatus. Endosomes can be classified as early, sorting, or late depending on their stage post internalization. Endosomes represent a major sorting compartment of the endomembrane system in cells. Function Endosomes provide an environment for material to be sorted before it reaches the degradative lysosome. For example, low-density lipoprotein (LDL) is taken into the cell by binding to the LDL receptor at the cell surface. Upon reaching early endosomes, the LDL dis ... [...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] |
Lipid
Lipids are a broad group of organic compounds which include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E and K), monoglycerides, diglycerides, phospholipids, and others. The functions of lipids include storing energy, signaling, and acting as structural components of cell membranes. Lipids have applications in the cosmetic and food industries, and in nanotechnology. Lipids are broadly defined as hydrophobic or amphiphilic small molecules; the amphiphilic nature of some lipids allows them to form structures such as vesicles, multilamellar/ unilamellar liposomes, or membranes in an aqueous environment. Biological lipids originate entirely or in part from two distinct types of biochemical subunits or "building-blocks": ketoacyl and isoprene groups. Using this approach, lipids may be divided into eight categories: fatty acyls, glycerolipids, glycerophospholipids, sphingolipids, saccharolipids, and polyketides (derived from condensatio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Primary Familial Brain Calcification
Primary familial brain calcification Initial Posting: April 18, 2004; Last Update: August 24, 2017. (PFBC), also known as familial idiopathic basal ganglia calcification (FIBGC) and Fahr's disease, is a rare, Dominance_(genetics), genetically dominant or recessive, inherited neurology, neurological disorder characterized by abnormal deposits of calcium in areas of the brain that control movement. Through the use of Computed tomography, CT scans, calcifications are seen primarily in the basal ganglia and in other areas such as the cerebral cortex. Signs and symptoms Symptoms of this disease include deterioration of motor functions and speech, seizures, and other involuntary movement. Other symptoms are headaches, dementia, and vision impairment. Characteristics of Parkinson's Disease are also similar to PFBC. The disease usually manifests itself in the third to fifth decade of life but may appear in childhood or later in life.Sobrido MJ, Hopfer S, Geschwind DH (2007)Familial idiop ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
