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Palmitoyl(protein) Hydrolase
Palmitoyl protein hydrolase/thioesterases is an enzyme (EC 3.1.2.22) that removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. It catalyzes the reaction :palmitoyl rotein+ H2O \rightleftharpoons palmitate + protein This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is palmitoyl roteinhydrolase. Other names in common use include palmitoyl-protein thioesterase, and palmitoyl-(protein) hydrolase. This enzyme participates in fatty acid elongation in mitochondria. Neuronal ceroid lipofuscinoses (NCL) represent a group of encephalopathies that occur in 1 in 12,500 children. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. The most common mutation results in intracellular accumulation of the polypeptide and undetectable enzyme activity in the brain. Direct sequencing of c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lipid Bilayer
The lipid bilayer (or phospholipid bilayer) is a thin polar membrane made of two layers of lipid molecules. These membranes form a continuous barrier around all cell (biology), cells. The cell membranes of almost all organisms and many viruses are made of a lipid bilayer, as are the nuclear envelope, nuclear membrane surrounding the cell nucleus, and biological membrane, membranes of the membrane-bound organelles in the cell. The lipid bilayer is the barrier that keeps ions, proteins and other molecules where they are needed and prevents them from diffusing into areas where they should not be. Lipid bilayers are ideally suited to this role, even though they are only a few nanometers in width, because they are impermeable to most water-soluble (hydrophilic) molecules. Bilayers are particularly impermeable to ions, which allows cells to regulate salt concentrations and pH by transporting ions across their membranes using proteins called Ion transporter, ion pumps. Biological bilaye ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PPT1
Palmitoyl-protein thioesterase 1 (PPT-1), also known as palmitoyl-protein hydrolase 1, is an enzyme that in humans is encoded by the PPT1 gene. Function PPT-1 a member of the palmitoyl protein thioesterase family. PPT-1 is a small glycoprotein involved in the catabolism of lipid-modified proteins during lysosomal degradation. This enzyme removes thioester In organic chemistry, thioesters are organosulfur compounds with the molecular structure . They are analogous to carboxylate esters () with the sulfur in the thioester replacing oxygen in the carboxylate ester, as implied by the thio- prefix ...-linked fatty acyl groups such as palmitate from cysteine residues. Clinical significance Defects in this gene are a cause of neuronal ceroid lipofuscinosis type 1 (CLN1). Genetic basis and phenotypic correlations of the neuronal ceroid lipofusinoses. eview Warrier V; Vieira M; Mole SE. Biochimica et Biophysica Acta. 1832(11):1827-30, 2013 References Further readin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EC 3
EC3 can refer to: People * Ethan Carter III (EC3) (born 1983), American professional wrestler Places * EC3, a district in the London EC postcode area Groups, organizations, companies * European Cybercrime Centre * EarthCheck, formerly EC3 Global; international tourism advisory group Transportation * BJEV ''EC3'', a Chinese electric vehicle * KUR ''EC3 class'', a class of steam locomotive * EC-3 radar, Italian WWII radar Other uses * Dolby Digital Plus, also known as EC-3 * Hydrolase enzymes (EC 3); see List of EC numbers (EC 3) See also * ECCC (other) {{Letter-NumberCombDisambig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acyl-protein Thioesterase
Acyl-protein thioesterases are enzymes that cleave off Lipid-anchored protein, lipid Post-translational modification, modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. Acyl-protein thioesterases are part of the Alpha/beta hydrolase superfamily, α/β hydrolase superfamily of proteins and have a conserved catalytic triad. For that reason, acyl-protein thioesterases are also able to Hydrolysis, hydrolyze oxygen-linked Ester, ester bonds. Function Acyl-protein thioesterases are involved in the Palmitoylation, depalmitoylation of proteins, meaning they cleave off Palmitoylation, palmitoyl modifications on proteins' cysteine residues. Biological target, Cellular targets include G alpha subunit, trimeric G-alpha proteins, ion channels and Gap-43 protein, GAP-43. Moreover, LYPLA1, human acyl-protein thioesterases 1 and LYPLA2, 2 have been identified as major components in controlling the palmitoylation cycle of the oncogene Ras subfa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Palmitoyl
In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (''S''-palmitoylation) and less frequently to serine and threonine (''O''-palmitoylation) residues of proteins, which are typically membrane proteins. The precise function of palmitoylation depends on the particular protein being considered. Palmitoylation enhances the hydrophobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments, as well as in modulating protein–protein interactions. In contrast to prenylation and myristoylation, palmitoylation is usually reversible (because the bond between palmitic acid and protein is often a thioester bond). The reverse reaction in mammalian cells is catalyzed by acyl-protein thioesterases (APTs) in the cytosol and palmitoyl protein thioesterases in lysosomes. Because palmitoylation i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules such as proteins and nucleic acids, which is overseen by the Worldwide Protein Data Bank (wwPDB). This structural data is obtained and deposited by biologists and biochemists worldwide through the use of experimental methodologies such as X-ray crystallography, Nuclear magnetic resonance spectroscopy of proteins, NMR spectroscopy, and, increasingly, cryo-electron microscopy. All submitted data are reviewed by expert Biocuration, biocurators and, once approved, are made freely available on the Internet under the CC0 Public Domain Dedication. Global access to the data is provided by the websites of the wwPDB member organizations (PDBe, PDBj, RCSB PDB, and BMRB). The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tertiary Structure
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of these structures may bind to each other, forming a quaternary structure. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demon ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PPT2
Lysosomal thioesterase PPT2 (PPT-2), also known as S-thioesterase G14, is an enzyme that in humans is encoded by the ''PPT2'' gene. Function This gene encodes a member of the palmitoyl protein thioesterase family. The encoded glycosylated lysosomal protein has palmitoyl-CoA hydrolase activity in vitro, but does not hydrolyze palmitate from cysteine Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the chemical formula, formula . The thiol side chain in cysteine enables the formation of Disulfide, disulfide bonds, and often participates in enzymatic reactions as ... residues in proteins. References Further reading * * * * * * * * * * * * * * * * * EC 3.1.2 {{gene-6-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neuronal Ceroid Lipofuscinosis
Neuronal ceroid lipofuscinosis is a family of at least eight genetically separate neurodegenerative lysosomal storage diseases that result from excessive accumulation of lipopigments (lipofuscin) in the body's tissues. These lipopigments are made up of fats and proteins. Their name comes from the word stem "lipo-", which is a variation on lipid, and from the term "pigment", used because the substances take on a greenish-yellow color when viewed under an ultraviolet light microscope. These lipofuscin materials build up in neuronal cells and many organs, including the liver, spleen, myocardium, and kidneys. Signs and symptoms The classic characterization of the group of neurodegenerative, lysosomal storage disorders called the neuronal ceroid lipofuscinoses (NCLs) is through the progressive, permanent loss of motor and psychological ability with a severe intracellular accumulation of lipofuscins, with the United States and Northern European populations having slightly higher freque ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thioester
In organic chemistry, thioesters are organosulfur compounds with the molecular structure . They are analogous to carboxylate esters () with the sulfur in the thioester replacing oxygen in the carboxylate ester, as implied by the thio- prefix. They are the product of esterification of a carboxylic acid () with 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. The R and R' represent organyl groups, or H in the case of R. Synthesis One route to thioesters involves the reaction of an acid chloride with an alkali metal salt of a thiol: : 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: : Th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fatty Acid Elongation In Mitochondria
Fatty is a derogatory term for someone who is obese. It may refer also to: People Nickname * Roscoe Arbuckle (1887–1933), American actor and comedian * Fatty Briody (1858–1903), American Major League Baseball player * Bob Fothergill (1897–1938), American Major League Baseball outfielder * William Foulke (footballer) (1874–1916), English cricketer and footballer * Richard Lamb (1907–1974), Australian racing cyclist * Fatty Lawrence (1903–1976), American college gridiron football player * W. T. McLain (1885–1938), American college gridiron football player, lawyer and politician * Charles H. Smith (American football), University of Michigan football player in 1893–1894 * Fatty Taylor (1946–2017), retired American Basketball Association and National Basketball Association player * Paul Vautin (born 1959), Australian former rugby league footballer and coach, television presenter and commentator * Thomas Walsh (mobster) (died 1929), New York City mobster * Fa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
List Of Enzymes
Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: :Oxidoreductases (EC 1) ( Oxidoreductase) * Dehydrogenase * Luciferase * DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) ** Homoserine dehydrogenase ** Aminopropanol oxidoreductase ** Diacetyl reductase ** Glycerol dehydrogenase ** Propanediol-phosphate dehydrogenase ** glycerol-3-phoshitiendopene dehydrogenase (NAD+) ** D-xylulose reductase ** L-xylulose reductase ** Lactate dehydrogenase ** Malate dehydrogenase ** Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) ** Glucose oxidase ** L-gulonolactone oxidase ** Thiamine oxidase ** Xanthine oxidase * EC 1.1.4 (with a disulfide as accep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
