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Protein-arginine Deiminase
In enzymology, a protein-arginine deiminase (PAD) () is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrullination: :protein L-arginine + H2O \rightleftharpoons protein L-citrulline + NH3 Thus, the two substrates of this enzyme are protein L-arginine (arginine residue inside a protein) and H2O, whereas its two products are protein L-citrulline and NH3: : This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is protein-L-arginine iminohydrolase. This enzyme is also called peptidylarginine deiminase. Structural studies As of late 2007, seven structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and . Mammalian proteins Mammals have 5 protein-arginine deiminases, with symbols * PADI1, PADI2, PADI3, PADI4, PADI6 except for rodent Rodents ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzymology
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] |
Amidine
Amidines are organic compounds with the functional group RC(NR)NR2, where the R groups can be the same or different. They are the imine derivatives of amides (RC(O)NR2). The simplest amidine is formamidine, HC(=NH)NH2. Examples of amidines include: * 1,8-Diazabicycloundec-7-ene, DBU * diminazene * benzamidine * Pentamidine * Paranyline Preparation A common route to primary amidines is the Pinner reaction. Reaction of the nitrile with alcohol in the presence of acid gives an Carboximidate, iminoether. Treatment of the resulting compound with ammonia then completes the conversion to the amidine. Instead of using a Brønsted–Lowry acid–base theory, Bronsted acid, Lewis acids and bases, Lewis acids such as Aluminium chloride, aluminium trichloride promote the direct amination of nitriles, or, in certain exceptional cases, of amides. Dimethylformamide acetal reacts with primary amines to give amidines: :Me2NC(H)(OMe)2 + RNH2 → Me2NC=NHR + 2 MeOH Catalysis is likewise not require ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GSK484
GSK484 is an experimental drug which acts as a selective inhibitor of the enzyme peptidylarginine deiminase 4 (PAD4). It has antiinflammatory effects and has been researched for potential use in the treatment of various inflammatory conditions, primarily rheumatoid arthritis, but it has also been used to investigate the role of PAD4 in acute kidney injury, lung inflammation, heart muscle damage following heart attack, osteoporosis, diabetes, and some forms of cancer Cancer is a group of diseases involving Cell growth#Disorders, abnormal cell growth with the potential to Invasion (cancer), invade or Metastasis, spread to other parts of the body. These contrast with benign tumors, which do not spread. Po .... See also * AFM-30a * BB-Cl-Amidine * JBI-589 References {{reflist Experimental drugs Alcohols Alkylamines Benzamides Cyclopropanes Imidazoles Methoxy compounds Piperidines Indoles ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
BB-Cl-Amidine
BB-Cl-Amidine is an experimental drug which acts as a non-subtype selective, irreversible inhibitor of the enzyme peptidylarginine deiminase (PAD). It has anti-cancer effects and is useful for various inflammatory conditions such as arthritis, and while it may be unlikely to be developed for human use due to toxicity concerns, it is widely used in scientific research. As well as its activity as a PAD inhibitor, BB-Cl-Amidine also inhibits the action of the Stimulator of interferon genes (STING) protein by preventing STING oligomerization and thereby terminating the signalling pathway. See also * AFM-30a * GSK484 GSK484 is an experimental drug which acts as a selective inhibitor of the enzyme peptidylarginine deiminase 4 (PAD4). It has antiinflammatory effects and has been researched for potential use in the treatment of various inflammatory conditions, ... * JBI-589 References {{reflist Experimental drugs Biphenyls Benzamides Benzimidazoles Amidines Organochlorid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rodent
Rodents (from Latin , 'to gnaw') are mammals of the Order (biology), order Rodentia ( ), which are characterized by a single pair of continuously growing incisors in each of the upper and Mandible, lower jaws. About 40% of all mammal species are rodents. They are native to all major land masses except for Antarctica, and several oceanic islands, though they have subsequently been introduced to most of these land masses by human activity. Rodents are extremely diverse in their ecology and lifestyles and can be found in almost every terrestrial habitat, including human-made environments. Species can be arboreal, fossorial (burrowing), saltatorial/ricochetal (leaping on their hind legs), or semiaquatic. However, all rodents share several morphological features, including having only a single upper and lower pair of ever-growing incisors. Well-known rodents include Mouse, mice, rats, squirrels, prairie dogs, porcupines, beavers, Cavia, guinea pigs, and hamsters. Once included wi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PADI4
Protein-arginine deiminase type-4, is a human protein which in humans is encoded by the ''PADI4'' gene. The protein as an enzyme, specifically protein-arginine deiminase, a type of hydrolase. Molecular biology The human gene is found on the short arm of Chromosome 1 near the telomere (1p36.13). It is located on the Watson (plus) strand and is 55,806 bases long. The protein is 663 amino acids long with a molecular weight of 74,095 Da. Function This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine to citrulline residues (citrullination). This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response. PADI4 plays a role in the epigenetics, the deimination of arginines on histones H3 and H4 can act antagonistically to arginine methylation. The protein may be found in oligomers and binds 5 calcium ions per subunit. It catalyses the reaction: * Protein L-arginine + H2O = protei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PADI3
Peptidyl arginine deiminase, type III, also known as PADI3, is a protein which in humans is encoded by the ''PADI3'' gene. This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type III enzyme modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation. Together with the type I enzyme, this enzyme may also play a role in terminal differentiation of the epidermis. This gene exists in a cluster with four other paralogous genes. See also *Protein-arginine deiminase In enzymology, a protein-arginine deiminase (PAD) () is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrull ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PADI2
Protein-arginine deiminase type-2 is an enzyme that in humans is encoded by the ''PADI2'' gene. This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post- translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous Sequence homology is the biological homology between DNA, RNA, or protein sequences, define ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PADI1
Peptidyl arginine deiminase, type I, also known as PADI1, is a protein which in humans is encoded by the ''PADI1'' gene. This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type I enzyme is involved in the late stages of epidermal differentiation, where it deiminates filaggrin and keratin K1, which maintains hydration of the stratum corneum, and hence the cutaneous barrier function. This enzyme may also play a role in hair follicle formation. This gene exists in a cluster with four other paralogous Sequence homology is the biological homology between DNA, RNA, or protein sequences, defined in terms of shared ancestry in the evolutionary history of life. Two segments of DNA can have shared ancestry because ... [...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] |
