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Nocturnin
Nocturnin is a human hydrolase enzyme that is involved in metabolism and its expression is controlled by the rhythmic circadian clock. It is encoded by the NOCT gene located on chromosome 4. Nocturnin contains a c-terminal structural domain of the Endonuclease/Exonuclease/phosphatase family. A study in January 2019, demonstrated that NADP+ and NADPH are the direct targets of Nocturnin. * The ''Drosophila melanogaster'' ortholog of Nocturnin is Curled. Knockouts of Curled lead to the curled wing phenotype in fruit flies. The curled wing phenotype was first discovered by Thomas Hunt Morgan in 1915. In mice the Nocturnin ortholog is responsible for controlling diet and weight-gain, knockout mice do not gain weight when placed on a high-fat diet, when compared to normal mice containing Nocturnin. In mice it has also been shown that Nocturnin is rhythmically expressed even when mice are placed in complete darkness, demonstrating that Nocturnin expression is driven by our body's i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NADP+
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP or, in older notation, TPN (triphosphopyridine nucleotide), is a Cofactor (biochemistry), cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). It is used by all forms of cellular life. NADPH is the redox, reduced form of NADP. NADP differs from NAD+, NAD by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine Moiety (chemistry), moiety. This extra phosphate is added by NAD+ kinase, NAD+ kinase and removed by NADP+ phosphatase. Biosynthesis NADP In general, NADP+ is synthesized before NADPH is. Such a reaction usually starts with NAD+, NAD+ from either the de-novo or the salvage pathway, with NAD+ kinase, NAD+ kinase adding the extra phosphate group. ADP-ribosyl cyclase allows for synthesis from nicotinamide in the salvage pathway, and NADP+ phosphatase ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NADPH
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). It is used by all forms of cellular life. NADPH is the reduced form of NADP. NADP differs from NAD by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety. This extra phosphate is added by NAD+ kinase and removed by NADP+ phosphatase. Biosynthesis NADP In general, NADP+ is synthesized before NADPH is. Such a reaction usually starts with NAD+ from either the de-novo or the salvage pathway, with NAD+ kinase adding the extra phosphate group. ADP-ribosyl cyclase allows for synthesis from nicotinamide in the salvage pathway, and NADP+ phosphatase can convert NADPH back to NADH to maintain a balance. Some forms of the NAD+ kinas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrolase
Hydrolase is a class of enzyme that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases. Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase, which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid. Acetic acid is an important metabolite in the body and a critical intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleotides. Hydrolase enzymes are important for the body because they have degra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Current Biology
''Current Biology'' is a biweekly peer-reviewed scientific journal that covers all areas of biology, especially molecular biology, cell biology, genetics, neurobiology, ecology, and evolutionary biology. The journal includes research articles, various types of review articles, as well as an editorial magazine section. The journal was established in 1991 by the Current Science group, acquired by Elsevier in 1998 and has since 2001 been part of Cell Press, a subdivision of Elsevier. According to ''Journal Citation Reports'', the journal has a 2020 impact factor The impact factor (IF) or journal impact factor (JIF) of an academic journal is a scientometric index calculated by Clarivate that reflects the yearly mean number of citations of articles published in the last two years in a given journal, as i ... of 10.834. It was categorized as a "high impact journal" by the Superfund Research Program. References External links * Biology journals English-language journals Cell ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CNOT6L
CCR4-NOT transcription complex subunit 6 like is a protein that in humans is encoded by the CNOT6L gene. It is a paralog of CNOT6 and therefore a potential subunit of the CCR4-Not Carbon Catabolite Repression—Negative On TATA-less, or CCR4-Not, is a multiprotein complex that functions in gene expression. The complex has multiple enzymatic activities as both a poly(A) 3′-5′ exonuclease and a ubiquitin ligase. The com ... deadenylase complex. References Further reading * * * * * * * * * {{gene-4-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PDE12
Phosphodiesterase 1, PDE1, EC 3.1.4.1, systematic name oligonucleotide 5′-nucleotidohydrolase) is a phosphodiesterase enzyme also known as calcium- and calmodulin-dependent phosphodiesterase. It is one of the 11 families of phosphodiesterase (PDE1-PDE11). Phosphodiesterase 1 has three subtypes, PDE1A, PDE1B and PDE1C which divide further into various isoforms. The various isoforms exhibit different affinities for cAMP and cGMP. Discovery The existence of the Ca2+-stimulated Phosphodiesterase 1 was first demonstrated by Cheung (1970), Kakiuchi and Yamazaki (1970) as a result of their research on bovine brain and rat brain respectively. It has since been found to be widely distributed in various mammalian tissues as well as in other eukaryotes. It is now one of the most intensively studied member of the PDE superfamily of enzymes, which today represents 11 gene families, and the best characterized one as well. Further research in the field along with increased availability of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TDP2
TDP or tdp may refer to: Computing * Thermal design power, a value describing the thermal limits of a computer system * Transparent Distributed Processing, network distributed architecture in the QNX operating system Politics *Telugu Desam Party, a regional political party in the South Indian states of Telangana and Andhra Pradesh *Territoires de progrès, a political movement in France *Socialist Democratic Party (Turkey), a former political party * Communal Democracy Party, a political party in Northern Cyprus *Democratic Party of Turks, a political party in Macedonia Science and medicine *TDaP, tetanus, diphtheria and pertussis vaccine * Thermal depolymerization, a process for converting biomass into oil *Thymidine diphosphate, a nucleotide *Thiamine pyrophosphate (thiamine diphosphate), an enzyme cofactor * Torsades de pointes, a form of cardiac arrhythmia *One or more isoforms of TARDBP, a TAR DNA-binding protein Other uses *Tour de Pologne (TdP), annual men's multiple-sta ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sphingomyelin Phosphodiesterase
Sphingomyelin phosphodiesterase (EC 3.1.4.12, also known as neutral sphingomyelinase, sphingomyelinase, or SMase; systematic name sphingomyelin cholinephosphohydrolase) is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Sphingomyelinase family Five types of SMase have been identified. These are classified according to their cation dependence and pH optima of action and are: * Lysosomal acid SMase * Secreted zinc-dependent acid SMase * Magnesium-dependent neutral SMase * Magnesium-independent neutral SMase * Alkaline SMase Of these, the lysosomal acidic SMase and the magnesium-dependent neutral SMase are considered major candidates for the production of ceramide in the cellular ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
INPP5B
Type II inositol-1,4,5-trisphosphate 5-phosphatase is an enzyme that in humans is encoded by the ''INPP5B'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... Cellular calcium signaling is controlled by the production of inositol phosphates (IPs) by phospholipase C in response to extracellular signals. The IP signaling molecules are inactivated by a family of inositol polyphosphate-5-phosphatases (5-phosphatases). This gene encodes the type II 5-phosphatase. The protein is localized to the cytosol and mitochondria, and associates with membranes through an isoprenyl modification near the C-terminus. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. References Furth ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AP Endonuclease
Apurinic/apyrimidinic (AP) endonuclease is an enzyme that is involved in the DNA base excision repair pathway (BER). Its main role in the repair of damaged or mismatched nucleotides in DNA is to create a nick in the phosphodiester backbone of the AP site created when DNA glycosylase removes the damaged base. There are four types of AP endonucleases that have been classified according to their mechanism and site of incision. Class I AP endonucleases () cleave 3′ to AP sites by a β-lyase mechanism, leaving an unsaturated aldehyde, termed a 3′-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5′-phosphate. Class II AP endonucleases incise DNA 5′ to AP sites by a hydrolytic mechanism, leaving a 3′-hydroxyl and a 5′-deoxyribose phosphate residue. Class III and class IV AP endonucleases also cleave DNA at the phosphate groups 3′ and 5′ to the baseless site, but they generate a 3′-phosphate and a 5′-OH. Humans have two AP endonucleases, APE1 and APE2. APE1 exhibits ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deoxyribonuclease I
Deoxyribonuclease I (usually called DNase I), is an endonuclease of the DNase family coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin. In addition to its role as a waste-management endonuclease, it has been suggested to be one of the deoxyribonucleases responsible for DNA fragmentation during apoptosis. DNase I binds to the cytoskeletal protein actin. It binds actin monomers with very high (sub-nanomolar) affinity and actin polymers with lower affinity. The function of this interaction is unclear. However, since actin-bound DNase I is enzymatically inactive, the DNase-actin complex might be a storage form of DNase I that prevents damage of the genetic information. This protein is store ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
