source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/Insulin%20receptor%20substrate%201 | Insulin receptor substrate 1 (IRS-1) is a signaling adapter protein that in humans is encoded by the IRS1 gene. It is a 131 kDa protein with amino acid sequence of 1242 residues. It contains a single pleckstrin homology (PH) domain at the N-terminus and a PTB domain ca. 40 residues downstream of this, followed by a poorly conserved C-terminus tail. Together with IRS2, IRS3 (pseudogene) and IRS4, it is homologous to the Drosophila protein chico, whose disruption extends the median lifespan of flies up to 48%. Similarly, Irs1 mutant mice experience moderate life extension and delayed age-related pathologies.
Function
Insulin receptor substrate 1 plays a key role in transmitting signals from the insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF-1) to intracellular pathways PI3K / Akt and Erk MAP kinase pathways. Tyrosine phosphorylation of IRS-1 by insulin receptor (IR) introduces multiple binding sites for proteins bearing SH2 homology domain, such as PI3K, Grb-2/Sos complex and SHP2. PI3K, involved in interaction with IRS-1, produces PIP3, which, in turn, recruits Akt kinase. Further, Akt kinase is activated via phosphorylation of its T308 residue and analogous sites in PKC by PDK1. This phosphorylation is absent in tissues lacking IRS-1. The cascade is followed by glucose uptake. Formation of the Grb-2/Sos complex, also known as the RAS guanine nucleotide exchange factor complex, results in ERK1/2 activation. IRS-1 signal transduction may be inhibited by |
https://en.wikipedia.org/wiki/SYK | SYK may refer to:
Helsingin Suomalainen Yhteiskoulu, middle and high school in Helsinki, Finland
South Yorkshire, county in England, Chapman code
Tyrosine-protein kinase SYK, an enzyme
Sachdev-Ye-Kitaev model |
https://en.wikipedia.org/wiki/Surif | Surif () is a Palestinian City in the Hebron Governorate located 25 km northwest of the city of Hebron. According to the Palestinian Central Bureau of Statistics census, Surif had a population of 17,287 in 2011. The population is entirely Muslim.
Most of the town's 15,000 dunams is used for agriculture, in particular, olives, wheat and barley. There are seven mosques and four schools located in its vicinity.
Ahmad Lafi is the mayor.
History
In 1838 Surif was noted as a Muslim village, located between Hebron and Gaza, but subjected to the government of Hebron.
In 1863 Victor Guérin found Surif to be a village with 700 inhabitants. He further noted that beside a birket in the rock, a few cisterns and an ancient column shaft which was placed near a small mosque, all of Surif's constructions seemed more or less modern.
An official Ottoman village list from about 1870 showed 87 houses and a population of 265, counting men only.
In 1883, the PEF's Survey of Western Palestine described Surif as "A small village on a low hill, with olives to the south."
In 1896 the population of Surif was estimated to be about 1164 persons.
British Mandate Era
According to the 1922 census of Palestine conducted by the British Mandate authorities, Surif had a population of 1,265 inhabitants, all Muslims, increasing in the 1931 census to 1,640, in 344 inhabited houses.
In the 1945 statistics the population of Surif was 2,190, all Muslims, with a total of 38,876 dunams of land acc |
https://en.wikipedia.org/wiki/Grothendieck%27s%20connectedness%20theorem | In mathematics, Grothendieck's connectedness theorem , states that if A is a complete Noetherian local ring whose spectrum is k-connected and f is in the maximal ideal, then Spec(A/fA) is (k − 1)-connected. Here a Noetherian scheme is called k-connected if its dimension is greater than k and the complement of every closed subset of dimension less than k is connected.
It is a local analogue of Bertini's theorem.
See also
Zariski connectedness theorem
Fulton–Hansen connectedness theorem
References
Bibliography
Theorems in algebraic geometry |
https://en.wikipedia.org/wiki/Norpethidine | Norpethidine (normeperidine, pethidine intermediate B) is a 4-phenylpiperidine derivative that is both a precursor to, and the toxic metabolite of, pethidine (meperidine). It is scheduled by UN Single Convention on Narcotic Drugs. It is a Schedule II Narcotic controlled substance in the United States and has an ACSCN of 9233. The 2014 annual manufacturing quota was .
Norpethidine is a controlled drug because of its potential uses in manufacturing both pethidine itself and a range of N-substituted derivatives, but it has little opioid activity in its own right. Instead, norpethidine acts as a stimulant and causes convulsions.
Bioaccumulation of norpethidine is a major complication when pethidine is used in medicine as an analgesic, as when pethidine is used in high doses or administered by intravenous infusion, norpethidine can accumulate in the body at a faster rate than it is being excreted, particularly in elderly patients or those with compromised liver or kidney function, resulting in a range of toxic effects, mainly convulsions, but also myoclonus and hyponatremia. These complications can be serious and have sometimes resulted in death.
Metabolism of pethidine to norpethidine is carried out mainly by the CYP enzymes, CYP2B6, CYP2C19 and CYP3A4, in the liver, and since the activity of these enzymes can vary between individuals and can be influenced by concurrent use of other drugs, the rate and extent of norpethidine production can be difficult to predict.
Norpet |
https://en.wikipedia.org/wiki/Jeler%C4%83u | The Jelerău is a left tributary of the river Cerna in Romania. It flows into the Cerna in the town Băile Herculane. Its length is and its basin size is .
References
Rivers of Romania
Rivers of Caraș-Severin County |
https://en.wikipedia.org/wiki/NXF1 | Nuclear RNA export factor 1, also known as NXF1 or TAP, is a protein which in humans is encoded by the NXF1 gene.
Function
This gene is one member of a family of nuclear RNA export factor genes. Common domain features of this family are a noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain that allows heterodimerization with NTF2-related export protein-1 (NXT1), and a ubiquitin-associated domain that mediates interactions with nucleoporins. Alternative splicing results in transcript variants. The LRRs and NTF2-like domains are required for export activity. The encoded protein of this gene shuttles between the nucleus and the cytoplasm and binds in vivo to poly(A)+ RNA. It is the vertebrate homologue of the yeast protein Mex67p. The encoded protein overcomes the mRNA export block caused by the presence of saturating amounts of CTE (constitutive transport element) RNA of type D retroviruses. A variant allele of the homologous Nxf1 gene in mice suppresses a class of mutations caused by integration of an endogenous retrovirus (intracisternal A particle) into an intron.
Interactions
NXF1 has been shown to interact with TNPO2, MAGOH, U2 small nuclear RNA auxiliary factor 1, DHX9, HuD and NUP214.
Tap protein
In molecular biology, another name for the protein NXF1 is TAP. In particular this entry focuses on the C-terminal domain, which also contains the UBA (protein domain).
This entry contains the NXF |
https://en.wikipedia.org/wiki/MFN2 | Mitofusin-2 is a protein that in humans is encoded by the MFN2 gene. Mitofusins are GTPases embedded in the outer membrane of the mitochondria. In mammals MFN1 and MFN2 are essential for mitochondrial fusion. In addition to the mitofusins, OPA1 regulates inner mitochondrial membrane fusion, and DRP1 is responsible for mitochondrial fission.
Mitofusin-2 (MFN2) is a mitochondrial membrane protein that plays a central role in regulating mitochondrial fusion and cell metabolism. More specifically, MFN2 is a dynamin-like GTPase embedded in the outer mitochondrial membrane (OMM) which in turn affects mitochondrial dynamics, distribution, quality control, and function.
In addition to the MFN2, OPA1 regulates inner mitochondrial membrane fusion, MFN1 is a mediator of mitochondrial fusion and DRP1 is responsible for mitochondrial fission.
Structure
The human mitofusin-2 protein contains 757 amino acid residues. The MFN2 comprises a large cytosolic GTPase domain at the N-terminal, followed by a coiled-coil heptad-repeat (HR1) domain, a proline-rich (PR) region, two sequential transmembrane (TM) domains crossing the OMM and a second cytosolic heptad-repeat (HR2) domain at the C-terminal. MFN2 has been shown by electron microscopy (EM) to accumulate in contact regions between adjacent mitochondria, supporting their role in mitochondrial fusion. Seminal studies revealed that both, MFN1 and MFN2 spanning from the OMM of two opposing mitochondria, physically interact in trans, by the f |
https://en.wikipedia.org/wiki/STIM1 | Stromal interaction molecule 1 is a protein that in humans is encoded by the STIM1 gene. STIM1 has a single transmembrane domain, and is localized to the endoplasmic reticulum, and to a lesser extent to the plasma membrane.
Even though the protein has been identified earlier, its function was unknown until recently. In 2005, it was discovered that STIM1 functions as a calcium sensor in the endoplasmic reticulum. Upon activation of the IP3 receptor, the calcium concentration in the endoplasmic reticulum decreases, which is sensed by STIM1, via its EF hand domain. STIM1 activates the "store-operated" ORAI1 calcium ion channels in the plasma membrane, via intracellular STIM1 movement, clustering under plasma membrane and protein interaction with ORAI isoforms. STIM1-mediated calcium entry is required for thrombin-induced disassembly of VE-cadherin adherens junctions. 2-Aminoethoxydiphenyl borate (2-APB) and 4-chloro-3-ethylphenol (4-CEP) cause STIM1 clustering in a cell and prevent STIM1 moving toward plasma membrane.
Interactions
STIM1 has been shown to interact with ORAI1, TMEM110 (STIMATE), SERCA, TMEM66 (SARAF), and STIM2.
References |
https://en.wikipedia.org/wiki/John%20Milton%20Miller | John Milton Miller (June 22, 1882 – May 17, 1962) was a noted American electrical engineer, best known for discovering the Miller effect and inventing fundamental circuits for quartz crystal oscillators (Miller oscillators).
Formative years and family
Miller was born in Hanover, Pennsylvania on June 22, 1882. In 1904, he graduated from Yale University. He then obtained his M.A. there in 1907, followed by his Ph.D. in Physics in 1915.
He married Frances Riley; the couple had seven children — two girls and five boys.
Career
From 1907 to 1919, Miller was employed as a physicist with the National Bureau of Standards; he then worked as a radio engineer at the United States Navy's Radio Laboratory in Anacostia, District of Columbia from 1919 to 1923, and subsequently at the Naval Research Laboratory (NRL). From 1925 to 1936, he led radio receiver research at the Atwater Kent Manufacturing Company, Philadelphia. From 1936 to 1940, he was the assistant head of the research laboratory for the RCA Radiotron Company. In 1940, he returned to NRL where he became superintendent of Radio I Division (1945), associate director of research (1951), and scientific research administrator (1952).
Honors
Miller was awarded the Distinguished Civilian Service Award in 1945 for "initiation of the development of a new flexible radio-frequency cable urgently needed in radio and radar equipment which solved a desperate material shortage in the United States during World War II," and the IRE Medal of |
https://en.wikipedia.org/wiki/Pethidinic%20acid | Pethidinic acid (meperidinic acid, pethidine intermediate C) is a 4-phenylpiperidine derivative that is both a metabolite of and a precursor to pethidine (meperidine). It is scheduled by UN Single Convention on Narcotic Drugs. It is a Schedule II Narcotic controlled substance in the United States and has an ACSCN of 9234. The 2014 annual manufacturing quota was 6 grams.
Pethidinic acid is a controlled drug because of its potential uses in manufacturing both pethidine itself and some of its substituted derivatives, but it has little opioid activity in its own right. Metabolism of pethidine to pethidinic acid is carried out mainly by the carboxylesterase enzyme hCE-1 in the liver, and since the activity of this enzyme can vary between individuals, the rate and extent of pethidinic acid production can vary.
Frank Wätjen used pethidinic acid as a precursor chemical to a heterocyclic moiety.
See also
Moramide intermediate
Methadone intermediate
Pethidine intermediate A
Pethidine intermediate B (norpethidine)
References
Synthetic opioids
4-Phenylpiperidines
Gamma-Amino acids
Human drug metabolites |
https://en.wikipedia.org/wiki/Benzethidine | Benzethidine is a 4-phenylpiperidine derivative that is related to the clinically used opioid analgesic drug pethidine (meperidine, or Demerol).
Benzethidine is not currently used in medicine and is a Class A/Schedule I drug which is controlled under UN drug conventions. It has similar effects to other opioid derivatives, such as analgesia, sedation, nausea and respiratory depression. In the United States, the drug is a Schedule I Narcotic Controlled Substance with a DEA ACSCN of 9606 and 2014 annual aggregate manufacturing quota of nil. The most common salt in use is the hydrochloride, free base conversion ratio of 0.910.
Legal Status
Australia
Benzethidine is considered a Schedule 9 prohibited substance in Australia under the Poisons Standard (February 2017). A Schedule 9 substance is a substance which may be abused or misused, the manufacture, possession, sale or use of which should be prohibited by law except when required for medical or scientific research, or for analytical, teaching or training purposes with approval of Commonwealth and/or State or Territory Health Authorities.
References
External links
UNODC Bulletin on Narcotics 1961
Synthetic opioids
4-Phenylpiperidines
Ethers
Carboxylate esters
Mu-opioid receptor agonists
Ethyl esters |
https://en.wikipedia.org/wiki/Die%20shrink | The term die shrink (sometimes optical shrink or process shrink) refers to the scaling of metal–oxide–semiconductor (MOS) devices. The act of shrinking a die creates a somewhat identical circuit using a more advanced fabrication process, usually involving an advance of lithographic nodes. This reduces overall costs for a chip company, as the absence of major architectural changes to the processor lowers research and development costs while at the same time allowing more processor dies to be manufactured on the same piece of silicon wafer, resulting in less cost per product sold.
Die shrinks are the key to lower prices and higher performance at semiconductor companies such as Samsung, Intel, TSMC, and SK Hynix, and fabless manufacturers such as AMD (including the former ATI), NVIDIA and MediaTek.
Details
Examples in the 2000s include the downscaling of the PlayStation 2's Emotion Engine processor from Sony and Toshiba (from 180 nm CMOS in 2000 to 90 nm CMOS in 2003), the codenamed Cedar Mill Pentium 4 processors (from 90 nm CMOS to 65 nm CMOS) and Penryn Core 2 processors (from 65 nm CMOS to 45 nm CMOS), the codenamed Brisbane Athlon 64 X2 processors (from 90 nm SOI to 65 nm SOI), various generations of GPUs from both ATI and NVIDIA, and various generations of RAM and flash memory chips from Samsung, Toshiba and SK Hynix. In January 2010, Intel released Clarkdale Core i5 and Core i7 processors fabricated with a 32 nm process, down from a previous 45 nm process used in olde |
https://en.wikipedia.org/wiki/Etoxeridine | Etoxeridine (Carbetidine, Atenos) is a 4-phenylpiperidine derivative that is related to the clinically used opioid analgesic drug pethidine (meperidine).
Etoxeridine was developed in the 1950s and investigated for use in surgical anesthesia, however it was never commercialized and is not currently used in medicine. As with other opioids which were not in clinical use during the drafting of the Controlled Substances Act, it is categorized as a Schedule I narcotic.
References
Synthetic opioids
4-Phenylpiperidines
Primary alcohols
Ethers
Mu-opioid receptor agonists
Ethyl esters |
https://en.wikipedia.org/wiki/XDNA%20%28multi-graphics%29 | The xDNA technology is a technology designed by Diamond Multimedia, allowing motherboards which are not certified for ATI CrossFire (for instance, nForce 500/600 series motherboards designed by Nvidia) to install multiple ATI Radeon video cards (up to four) as a CrossFire setup and operate in rendering modes which are exclusively made for CrossFire setups. Diamond Multimedia will provide optimized Catalyst drivers and middleware for the platform in a single package.
See also
SLI
References
External links
Diamond Multimedia website
Graphics cards |
https://en.wikipedia.org/wiki/Range%20Fuels | Range Fuels was a company that tried to develop technology for the conversion of biomass into ethanol without the use of enzymes. The technology employed was biomass gasification followed by syngas conversion over heterogeneous molybdenum-based catalysts to a mixture of aliphatic alcohols. The company began in 2006 as Kergy and changed its name to Range Fuels in 2007. The company broke ground on its first commercial-scale cellulosic ethanol facility in November 2007.
According to the Washington Examiner, Range Fuels' Soperton, GA plant closed down in January 2011 after receiving a $76 million grant from the US Department of Energy, $6 million from the State of Georgia, and an $80 million loan guaranteed by the U.S. Biorefinery Assistance Program.
Range Fuel officially closed down in late 2011 with a foreclosure sale of its plant held on 3 January 2012.
The facility was sold to New Zealand-based start-up LanzaTech in 2012 for $5.4 million and renamed the Freedom Pines Biorefinery. Unlike Range Fuels, LanzaTech will use microbes to transform the gas into ethanol; a byproduct to their process is butanediol. Both products can be formulated into jet fuel with assistance from LanzaTech partner firms. Lanzatech is also a Vinod Khosla-funded venture.
References
External links
U.S. Dept. of Energy: Biomass topics
Alcohol fuel producers
Defunct energy companies of the United States
Defunct companies based in Colorado
Companies based in Broomfield, Colorado
Renewable resource |
https://en.wikipedia.org/wiki/Giordano%20Vitale | Giordano Vitale or Vitale Giordano (October 15, 1633 – November 3, 1711) was an Italian mathematician. He is best known for his theorem on Saccheri quadrilaterals. He may also be referred to as Vitale Giordani, Vitale Giordano da Bitonto, and simply Giordano.
Life
Giordano was born in Bitonto, in southeastern Italy, probably on October 15, 1633. As an adolescent he left (or was forced to leave) his city and, after an adventurous youth (that included killing his brother-in-law for calling him lazy) he became a soldier in the Pontifical army. During these adventures he read his first book of mathematics, the Aritmetica prattica by Clavius. At twenty-eight, living in Rome, he decided to devote himself to mathematics. The most important book he studied was Euclid's Elements in the Italian translation by Commandino.
In Rome he made acquaintance with the renowned mathematicians Giovanni Borelli and Michelangelo Ricci, who became his friends. He was employed for a year as a mathematician by ex-Queen Christina of Sweden during her final stay in Rome. In 1667, a year after its foundation by Louis XIV, he became a lecturer in mathematics at the French Academy in Rome, and in 1685 he gained the chair of mathematics at the prestigious Sapienza University of Rome. Friend of Vincenzo Viviani, Giordano met Leibniz in Rome when Leibniz stayed there during his journey through Italy in the years 1689–90. He gave Leibniz a copy of the second edition of his book Euclide restituto. Giordano die |
https://en.wikipedia.org/wiki/Kevin%20Delaney | Kevin Delaney is an American voice actor, who is best known for voicing Edna Mode in Disney Infinity, Captain Marvel in Mortal Kombat vs. DC Universe and Ryuji Keikain in Nura: Rise of the Yokai Clan: Demon Capital. He also provided additional voices for Looney Tunes: Stranger Than Fiction, Looney Tunes: Reality Check, and Lightning Returns: Final Fantasy XIII.
Filmography
Anime
Nura: Rise of the Yokai Clan - Demon Capital - Ryuji Keikain (2013)
Video games
Agatha Christie: Evil Under the Sun - Hercule Poirot
Anvil of Dawn - Court Magician, Book Thing, Second in Command
Chronomaster - Fortune Teller
Disney's Chicken Little: Ace in Action - Space Goosey Lucy
Disney Infinity - Edna Mode
Dracula: Origin - Abraham Van Helsing, Dracula
Earth Defense Force 2025 - Soldier
Experience112 - Mike Loyd
Galactic Bowling - Sasquatch
Kingdom Hearts II - Tournament Announcer
Lightning Returns: Final Fantasy XIII - Additional Voices
Math Blaster: Master the Basics - Cyclotron X, Tribal Leader, Announcer
The Matrix: Path of Neo - Theater Heckler, SWAT, Army Soldier
Mortal Kombat vs. DC Universe - Captain Marvel
Sanitarium - Scotty Havel, Hector Vasquez, Frank Rizzo, Ometoch, Priest, Newscaster
Tarr Chronicles - Captain Eric Heriot
Watchmen: The End Is Nigh - Mercenary
World of Warcraft: Wrath of the Lich King - Varos Cloudstrider, Skarvald the Constructor, Slad'ran, XT-002 Deconstructor
Other
Search For the Lost Giants - Narrator
Looney Tunes - Various
Movies
50 Ways |
https://en.wikipedia.org/wiki/Diffusiophoresis%20and%20diffusioosmosis | Diffusiophoresis is the spontaneous motion of colloidal particles or molecules in a fluid, induced by a concentration gradient of a different substance. In other words, it is motion of one species, A, in response to a concentration gradient in another species, B. Typically, A is colloidal particles which are in aqueous solution in which B is a dissolved salt such as sodium chloride, and so the particles of A are much larger than the ions of B. But both A and B could be polymer molecules, and B could be a small molecule. For example, concentration gradients in ethanol solutions in water move 1 μm diameter colloidal particles with diffusiophoretic velocities of order 0.1 to 1 μm/s, the movement is towards regions of the solution with lower ethanol concentration (and so higher water concentration). Both species A and B will typically be diffusing but diffusiophoresis is distinct from simple diffusion: in simple diffusion a species A moves down a gradient in its own concentration.
Diffusioosmosis, also referred to as capillary osmosis, is flow of a solution relative to a fixed wall or pore surface, where the flow is driven by a concentration gradient in the solution. This is distinct from flow relative to a surface driven by a gradient in the hydrostatic pressure in the fluid. In diffusioosmosis the hydrostatic pressure is uniform and the flow is due to a concentration gradient.
Diffusioosmosis and diffusiophoresis are essentially the same phenomenon. They are both relative m |
https://en.wikipedia.org/wiki/Crystal%20skull%20%28disambiguation%29 | Crystal skull refers to a number of human-like skull carvings made of quartz crystal and their associated myth and research.
Crystal skull may also refer to:
The Crystal Skull (video game), a 1996 adventure game
Crystal Skull (Stargate SG-1), an episode of the TV show Stargate SG-1
Indiana Jones and the Kingdom of the Crystal Skull, the fourth movie in the Indiana Jones franchise.
"Crystal Skull", a single by Mastodon from the album Blood Mountain
See also
Skull (disambiguation) |
https://en.wikipedia.org/wiki/Craiova%20%28Cerna%29 | The Craiova is a right tributary of the river Cerna in Romania. It flows into the Cerna downstream from Cerna-Sat. Its length is and its basin size is .
References
Rivers of Romania
Rivers of Caraș-Severin County |
https://en.wikipedia.org/wiki/Dose%20dumping | Dose dumping is a phenomenon of drug metabolism in which environmental factors can cause the premature and exaggerated release of a drug. This can greatly increase the concentration of a drug in the body and thereby produce adverse effects or even drug-induced toxicity.
Dose dumping is most commonly seen in drugs taken by mouth and digested in the gastrointestinal tract. Around the same time patients take their medication, they can also ingest other substances like fatty meals or alcohol that increase drug delivery. The substances may act on the drug's capsule to speed up drug release, or they may stimulate the body's absorptive surfaces to increase the rate of drug uptake.
Dose dumping is a disadvantage found in extended release dosage form.
In general, drug companies try to avoid drugs with significant dose dumping effects. Such drugs are prone to problems and are often pulled from the market. Such was the case with the pain medication Palladone Once Daily formulation due to its dose-dumping effects when taken with alcohol.
Types of dose dumping
Alcohol-induced dose dumping (AIDD)
It is by definition an unintended rapid release in large amounts of a modified-release dosage due to a co-ingestion with ethanol.
Some interactions between alcohol, biological factors and the presentation of the drug can influence the apparition of AIDD by:
Disrupting the drug release mechanism.
Prolonging gastric emptying.
Changing the amount of gastric acid.
Enhancing the drug absor |
https://en.wikipedia.org/wiki/Iauna | The Iauna is a right tributary of the river Cerna in Romania. It discharges into the Cerna near Țațu. Its length is and its basin size is .
References
Rivers of Romania
Rivers of Caraș-Severin County |
https://en.wikipedia.org/wiki/Pris%C4%83cina | The Prisăcina is a right tributary of the river Cerna in Romania. It flows into the Cerna near Cracu Mare. Its length is and its basin size is .
References
Rivers of Romania
Rivers of Caraș-Severin County |
https://en.wikipedia.org/wiki/SMK%20box%20riboswitch | The SMKbox riboswitch (also known as SAM-III) is an RNA element that regulates gene expression in bacteria. The SMK box riboswitch is found in the 5' UTR of the MetK gene in lactic acid bacteria. The structure of this element changes upon binding to S-adenosyl methionine (SAM) to a conformation that blocks the shine-dalgarno sequence and blocks translation of the gene.
There are other known SAM-binding riboswitches such as SAM-I and SAM-II, but these appear to share no similarity in sequence or structure to SAM-III.
Structure
The crystal structure of the riboswitch from E. faecalis was solved by X-ray crystallography. The structure showed that the most conserved nucleotides involved in SAM binding were organised around a junction between three helices. In some species there are large insertions of up to 210 nucleotides within this structure.
See also
SAH riboswitch
SAM-I riboswitch
SAM-II riboswitch
SAM-IV riboswitch
SAM-V riboswitch
SAM-VI riboswitch
SAM-Chlorobi RNA motif
SAM–SAH riboswitch
References
External links
Cis-regulatory RNA elements
Riboswitch |
https://en.wikipedia.org/wiki/Belareca | The Belareca or Bela Reca is a right tributary of the river Cerna in Romania. It discharges into the Cerna near the town Băile Herculane. Its length is and its basin size is .
References
Rivers of Romania
Rivers of Caraș-Severin County |
https://en.wikipedia.org/wiki/Craiova%20%28disambiguation%29 | Craiova may refer to the following places in Romania:
Craiova, a city, capital of Dolj County
Craiova (Cerna), a tributary of the Cerna in Caraș-Severin County
Craiova, another name for the river Globu in Caraș-Severin County |
https://en.wikipedia.org/wiki/Furethidine | Furethidine is a 4-phenylpiperidine derivative that is related to the clinically used opioid analgesic drug pethidine (meperidine), but with around 25x higher potency. According to another source, Furethidine is 500/30 = 16.7 x the potency of pethidine (table VII).
Furethidine is not currently used in medicine and is a Class A/Schedule I drug which is controlled under UN drug conventions. It has similar effects to other opioid derivatives, such as analgesia, sedation, nausea and respiratory depression. In the United States it is a Schedule I Narcotic controlled substance with the ACSCN of 9626.
References
External links
UNODC Bulletin on Narcotics 1961
Synthetic opioids
Tetrahydrofurans
4-Phenylpiperidines
Carboxylate esters
Ethyl esters
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/Morpheridine | Morpheridine (Morpholinoethylnorpethidine) is a 4-phenylpiperidine derivative that is related to the clinically used opioid analgesic drug pethidine (meperidine). It is a strong analgesic with around 4 times the potency of pethidine, and unlike pethidine, does not cause convulsions, although it produces the standard opioid side effects such as sedation and respiratory depression.
Morpheridine is not currently used in medicine and is a Schedule I drug which is controlled under UN drug conventions.
Synthesis
The key intermediate, normeperidine, is obtained by a scheme closely akin to the parent molecule. Thus, alkylation of benzyl cyanide (1) with the tosyl analog of the bischloroethylamine (2) leads to the substituted piperidine (3). Basic hydrolysis serves to convert the nitrile to the acid (4). Treatment of this last with sulfuric acid in ethanol serves both to esterify the acid and to remove the tosyl group to yield the secondary amine (5).
Alkylation of that amine by means of N-(2-chloroethyl)morpholine gives morpheridine.
See also
Anileridine
Furethidine
Carbetidine
References
4-Phenylpiperidines
Analgesics
Ethyl esters
4-Morpholinyl compounds
Mu-opioid receptor agonists
Synthetic opioids |
https://en.wikipedia.org/wiki/List%20of%20Egyptian%20pyramids | This list presents the vital statistics of the pyramids listed in chronological order, when available.
See also
Egyptian pyramids
Great Sphinx of Giza
Lepsius list of pyramids
List of Egyptian pyramidia
List of finds in Egyptian pyramids
List of the oldest buildings in the world
Umm El Qa'ab
References and notes
Bibliography
Pyramids, Egyptian
Pyramids
Pyramids in Egypt |
https://en.wikipedia.org/wiki/Pheneridine | Pheneridine is a 4-Phenylpiperidine derivative that is related to the opioid analgesic drug pethidine (meperidine).
Pheneridine is not currently used in medicine. Presumably it has similar effects to other opioid derivatives, such as analgesia, sedation, nausea and respiratory depression, however unlike most opioid derivatives it is not specifically listed as an illegal drug, although it would probably be regarded as a controlled substance analogue of pethidine on the grounds of its related chemical structure in some jurisdictions such as the United States, Canada and Australia, and would be classified as a "Pethidine Analogue" under the New Zealand Misuse of Drugs Act Class C7.
See also
Anileridine
PEPAP
Diphenoxylate
Pethidine
References
Synthetic opioids
4-Phenylpiperidines
Carboxylate esters
Mu-opioid receptor agonists
Phenethylamines |
https://en.wikipedia.org/wiki/Ecotoxicity | Ecotoxicity, the subject of study in the field of ecotoxicology (a portmanteau of ecology and toxicology), refers to the biological, chemical or physical stressors that affect ecosystems. Such stressors could occur in the natural environment at densities, concentrations, or levels high enough to disrupt natural biochemical and physiological behavior and interactions. This ultimately affects all living organisms that comprise an ecosystem.
Ecotoxicology has been defined as a branch of toxicology that focuses on the study of toxic effects, caused by natural or synthetic pollutants. These pollutants affect animals (including humans), vegetation, and microbes, in an intrinsic way.
Acute vs. chronic ecotoxicity
According to Barrie Peake in their paper “Impact of Pharmaceuticals on the Environment.”, The ecotoxicity of chemicals can be described based on the amount of exposure to any hazardous materials. There are two categories of ecotoxicity founded off of this description: acute toxins and chronic toxins (Peake, 2016). Acute ecotoxicity refers to the detrimental effects resulting from a hazardous exposure for no more than 15 days. Acute ecotoxicity is the direct result from the interaction of a chemical hazard with cell membranes of an organism (Peake, 2016). This interaction often leads to cell or tissue damage or death. Chronic ecotoxicity on the other hand are the detrimental effects resulting from a hazardous exposure of 15 days, to possibly years (Peake, 2016). Chronic |
https://en.wikipedia.org/wiki/Oxpheneridine | Oxpheneridine is a 4-phenylpiperidine derivative that is related to the opioid analgesic drug pethidine (meperidine).
Oxpheneridine is not currently used in medicine. Presumably it has similar effects to other opioid derivatives, such as analgesia, sedation, nausea and respiratory depression.
Unlike most opioid derivatives, oxpheneridine is not specifically listed as an illegal drug. In the UNODC narcotics report of 1958, they state that it was not possible to administer oxpheneridine in high doses as it is poorly soluble and highly irritating, and at the low doses administered it did not produce addiction in animals. This appears to be the only time oxpheneridine has been investigated, and so its pharmacological properties have not been well established.
Oxpheneridine would probably be regarded as a controlled substance analogue of pethidine on the grounds of its related chemical structure in some jurisdictions such as the United States, Australia and New Zealand.
In Canada, Oxpheneridine is specifically excluded from the illegal drugs list on the Controlled Drugs and Substances Act schedules, presumably on the basis of the lack of addictive potential found by the UNODC.
See also
Opioid
Meperidine
Pheneridine
Fentanyl
Carbamethidine
References
UNODC Bulletin on Narcotics 1958
Canadian Controlled Drug Schedules
Synthetic opioids
4-Phenylpiperidines
Secondary alcohols
Phenylethanolamines
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/List%20of%20Norwich%20City%20F.C.%20records%20and%20statistics | This is a list of the most notable Norwich City F.C. club records.
Players
Appearances
Kevin Keelan holds the record for Norwich City appearances, having played 673 first-team matches between 1963 and 1980.
Goals
Ralph Hunt holds the record for the most League goals scored in a season, 31 in the 1955–56 season in Division Three (South).
Johnny Gavin the top scorer over a career - 122 between 1948 and 1955.
Transfers
The highest transfer fee received for a Norwich City player is approximately £33 million for Emiliano Buendia (to Aston Villa) in June 2021,
Most spent by the club on a player was £9.1 million for Steven Naismith from Everton in 2016.
Matches
The club's widest victory margin in the league was their 10–2 win against Coventry City in the Division Three (South) in 1930. Their heaviest defeat in the league was 10–2 against Swindon Town in 1908 in the Southern Football League.
Norwich's record home attendance is 43,984 for a sixth round FA Cup match against Leicester City on 30 March 1963. With the introduction of regulations enforcing all-seater stadiums, it is unlikely that this record will be beaten in the foreseeable future, as Carrow Road's capacity is currently 27,224.
Seasons
The club's highest league finish was third in the FA Premiership in 1992–93. The club has won the League Cup twice (most recently in 1985) and also reached the FA Cup semi-final three times, most recently in 1992. Norwich have taken part in European competition just once, reaching |
https://en.wikipedia.org/wiki/Secarecytosis | Secarecytosis is a process involved in the development of a bird's lung cells, before the bird hatches from its egg. It is the processes of cell cutting during attenuation of the tubular epithelium of the developing avian lung. The word secarecytosis is derived from the Latin word secare which means "to cut".
Secarecytosis differs from holocrine and apocrine secretory mechanisms in that it occurs only during development and that portions of cells, complete with their organelles, are lost. It has three documented phenotypes. These are:
formation of a double cell membrane and separation between the two membranes;
formation of large vacuoles in the supranuclear cytoplasm, their subsequent fusion with each other and with the lateral cell membranes thus separating the apical portion;
formation of many tiny vesicles that fuse with each other and the cell membrane thus severing portions of the cell.
The process was initially described in the domestic chicken but it has also been shown to occur in the ostrich.
References
Bird anatomy |
https://en.wikipedia.org/wiki/Sonomicrometry | Sonomicrometry is a technique of measuring the distance between piezoelectric crystals based on the speed of acoustic signals through the medium they are embedded in. Typically, the crystals will be coated with an epoxy 'lens' and placed into the material facing each other. An electrical signal sent to either crystal will be transformed into sound, which passes through the medium, eventually reaching the other crystal, which converts the sound into electricity, detected by a receiver. From the time taken for sound to move between the crystals and the speed of sound in the medium, the distance between the crystals can be calculated.
History
Sonomicrometry was originally applied in the study of cardiac function in research animals by Dean Franklin in 1956, and was quickly adopted by biologists working in biomechanics as well as other physiological organ systems and structures (gastro-intestinal, uro-genital and musculo-skeletal). Medical device companies also use sonomicrometry to assess the physical performance, durability and longevity of devices during R&D phase of development. Sonomicrometry is currently the most prevalent method for determining muscle length changes during animal locomotion, feeding, and other biomechanical functions.
When originally developed decades ago, care was taken to orient the crystals correctly to ensure satisfactory signal detection between the crystals, but more modern versions of sonomicrometer hardware (typically dating from 1995 to the |
https://en.wikipedia.org/wiki/Advanced%20superionic%20conductor | An advanced superionic conductor (AdSIC) in materials science, is fast ion conductor that has a crystal structure close to optimal for fast ion transport (FIT).
History
The term was introduced in a paper by A.L. Despotuli, A.V. Andreeva and B. Rambaby.
Characteristics
The rigid ion sublattice of Advanced SuperIonic Conductors (AdSICs) has structure channels where mobile ions of opposite sign migrate. Their ion-transport characteristics display ionic conductivity of ~0.3/Ω cm (RbAg4I5, 300 K) and activation energy of Ei~0.1 eV. This determines the temperature-dependent concentration of mobile ions ni~Ni x eEi/kBT capable to migrate in conduction channels at each moment (Ni~1022/cm3, ni~2x1020/cm3, 300 K).
The Rubidium silver iodide–family is a group of AdSIC compounds and solid solutions that are isostructural with the RbAg4I5 alpha modification. Examples of such compounds with mobile Ag+- and Cu+-cations include KAg4I5, NH4Ag4I5, K1−xCsxAg4I5, Rb1−xCsxAg4I5, CsAg4Br1−xI2+x, CsAg4ClBr2I2, CsAg4Cl3I2, RbCu4Cl3I2 and KCu4I5.
RbAg4I5 AdSIC displays peculiar features of crystal structure and dynamics of mobile ions.
Recently, all solid state micrometre-sized supercapacitors based on AdSICs (nanoionic supercapacitors) had been recognized as critical electron component of future sub-voltage and deep-sub-voltage nanoelectronics and related technologies (22 nm technological node of CMOS and beyond). Researchers also developed an all-solid-state battery employing RbAg4I5 superio |
https://en.wikipedia.org/wiki/Notch%201 | Neurogenic locus notch homolog protein 1 (Notch 1) is a protein encoded in humans by the NOTCH1 gene. Notch 1 is a single-pass transmembrane receptor.
Function
This gene encodes a member of the Notch family. Members of this Type 1 transmembrane protein family share structural characteristics including an extracellular domain consisting of multiple epidermal growth factor-like (EGF) repeats, and an intracellular domain consisting of multiple, different domain types. Notch family members play a role in a variety of developmental processes by controlling cell fate decisions. The Notch signaling network is an evolutionarily conserved intercellular signaling pathway that regulates interactions between physically adjacent cells. In Drosophila, notch interaction with its cell-bound ligands (delta, serrate) establishes an intercellular signaling pathway that plays a key role in development. Homologues of the notch-ligands have also been identified in humans, but precise interactions between these ligands and the human notch homologues remain to be determined. This protein is cleaved in the trans-Golgi network, and presented on the cell surface as a heterodimer. This protein functions as a receptor for membrane bound ligands, and may play multiple roles during development.
A deficiency can be associated with bicuspid aortic valve.
There is evidence that activated Notch 1 and Notch 3 promote differentiation of progenitor cells into astroglia. Notch 1, when activated before birth, |
https://en.wikipedia.org/wiki/PAK1 | Serine/threonine-protein kinase PAK 1 is an enzyme that in humans is encoded by the PAK1 gene.
PAK1 is one of six members of the PAK family of serine/threonine kinases which are broadly divided into group I (PAK1, PAK2 and PAK3) and group II (PAK4, PAK6 and PAK5/7). The PAKs are evolutionarily conserved. PAK1 localizes in distinct sub-cellular domains in the cytoplasm and nucleus. PAK1 regulates cytoskeleton remodeling, phenotypic signaling and gene expression, and affects a wide variety of cellular processes such as directional motility, invasion, metastasis, growth, cell cycle progression, angiogenesis. PAK1-signaling dependent cellular functions regulate both physiologic and disease processes, including cancer, as PAK1 is widely overexpressed and hyperstimulated in human cancer, at-large.
Discovery
PAK1 was first discovered as an effector of the Rho GTPases in rat brain by Manser and colleagues in 1994. The human PAK1 was identified as a GTP-dependent interacting partner of Rac1 or Cdc42 in the cytosolic fraction from neutrophils, and its complementary DNA was cloned from a human placenta library by Martin and Colleagues in 1995.
Function
PAK proteins are critical effectors that link the Rho family of GTPases (Rho GTPases) to cytoskeleton reorganization and nuclear signaling. PAK proteins, a family of serine/threonine p21-activated kinases, include PAK1, PAK2, PAK3 and PAK4. These proteins serve as targets for the small GTP binding proteins Cdc42 and Rac and have bee |
https://en.wikipedia.org/wiki/POLR2A | DNA-directed RNA polymerase II subunit RPB1, also known as RPB1, is an enzyme that is encoded by the POLR2A gene in humans.
Function
This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA-binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA.
Interactions
POLR2A has been shown to interact with:
BRCA1,
CREBBP,
CTDP1,
CDK8,
GTF2B,
GTF2F1,
GTF2H4,
MED21,
MED26,
PCAF,
POLR2C,
POLR2E,
POLR2H,
POLR2L,
PQBP1,
SMARCA2,
SMARCA4
SMARCB1,
SMYD3,
SND1,
SUPT5H,
TAF11,
TBP,
TCEA1,
TCERG1, and
ZNF74.
References
Further reading |
https://en.wikipedia.org/wiki/Roxan%20%28protein%29 | RoXaN (Rotavirus 'X'-associated non-structural protein) also known as ZC3H7B (zinc finger CCCH-type containing 7B), is a protein that in humans is encoded by the ZC3H7B gene. RoXaN is a protein that contains tetratricopeptide repeat and leucine-aspartate repeat as well as zinc finger domains. This protein also interacts with the rotavirus non-structural protein NSP3.
Function
Rotavirus mRNAs are capped but not polyadenylated, and viral proteins are translated by the cellular translation machinery. This is accomplished through the action of the viral Nonstructural Protein NSP3 which specifically binds the 3' consensus sequence of viral mRNAs and interacts with the eukaryotic translation initiation factor eIF4G I.
RoXaN (rotavirus X protein associated with NSP3) is 110-kDa cellular protein that contains a minimum of three regions predicted to be involved in protein–protein or nucleic acid–protein interactions. A tetratricopeptide repeat region, a protein–protein interaction domain most often found in multiprotein complexes, is present in the amino-terminal region. In the carboxy terminus, at least five zinc finger motifs are observed, further suggesting the capacity of RoXaN to bind other proteins or nucleic acids. Between these two regions exists a paxillin leucine-aspartate repeat (LD) motif which is involved in protein–protein interactions.
Clinical significance
RoXaN is capable of interacting with NSP3 in vivo and during rotavirus infection. Domains of interaction c |
https://en.wikipedia.org/wiki/SSS%2A | SSS* is a search algorithm, introduced by George Stockman in 1979, that conducts a state space search traversing a game tree in a best-first fashion similar to that of the A* search algorithm.
SSS* is based on the notion of solution trees. Informally, a solution tree can be formed from any arbitrary game tree by pruning the number of branches at each MAX node to one. Such a tree represents a complete strategy for MAX, since it specifies exactly one MAX action for every possible sequence of moves made by the opponent. Given a game tree, SSS* searches through the space of partial solution trees, gradually analyzing larger and larger subtrees, eventually producing a single solution tree with the same root and Minimax value as the original game tree. SSS* never examines a node that alpha–beta pruning would prune, and may prune some branches that alpha–beta would not. Stockman speculated that SSS* may therefore be a better general algorithm than alpha–beta. However, Igor Roizen and Judea Pearl have shown that the savings in the number of positions that SSS* evaluates relative to alpha/beta is limited and generally not enough to compensate for the increase in other resources (e.g., the storing and sorting of a list of nodes made necessary by the best-first nature of the algorithm). However, Aske Plaat, Jonathan Schaeffer, Wim Pijls and Arie de Bruin have shown that a sequence of null-window alpha–beta calls is equivalent to SSS* (i.e., it expands the same nodes in the same order) |
https://en.wikipedia.org/wiki/Vantasselite | Vantasselite is a rare aluminium phosphate mineral with formula: Al4(PO4)3(OH)3 •9H2O. It crystallizes in the orthorhombic system and has a white color, a hardness of 2 to 2.5, a white streak and a pearly luster.
It occurs in a quartzite quarry north of Bihain, Belgium It was first described in 1987 and named after Belgian mineralogist René Van Tassel.
References
Phosphate minerals
Aluminium minerals
Orthorhombic minerals |
https://en.wikipedia.org/wiki/Dopamine%20receptor%20D2 | {{DISPLAYTITLE:Dopamine receptor D2}}
Dopamine receptor D2, also known as D2R, is a protein that, in humans, is encoded by the DRD2 gene. After work from Paul Greengard's lab had suggested that dopamine receptors were the site of action of antipsychotic drugs, several groups, including those of Solomon Snyder and Philip Seeman used a radiolabeled antipsychotic drug to identify what is now known as the dopamine D2 receptor. The dopamine D2 receptor is the main receptor for most antipsychotic drugs. The structure of DRD2 in complex with the atypical antipsychotic risperidone has been determined.
Function
D2 receptors are coupled to Gi subtype of G protein. This G protein-coupled receptor inhibits adenylyl cyclase activity.
In mice, regulation of D2R surface expression by the neuronal calcium sensor-1 (NCS-1) in the dentate gyrus is involved in exploration, synaptic plasticity and memory formation. Studies have shown potential roles for D2R in retrieval of fear memories in the prelimbic cortex and in discrimination learning in the nucleus accumbens.
In flies, activation of the D2 autoreceptor protected dopamine neurons from cell death induced by MPP+, a toxin mimicking Parkinson's disease pathology.
While optimal dopamine levels favor D1R cognitive stabilization, it is the D2R that mediates the cognitive flexibility in humans.
Isoforms
Alternative splicing of this gene results in three transcript variants encoding different isoforms.
The long form (D2Lh) has the "cano |
https://en.wikipedia.org/wiki/SOD2 | Superoxide dismutase 2, mitochondrial (SOD2), also known as manganese-dependent superoxide dismutase (MnSOD), is an enzyme which in humans is encoded by the SOD2 gene on chromosome 6. A related pseudogene has been identified on chromosome 1. Alternative splicing of this gene results in multiple transcript variants. This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer.
Structure
The SOD2 gene contains five exons interrupted by four introns, an uncharacteristic 5′-proximal promoter that possesses a GC-rich region in place of the TATA or CAAT, and an enhancer in the second intron. The proximal promoter region contains multiple binding sites for transcription factors, including specific-1 (Sp1), activator protein 2 (AP-2), and early growth response 1 (Egr-1). This gene is a mitochondrial member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial matrix protein that forms a homotetramer and binds one manganese ion per subunit. The manganese site forms a trigonal bipyramidal geometry with four ligands from the protein and a fifth solvent ligand. This solvent li |
https://en.wikipedia.org/wiki/KRMW | KRMW (94.9 FM) is a radio station licensed to Cedarville, Arkansas, United States. It serves the Fayetteville/Fort Smith area. The station is owned by Cumulus Media.
Formats
The 94.9 frequency went through many formats in the 2010s. It started as an adult alternative music format. In 2012 it changed to an adult contemporary radio station as "Warm 94.9." Next, the station flipped to country music under the "Nash FM" umbrella in August 2014. As of 2016, KRMW is an eclectic format branded as "Radio Jon/Deek," named after the only on-air personalities at the station, Jon Williams and Derek "Deek" Kastner.
References
External links
RMW
Adult album alternative radio stations in the United States
Radio stations established in 1992
Cumulus Media radio stations |
https://en.wikipedia.org/wiki/10-hydroxydihydrosanguinarine%2010-O-methyltransferase | In enzymology, a 10-hydroxydihydrosanguinarine 10-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 10-hydroxydihydrosanguinarine S-adenosyl-L-homocysteine + dihydrochelirubine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 10-hydroxydihydrosanguinarine, whereas its two products are S-adenosylhomocysteine and dihydrochelirubine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:10-hydroxydihydrosanguinarine 10-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/12-hydroxydihydrochelirubine%2012-O-methyltransferase | In enzymology, a 12-hydroxydihydrochelirubine 12-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 12-hydroxydihydrochelirubine S-adenosyl-L-homocysteine + dihydromacarpine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 12-hydroxydihydrochelirubine, whereas its two products are S-adenosylhomocysteine and dihydromacarpine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:12-hydroxydihydrochelirubine 12-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/24-methylenesterol%20C-methyltransferase | In enzymology, a 24-methylenesterol C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 24-methylenelophenol S-adenosyl-L-homocysteine + (Z)-24-ethylidenelophenol
Thus, the two substrates of this enzyme are S-adenosyl methionine and 24-Methylenelophenol, whereas its two products are S-adenosylhomocysteine and (Z)-24-ethylidenelophenol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:24-methylenelophenol C-methyltransferase. Other names in common use include SMT2, and 24-methylenelophenol C-241-methyltransferase. This enzyme participates in the biosynthesis of steroids.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%2C7-dimethylquercetin%204%27-O-methyltransferase | In enzymology, a 3,7-dimethylquercetin 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,3',4'-trihydroxy-3,7-dimethoxyflavone S-adenosyl-L-homocysteine + 5,3'-dihydroxy-3,7,4'-trimethoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,3',4'-trihydroxy-3,7-dimethoxyflavone (rhamnazin), whereas its two products are S-adenosylhomocysteine and 5,3'-dihydroxy-3,7,4'-trimethoxyflavone (ayanin).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,3',4'-trihydroxy-3,7-dimethoxyflavone 4'-O-methyltransferase. Other names in common use include flavonol 4'-O-methyltransferase, flavonol 4'-methyltransferase, 4'-OMT, S-adenosyl-L-methionine:3',4',5-trihydroxy-3,7-dimethoxyflavone, 4'-O-methyltransferase, and 3,7-dimethylquercitin 4'-O-methyltransferase [mis-spelt].
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%27-demethylstaurosporine%20O-methyltransferase | In enzymology, a 3'-demethylstaurosporine O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3'-demethylstaurosporine S-adenosyl-L-homocysteine + staurosporine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3'-demethylstaurosporine, whereas its two products are S-adenosylhomocysteine and staurosporine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3'-demethylstaurosporine O-methyltransferase. Other names in common use include 3'-demethoxy-3'-hydroxystaurosporine O-methyltransferase, and staurosporine synthase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-demethylubiquinone-9%203-O-methyltransferase | In enzymology, a 3-demethylubiquinone-9 3-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3-demethylubiquinone-9 S-adenosyl-L-homocysteine + ubiquinone-9
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-demethylubiquinone-9, whereas its two products are S-adenosylhomocysteine and ubiquinone-9.
This enzyme participates in ubiquinone biosynthesis.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:2-nonaprenyl-3-methyl-5-hydroxy-6-methoxy-1, 4-benzoquinone 3-O-methyltransferase. Other names in common use include 5-demethylubiquinone-9 methyltransferase, OMHMB-methyltransferase, 2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone, methyltransferase, S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-, and 1,4-benzoquinone-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxy-16-methoxy-2%2C3-dihydrotabersonine%20N-methyltransferase | In enzymology, a 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3-hydroxy-16-methoxy-2,3-dihydrotabersonine S-adenosyl-L-homocysteine + deacetoxyvindoline
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-hydroxy-16-methoxy-2,3-dihydrotabersonine, whereas its two products are S-adenosylhomocysteine and deacetoxyvindoline.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase. Other names in common use include 16-methoxy-2,3-dihydro-3-hydroxytabersonine methyltransferase, NMT, 16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase, S-adenosyl-L-methionine:16-methoxy-2,3-dihydro-3-hydroxytabersonine, and N-methyltransferase. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxyanthranilate%204-C-methyltransferase | In enzymology, a 3-hydroxyanthranilate 4-C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3-hydroxyanthranilate S-adenosyl-L-homocysteine + 3-hydroxy-4-methylanthranilate
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-hydroxyanthranilate, whereas its two products are S-adenosylhomocysteine and 3-hydroxy-4-methylanthranilate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3-hydroxyanthranilate 4-C-methyltransferase. This enzyme is also called 3-hydroxyanthranilate 4-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%27-hydroxy-N-methyl-%28S%29-coclaurine%204%27-O-methyltransferase | In enzymology, a 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine S-adenosyl-L-homocysteine + (S)-reticuline
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3'-hydroxy-N-methyl-(S)-coclaurine, whereas its two products are S-adenosylhomocysteine and (S)-reticuline.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methylquercetin%207-O-methyltransferase | In enzymology, a 3-methylquercetin 7-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxy-3-methoxyflavone S-adenosyl-L-homocysteine + 5,3',4'-trihydroxy-3,7-dimethoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,7,3',4'-tetrahydroxy-3-methoxyflavone (isorhamnetin), whereas its two products are S-adenosylhomocysteine and 5,3',4'-trihydroxy-3,7-dimethoxyflavone (rhamnazin).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,7,3',4'-tetrahydroxy-3-methoxyflavone 7-O-methyltransferase. Other names in common use include flavonol 7-O-methyltransferase, flavonol 7-methyltransferase, 7-OMT, S-adenosyl-L-methionine:3',4',5,7-tetrahydroxy-3-methoxyflavone, 7-O-methyltransferase, and 3-methylquercitin 7-O-methyltransferase [mis-spelt].
The enzyme can be found in Chrysosplenium americanum (American Golden Saxifrage).
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-Methyltetrahydropteroyltriglutamate%E2%80%94homocysteine%20S-methyltransferase | In enzymology, a 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine tetrahydropteroyltri-L-glutamate + L-methionine
Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamate and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamate and L-methionine. This enzyme participates in methionine metabolism. It has 2 cofactors: orthophosphate, and zinc.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase. Other names in common use include tetrahydropteroyltriglutamate methyltransferase, homocysteine methylase, methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase, methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase, cobalamin-independent methionine synthase, methionine synthase (cobalamin-independent), and MetE.
Structure
The enzyme from Escherichia coli consists of two alpha8-beta8 (TIM) barrels positioned face to face and thought to have evolved by gene duplication. The active site lies between the tops of the two barrels, the N-terminal barrel binds 5-methyltetrahydropteroyltri-L-glutamic acid and the C-terminal barrel binds homocysteine. Homocysteine is co |
https://en.wikipedia.org/wiki/6-hydroxymellein%20O-methyltransferase | In enzymology, a 6-hydroxymellein O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 6-hydroxymellein S-adenosyl-L-homocysteine + 6-methoxymellein
Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-hydroxymellein, whereas its two products are S-adenosylhomocysteine and 6-methoxymellein.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:6-hydroxymellein 6-O-methyltransferase. This enzyme is also called 6-hydroxymellein methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-O-methylnorlaudanosoline%205%27-O-methyltransferase | In enzymology, a 6-O-methylnorlaudanosoline 5'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline S-adenosyl-L-homocysteine + nororientaline
Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-O-methylnorlaudanosoline, whereas its two products are S-adenosylhomocysteine and nororientaline.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:6-O-methylnorlaudanosoline 5'-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/7-methylxanthosine%20synthase | In enzymology, a 7-methylxanthosine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + xanthosine S-adenosyl-L-homocysteine + 7-methylxanthosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and xanthosine, whereas its two products are S-adenosylhomocysteine and 7-methylxanthosine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:xanthosine N7-methyltransferase. Other names in common use include xanthosine methyltransferase, XMT, xanthosine:S-adenosyl-L-methionine methyltransferase, CtCS1, CmXRS1, CaXMT1, and S-adenosyl-L-methionine:xanthosine 7-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/8-hydroxyquercetin%208-O-methyltransferase | In enzymology, a 8-hydroxyquercetin 8-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,5,7,8,3',4'-hexahydroxyflavone (gossypetin), whereas its two products are S-adenosylhomocysteine and 3,5,7,3',4'-pentahydroxy-8-methoxyflavone.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3,5,7,8,3',4'-hexahydroxyflavone 8-O-methyltransferase. Other names in common use include flavonol 8-O-methyltransferase, flavonol 8-methyltransferase, S-adenosyl-L-methionine:3,3',4',5,7,8-hexahydroxyflavone, 8-O-methyltransferase, and 8-hydroxyquercitin 8-O-methyltransferase [mis-spelt].
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Amine%20N-methyltransferase | Amine N-methyltransferase (), also called indolethylamine N-methyltransferase, and thioether S-methyltransferase, is an enzyme that is ubiquitously present in non-neural tissues and catalyzes the N-methylation of tryptamine and structurally related compounds. More recently, it was discovered that this enzyme can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.
The chemical reaction taking place is:
S-adenosyl-L-methionine + an amine S-adenosyl-L-homocysteine + a methylated amine
Thus, the two substrates of this enzyme are S-adenosyl methionine and amine, whereas its two products are S-adenosylhomocysteine and methylated amine. In the case of tryptamine and serotonin these then become the dimethylated indolethylamines N,N-dimethyltryptamine (DMT) and bufotenine respectively.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:amine N-methyltransferase. Other names in common use include nicotine N-methyltransferase, tryptamine N-methyltransferase, indolethylamine N-methyltransferase, and arylamine N-methyltransferase. This enzyme participates in tryptophan metabolism.
A wide range of primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.
Struct |
https://en.wikipedia.org/wiki/Anthranilate%20N-methyltransferase | In enzymology, an anthranilate N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + anthranilate S-adenosyl-L-homocysteine + N-methylanthranilate
Thus, the two substrates of this enzyme are S-adenosyl methionine and anthranilate, whereas its two products are S-adenosylhomocysteine and N-methylanthranilate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:anthranilate N-methyltransferase. This enzyme is also called anthranilic acid N-methyltransferase. This enzyme participates in acridone alkaloid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Apigenin%204%27-O-methyltransferase | In enzymology, an apigenin 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,7,4'-trihydroxyflavone (apigenin), whereas its two products are S-adenosylhomocysteine and 4'-methoxy-5,7-dihydroxyflavone (acacetin).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,7,4'-trihydroxyflavone 4'-O-methyltransferase. Other names in common use include flavonoid O-methyltransferase, and flavonoid methyltransferase. This enzyme participates in flavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
O-methylated flavones metabolism |
https://en.wikipedia.org/wiki/Betaine%E2%80%94homocysteine%20S-methyltransferase | In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively:
Trimethylglycine (methyl donor) + homocysteine (hydrogen donor) → dimethylglycine (hydrogen receiver) + methionine (methyl receiver)
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. This enzyme participates in the metabolism of glycine, serine, threonine and also methionine.
Isozymes
In humans, there are two isozymes, BHMT and BHMT2, each encoded by a separate gene.
Tissue distribution
BHMT is expressed most predominantly in the liver and kidney.
Clinical significance
Mutations in the BHMT gene are known to exist in humans. Anomalies may influence the metabolism of homocysteine , which is implicated in disorders ranging from vascular disease, autism, and schizophrenia to neural tube birth defects such as spina bifida.
See also
Betaine
References
Further reading
External links
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Caffeate%20O-methyltransferase | In enzymology, a caffeate O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,4-dihydroxy-trans-cinnamate (caffeic acid), whereas its two products are S-adenosylhomocysteine and 3-methoxy-4-hydroxy-trans-cinnamate (ferulic acid).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase. Other names in common use include caffeate methyltransferase, caffeate 3-O-methyltransferase, and ''S-adenosyl-L-methionine:caffeic acid-O''-methyltransferase. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure
O-methylated hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Caffeoyl-CoA%20O-methyltransferase | In enzymology, a caffeoyl-CoA O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + caffeoyl-CoA S-adenosyl-L-homocysteine + feruloyl-CoA
Thus, the two substrates of this enzyme are S-adenosyl methionine and caffeoyl-CoA, whereas its two products are S-adenosylhomocysteine and feruloyl-CoA. A large number of natural products are generated via a step involving this enzyme.
This enzyme is classified to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:caffeoyl-CoA 3-O-methyltransferase. Other names in common use include caffeoyl coenzyme A methyltransferase, caffeoyl-CoA 3-O-methyltransferase, and trans-caffeoyl-CoA 3-O-methyltransferase. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure
O-methylated hydroxycinnamic acids metabolism
O-methylation |
https://en.wikipedia.org/wiki/Calmodulin-lysine%20N-methyltransferase | In enzymology, a calmodulin-lysine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + calmodulin L-lysine S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and calmodulin L-lysine, whereas its two products are S-adenosylhomocysteine and calmodulin N6-methyl-L-lysine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:calmodulin-L-lysine N6-methyltransferase. Other names in common use include S-adenosylmethionine:calmodulin (lysine) N-methyltransferase, and S-adenosyl-L-methionine:calmodulin-L-lysine 6-N-methyltransferase. This enzyme participates in lysine degradation.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carnosine%20N-methyltransferase | In enzymology, a carnosine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + carnosine S-adenosyl-L-homocysteine + anserine
Thus, the two substrates of this enzyme are S-adenosyl methionine and carnosine, whereas its two products are S-adenosylhomocysteine and anserine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:carnosine N-methyltransferase. This enzyme participates in histidine metabolism.
Gene
The genes encoding carnosine N-methyltransferase activity have been identified by Jakub Drozak and coworkers in 2013 and 2015. In birds and reptiles, the enzyme is encoded by histamine N-methyltransferase-like gene (HNMT-like). Importantly, the HNMT-like gene is absent from available mammalian genomes and in mammalian species, the formation of anserine is catalyzed by methyltransferase that is unrelated to the reptilian and avian enzyme and encoded by C9orf41/UPF0586 gene.
Protein Nomenclature
Currently, the avian-reptilian enzyme encoded by HNMT-like gene is labeled as carnosine N-methyltransferase 2 in public databases, while the mammalian methyltransferase is named carnosine N-methyltransferase 1 (CARNMT1).
References
Further reading
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chlorophenol%20O-methyltransferase | In enzymology, a chlorophenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + trichlorophenol S-adenosyl-L-homocysteine + trichloroanisole
Thus, the two substrates of this enzyme are S-adenosyl methionine and trichlorophenol, whereas its two products are S-adenosylhomocysteine and trichloroanisole.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:trichlorophenol O-methyltransferase. Other names in common use include halogenated phenol O-methyltransferase, trichlorophenol, and O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cobalt-factor%20II%20C20-methyltransferase | In enzymology, a cobalt-factor II C20-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + cobalt-factor II S-adenosyl-L-homocysteine + cobalt-factor III
The two substrates of this enzyme are S-adenosyl methionine and cobalt-factor II; its two products are S-adenosylhomocysteine and cobalt-factor III.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:cobalt-factor-II C20-methyltransferase. This enzyme is also called CbiL. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium.
See also
Cobalamin biosynthesis
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Columbamine%20O-methyltransferase | In enzymology, a columbamine O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + columbamine S-adenosyl-L-homocysteine + palmatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and columbamine, whereas its two products are S-adenosylhomocysteine and palmatine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:columbamine O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Corydaline%20synthase | In enzymology, a corydaline synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + palmatine + 2 NADPH + H+ S-adenosyl-L-homocysteine + corydaline + 2 NADP+
The 4 substrates of this enzyme are S-adenosyl methionine, palmatine, NADPH, and H+, whereas its 3 products are S-adenosylhomocysteine, corydaline, and NADP+.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:protoberberine 13-C-methyltransferase.
References
EC 2.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cycloartenol%2024-C-methyltransferase | In enzymology, a cycloartenol 24-C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + cycloartenol S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
Thus, the two substrates of this enzyme are S-adenosyl methionine and cycloartenol, whereas its two products are S-adenosylhomocysteine and (24R)-24-methylcycloart-25-en-3beta-ol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:cycloartenol 24-C-methyltransferase. This enzyme is also called sterol C-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclopropane-fatty-acyl-phospholipid%20synthase | In enzymology, a cyclopropane-fatty-acyl-phospholipid synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + phospholipid olefinic fatty acid S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
Thus, the two substrates of this enzyme are S-adenosyl methionine and phospholipid olefinic fatty acid, whereas its two products are S-adenosylhomocysteine and phospholipid cyclopropane fatty acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase (cyclizing). Other names in common use include cyclopropane synthetase, unsaturated-phospholipid methyltransferase, cyclopropane synthase, cyclopropane fatty acid synthase, cyclopropane fatty acid synthetase, and CFA synthase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28cytochrome%20c%29-arginine%20N-methyltransferase | In enzymology, a [cytochrome c]-arginine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [cytochrome c]-arginine S-adenosyl-L-homocysteine + [cytochrome c]-Nomega-methyl-arginine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c-arginine, whereas its two products are S-adenosylhomocysteine and cytochrome c-Nomega-methyl-arginine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[cytochrome c]-arginine Nomega-methyltransferase. Other names in common use include S-adenosyl-L-methionine:[cytochrome c]-arginine, and omega-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28cytochrome%20c%29-lysine%20N-methyltransferase | In enzymology, a [cytochrome c]-lysine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [cytochrome c]-L-lysine S-adenosyl-L-homocysteine + [cytochrome c]-N-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c-L-lysine, whereas its two products are S-adenosylhomocysteine and cytochrome c-N6-methyl-L-lysine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[cytochrome c]-L-lysine N6-methyltransferase. Other names in common use include cytochrome c (lysine) methyltransferase, cytochrome c methyltransferase, cytochrome c-specific protein methylase III, cytochrome c-specific protein-lysine methyltransferase, S-adenosyl-L-methionine:[cytochrome c]-L-lysine, and 6-N-methyltransferase. This enzyme participates in lysine degradation.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28cytochrome%20c%29-methionine%20S-methyltransferase | In enzymology, a [cytochrome-c]-methionine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [cytochrome c]-methionine S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c methionine, whereas its two products are S-adenosylhomocysteine and cytochrome c-S-methyl-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[cytochrome c]-methionine S-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Demethylmacrocin%20O-methyltransferase | In enzymology, a demethylmacrocin O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + demethylmacrocin S-adenosyl-L-homocysteine + macrocin
Thus, the two substrates of this enzyme are S-adenosyl methionine and demethylmacrocin, whereas its two products are S-adenosylhomocysteine and macrocin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:demethylmacrocin 2"'-O-methyltransferase. This enzyme is also called demethylmacrocin methyltransferase. This enzyme participates in biosynthesis of 12-, 14- and 16-membered macrolides.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Demethylsterigmatocystin%206-O-methyltransferase | In enzymology, a demethylsterigmatocystin 6-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 6-demethylsterigmatocystin S-adenosyl-L-homocysteine + sterigmatocystin
Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-demethylsterigmatocystin, whereas its two products are S-adenosylhomocysteine and sterigmatocystin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:6-demethylsterigmatocystin 6-O-methyltransferase. Other names in common use include demethylsterigmatocystin methyltransferase, and O-methyltransferase I.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxycytidylate%20C-methyltransferase | In enzymology, a deoxycytidylate C-methyltransferase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + dCMP dihydrofolate + deoxy-5-methylcytidylate
Thus, the two substrates of this enzyme are 5,10-Methylenetetrahydrofolic acid and dCMP, whereas its two products are dihydrofolic acid and deoxy-5-methylcytidylic acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:dCMP C-methyltransferase. Other names in common use include deoxycytidylate methyltransferase, and dCMP methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylhistidine%20N-methyltransferase | In enzymology, a dimethylhistidine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + Nalpha,Nalpha-dimethyl-L-histidine S-adenosyl-L-homocysteine + Nalpha,Nalpha,Nalpha-trimethyl-L-histidine
Thus, the two substrates of this enzyme are S-adenosyl methionine and Nalpha,Nalpha-dimethyl-L-histidine, whereas its two products are S-adenosylhomocysteine and Nalpha,Nalpha,Nalpha-trimethyl-L-histidine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:Nalpha,Nalpha-dimethyl-L-histidine Nalpha-methyltransferase. Other names in common use include dimethylhistidine methyltransferase, histidine-alpha-N-methyltransferase, S-adenosyl-L-methionine:alpha-N,alpha-N-dimethyl-L-histidine, and alpha-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diphthine%20synthase | In enzymology, a diphthine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-(3-carboxy-3-aminopropyl)-L-histidine, whereas its two products are S-adenosylhomocysteine and [[2-[3-carboxy-3-(methylammonio)propyl]-L-histidine]].
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine methyltransferase. Other names in common use include S-adenosyl-L-methionine:elongation factor 2 methyltransferase, and diphthine methyltransferase.
Structural studies
As of late 2007, 84 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Fatty-acid%20O-methyltransferase | In enzymology, a fatty-acid O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + a fatty acid S-adenosyl-L-homocysteine + a fatty acid methyl ester
Thus, the two substrates of this enzyme are S-adenosyl methionine and fatty acid, whereas its two products are S-adenosylhomocysteine and fatty acid methyl ester.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:fatty-acid O-methyltransferase. Other names in common use include fatty acid methyltransferase, and fatty acid O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucuronoxylan%204-O-methyltransferase | In enzymology, a glucuronoxylan 4-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + glucuronoxylan D-glucuronate S-adenosyl-L-homocysteine + glucuronoxylan 4-O-methyl-D-glucuronate
Thus, the two substrates of this enzyme are S-adenosyl methionine and glucuronoxylan D-glucuronate, whereas its two products are S-adenosylhomocysteine and glucuronoxylan 4-O-methyl-D-glucuronate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:glucuronoxylan-D-glucuronate 4-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20N-methyltransferase | In enzymology, a glycine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + glycine S-adenosyl-L-homocysteine + sarcosine
Thus, the substrates of this enzyme are S-adenosyl methionine and glycine, whereas its two products are S-adenosylhomocysteine and sarcosine.
Glycine N-methyltransferase belongs to the family of methyltransferase enzymes. The systematic name of this enzyme class is S-adenosyl-L-methionine:glycine N-methyltransferase. Other names in common use include glycine methyltransferase, S-adenosyl-L-methionine:glycine methyltransferase, and GNMT. This family of enzymes participates in the metabolism of multiple amino acids.
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Viral%20nonstructural%20protein | In virology, a nonstructural protein is a protein encoded by a virus but that is not part of the viral particle. They typically include the various enzymes and transcription factors the virus uses to replicate itself, such as a viral protease (3CL/nsp5, etc.), an RNA replicase or other template-directed polymerases, and some means to control the host.
Examples
NSP1 (rotavirus)
NSP4 (rotavirus)
NSP5 (rotavirus)
Influenza non-structural protein
NS1 influenza protein
HBcAg, core antigen of hepatitis B
Bunyaviridae nonstructural S proteins
See also
Viral structural protein
References |
https://en.wikipedia.org/wiki/Guanidinoacetate%20N-methyltransferase | Guanidinoacetate N-methyltransferase () is an enzyme that catalyzes the chemical reaction and is encoded by gene GAMT located on chromosome 19p13.3.
S-adenosyl-L-methionine + guanidinoacetate S-adenosyl-L-homocysteine + creatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and guanidinoacetate, whereas its two products are S-adenosylhomocysteine and creatine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:N-guanidinoacetate methyltransferase. Other names in common use include GA methylpherase, guanidinoacetate methyltransferase, guanidinoacetate transmethylase, methionine-guanidinoacetic transmethylase, and guanidoacetate methyltransferase. This enzyme participates in glycine, serine and threonine metabolism and arginine and proline metabolism.
The protein encoded by this gene is a methyltransferase that converts guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects in this gene have been implicated in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. Two transcript variants encoding different isoforms have been described for this gene.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
See |
https://en.wikipedia.org/wiki/Hexaprenyldihydroxybenzoate%20methyltransferase | In enzymology, a hexaprenyldihydroxybenzoate methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-hexaprenyl-4,5-dihydroxybenzoate, whereas its two products are S-adenosylhomocysteine and 3-hexaprenyl-4-hydroxy-5-methoxybenzoate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3-hexaprenyl-4,5-dihydroxylate O-methyltransferase. Other names in common use include 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase, and dihydroxyhexaprenylbenzoate methyltransferase. This enzyme participates in ubiquinone biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homocysteine%20S-methyltransferase | In enzymology, a homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-methylmethionine + L-homocysteine 2 L-methionine
Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S-methyltransferase. This enzyme participates in methionine metabolism.
Alternative names
Other names of this enzyme in common use include S-adenosylmethionine homocysteine transmethylase, S-methylmethionine homocysteine transmethylase, adenosylmethionine transmethylase, methylmethionine:homocysteine methyltransferase, adenosylmethionine:homocysteine methyltransferase, homocysteine methylase, homocysteine methyltransferase, homocysteine transmethylase, L-homocysteine S-methyltransferase, S-adenosyl-L-methionine:L-homocysteine methyltransferase, S-adenosylmethionine-homocysteine transmethylase, and S-adenosylmethionine:homocysteine methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indolepyruvate%20C-methyltransferase | In enzymology, an indolepyruvate C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (indol-3-yl)pyruvate S-adenosyl-L-homocysteine + (3S)-3-(indol-3-yl)-3-oxobutanoate
Thus, the two substrates of this enzyme are S-adenosyl methionine and (indol-3-yl)pyruvate, whereas its two products are S-adenosylhomocysteine and (3S)-3-(indol-3-yl)-3-oxobutanoate.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine: (indol-3-yl)pyruvate C-methyltransferase. Other names in common use include indolepyruvate methyltransferase, indolepyruvate 3-methyltransferase, indolepyruvic acid methyltransferase, and S-adenosyl-L-methionine:indolepyruvate C-methyltransferase. This enzyme participates in tryptophan metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol%201-methyltransferase | In enzymology, an inositol 1-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + myo-inositol S-adenosyl-L-homocysteine + 1D-1-O-methyl-myo-inositol
Thus, the two substrates of this enzyme are S-adenosyl methionine and myo-inositol, whereas its two products are S-adenosylhomocysteine and 1D-1-O-methyl-myo-inositol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:1D-myo-inositol 1-O-methyltransferase. Other names in common use include inositol D-1-methyltransferase, S-adenosylmethionine:myo-inositol 3-methyltransferase, myo-inositol 3-O-methyltransferase, inositol 3-O-methyltransferase (name based on 1L-numbering system, and not 1D-numbering), and S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase. This enzyme participates in inositol phosphate metabolism.
References
EC 2.1.1
Enzymes of unknown structure
Inositol |
https://en.wikipedia.org/wiki/Inositol%203-methyltransferase | In enzymology, an inositol 3-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + myo-inositol S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol
Thus, the two substrates of this enzyme are S-adenosyl methionine and myo-inositol, whereas its two products are S-adenosylhomocysteine and 1D-3-O-methyl-myo-inositol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:1D-myo-inositol 3-O-methyltransferase. Other names in common use include inositol L-1-methyltransferase, myo-inositol 1-methyltransferase, S-adenosylmethionine:myo-inositol 1-methyltransferase, myo-inositol 1-O-methyltransferase (name based on 1L-numbering, system and not 1D-numbering), and S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase. This enzyme participates in inositol phosphate metabolism.
References
EC 2.1.1
Enzymes of unknown structure
Inositol |
https://en.wikipedia.org/wiki/Inositol%204-methyltransferase | In enzymology, an inositol 4-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + myo-inositol S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
Thus, the two substrates of this enzyme are S-adenosyl methionine and myo-inositol, whereas its two products are S-adenosylhomocysteine and 1D-4-O-methyl-myo-inositol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:1D-myo-inositol 4-methyltransferase. Other names in common use include myo-inositol 4-O-methyltransferase, S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase, and myo-inositol 6-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure
Inositol |
https://en.wikipedia.org/wiki/Iodophenol%20O-methyltransferase | In enzymology, an iodophenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 2-iodophenol S-adenosyl-L-homocysteine + 2-iodophenol methyl ether
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-iodophenol, whereas its two products are S-adenosylhomocysteine and 2-iodophenol methyl ether.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:2-iodophenol O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isobutyraldoxime%20O-methyltransferase | In enzymology, an isobutyraldoxime O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 2-methylpropanal oxime S-adenosyl-L-homocysteine + 2-methylpropanal O-methyloxime
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-methylpropanal oxime, whereas its two products are S-adenosylhomocysteine and 2-methylpropanal O-methyloxime.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:2-methylpropanal-oxime O-methyltransferase. Other names in common use include aldoxime methyltransferase, S-adenosylmethionine:aldoxime O-methyltransferase, and aldoxime O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28Iso%29eugenol%20O-methyltransferase | In enzymology, a (iso)eugenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + isoeugenol S-adenosyl-L-homocysteine + isomethyleugenol
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoeugenol, whereas its two products are S-adenosylhomocysteine and isomethyleugenol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:isoeugenol O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoflavone%204%27-O-methyltransferase | In enzymology, an isoflavone 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + an isoflavone S-adenosyl-L-homocysteine + a 4'-O-methylisoflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoflavone, whereas its two products are S-adenosylhomocysteine and 4'-O-methylisoflavone.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:isoflavone 4'-O-methyltransferase. Other names in common use include 4'-hydroxyisoflavone methyltransferase, isoflavone methyltransferase, and isoflavone O-methyltransferase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Isoflavonoids metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/Isoflavone%207-O-methyltransferase | In enzymology, an isoflavone 7-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + a 7-hydroxyisoflavone S-adenosyl-L-homocysteine + a 7-methoxyisoflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 7-hydroxyisoflavone, whereas its two products are S-adenosylhomocysteine and 7-methoxyisoflavone.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:hydroxyisoflavone 7-O-methyltransferase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Isoflavonoids metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/Isoliquiritigenin%202%27-O-methyltransferase | In enzymology, an isoliquiritigenin 2'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + isoliquiritigenin S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoliquiritigenin, whereas its two products are S-adenosylhomocysteine and 2'-O-methylisoliquiritigenin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:isoliquiritigenin 2'-O-methyltransferase. Other names in common use include chalcone OMT, and CHMT.
References
EC 2.1.1
Enzymes of unknown structure
Chalconoids metabolism |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.