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https://en.wikipedia.org/wiki/Crystal%20Airport | Crystal Airport may refer to:
Crystal Airport (Minnesota) in Crystal, Minnesota (suburb of Minneapolis), United States (FAA: MIC)
Crystal Airport (California) in Llano, California, United States (FAA: 46CN)
Other airport names starting with Crystal
Crystal City Municipal Airport in Crystal City, Texas, United States (FAA: 20R)
Crystal Lake Airport in Decatur, Arkansas, United States (FAA: 5M5)
Crystal River Airport in Crystal River, Florida, United States (FAA: CGC) |
https://en.wikipedia.org/wiki/Crystal%20River%20Airport | Crystal River Airport – Captain Tom Davis Field is a public airport located three miles (5 km) southeast of the central business district of Crystal River, in Citrus County, Florida, United States. It is owned by Citrus County.
This airport is assigned a three-letter location identifier of CGC by the Federal Aviation Administration, but it does not have an International Air Transport Association (IATA) airport code (the IATA assigned CGC to Cape Gloucester Airport in Papua New Guinea).
Facilities and aircraft
Crystal River Airport – Captain Tom Davis Field covers an area of which contains two runways: 9/27 with an asphalt surface measuring 4,555 x 75 ft (1,388 x 23 m) and 18/36 with a turf surface measuring 3,020 x 100 ft (920 x 30 m).
For the 12-month period ending May 9, 2002, the airport had 36,600 aircraft operations, an average of 100 per day: 98% general aviation, 1% air taxi and 1% military. There are 50 aircraft based at this airport: 86% single engine, 10% multi-engine, 2% helicopter and 2% glider.
A non-aviation Florida Army National Guard facility is located at the airport which periodically hosts visiting Florida Army National Guard aircraft from other FLARNG installations.
In December 2013, the Citrus County Board of County Commissioners passed a resolution modifying the airport's name to Crystal River Airport – Captain Tom Davis Field. CAPT Tom Davis, USN (Ret), is an accomplished Naval Aviator out of the Navy's jet fighter community and a recipient of |
https://en.wikipedia.org/wiki/Neomorphism | Neomorphism refers to the wet metamorphic process in which diagenetic alterations systematically transform minerals into either polymorphs or crystalline structures that are structurally identical to the rock(s) from which they developed.
Coined by the late Robert L. Folk, neomorphism encompasses the functions of both recrystallization and inversion, which are geological processes that deal primarily with rock reformation. The neomorphic process, as it relates to geology and petrography, is one of the many major processes that sustain both carbonate minerals and limestone. Neomorphism is largely held accountable for the metastability of aragonite and magnesium-rich calcite, and when conditions permit, neomorphic reactions and interactions can result in texture loss and/or feature deformation of affected rock formations.
Types of neomorphism
Recrystallization
The term "recrystallization" broadly refers to the many metamorphic processes that change the size and/or shape of crystal formations and preserve the chemical composition and mineralogy of the original mineral. Because recrystallization accounts for the majority of all visible changes produced by neomorphism, the terms "neomorphism" and "recrystallization" implicitly allude to each other and can therefore be used interchangeably under most circumstances. In petrology, there are two forms of recrystallization: recrystallization by inversion and recrystallization by replacement.
Inversion
Inversion is a complex form o |
https://en.wikipedia.org/wiki/Twisted%3A%20The%20Distorted%20Mathematics%20of%20Greenhouse%20Denial | Twisted: The Distorted Mathematics of Greenhouse Denial is a 2007 book by Ian G. Enting, who is the Professorial Research Fellow in the ARC Centre of Excellence for Mathematics and Statistics of Complex Systems (MASCOS) based at the University of Melbourne. The book analyses the arguments of climate change deniers and the use and presentation of statistics. Enting contends there are contradictions in their various arguments. The author also presents calculations of the actual emission levels that would be required to stabilise CO2 concentrations. This is an update of calculations that he contributed to the pre-Kyoto IPCC report on Radiative Forcing of Climate.
See also
Climate change
Greenhouse effect
Radiative forcing
References
Climate change books
2007 non-fiction books
2007 in the environment
Australian non-fiction books
Statistics books |
https://en.wikipedia.org/wiki/History%20of%20Crystal%20Palace%20F.C. | Crystal Palace Football Club is an English professional association football club based in Selhurst, South London, England. Although formally created as a professional outfit in 1905 at the site of the famous Crystal Palace Exhibition building, the club have claimed their official foundation date to be as far back as 1861,when an amateur Crystal Palace football team was established using the cricket pitch inside the Palace grounds. In recognition of their claim, the club changed the date of its official crest to 1861. The club played their home games inside the grounds of the Palace at the FA Cup Final stadium from 1905 until 1915, when they were forced to leave due to the outbreak of the First World War. They moved to their current home at Selhurst Park in 1924.
The amateur club became one of the original founder members of the Football Association in 1863, and went on to compete in the first ever FA Cup competition in 1871–72, reaching the semi-finals, before disappearing from historical records around 1876. Shortly after Crystal Palace returned to existence as a professional outfit in 1905, the club applied for election to the Football League, but were rejected and forced to settle for a place in the Southern League Second Division. They were eventually admitted to the Football League in 1920, and have overall mainly competed in the top two tiers of English football. Their best ever top flight season came in 1990–91, when the club challenged for the English league title, |
https://en.wikipedia.org/wiki/LCHAD | HADHA may refer to:
Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency
HADHA, enzyme |
https://en.wikipedia.org/wiki/Pre-measure | In mathematics, a pre-measure is a set function that is, in some sense, a precursor to a bona fide measure on a given space. Indeed, one of the fundamental theorems in measure theory states that a pre-measure can be extended to a measure.
Definition
Let be a ring of subsets (closed under union and relative complement) of a fixed set and let be a set function. is called a pre-measure if
and, for every countable (or finite) sequence of pairwise disjoint sets whose union lies in
The second property is called -additivity.
Thus, what is missing for a pre-measure to be a measure is that it is not necessarily defined on a sigma-algebra (or a sigma-ring).
Carathéodory's extension theorem
It turns out that pre-measures give rise quite naturally to outer measures, which are defined for all subsets of the space More precisely, if is a pre-measure defined on a ring of subsets of the space then the set function defined by
is an outer measure on and the measure induced by on the -algebra of Carathéodory-measurable sets satisfies for (in particular, includes ). The infimum of the empty set is taken to be
(Note that there is some variation in the terminology used in the literature. For example, Rogers (1998) uses "measure" where this article uses the term "outer measure". Outer measures are not, in general, measures, since they may fail to be -additive.)
See also
References
(See section 1.2.)
Measures (measure theory) |
https://en.wikipedia.org/wiki/Champagne%20Beach%20%28Vanuatu%29 | Champagne Beach is a popular beach located on the island of Espiritu Santo in Vanuatu. The beach is famous for its crystal clear waters and powdery white sands, which is one of the best in the South Pacific region. It is visited regularly by tourists and cruise boats from Australia.
Champagne Beach is located in adjacent and close proximity to Hog Harbour village on the northeast of Santo.
Beaches of Vanuatu |
https://en.wikipedia.org/wiki/Eutely | Eutelic organisms have a fixed number of somatic cells when they reach maturity, the exact number being relatively constant for any one species. This phenomenon is also referred to as cell constancy. Development proceeds by cell division until maturity; further growth occurs via cell enlargement only. This growth is known as auxetic growth. It is shown by members of phylum Aschelminthes. In some cases, individual organs show eutelic properties while the organism itself does not.
Background
In 1909, Eric Martini coined the term eutely to describe the idea of cell constancy and to introduce a term literature sources would be able to use to identify organisms with a fixed amount and arrangement of cells and tissues. Since the introduction of eutely in the early 1900s, textbooks and theories of cytology and ontogeny have not used the term consistently. Advancements in the field of eutely has been developed by morphologists.
Studying of eutelic organisms has proved challenging, as most eutelic organisms are microscopic. Additionally, there is potential for mistakes in cell counting (often completed via an automated cell counter) and observation when larger organisms have numerous cells. In organisms of small size, errors in the examination and explanation of units may entirely negate reconstructions and deductions. Therefore, investigation of most eutelic organisms is done with intense scrutiny and review.
There are two distinct classes of organisms which display eutely:
Eut |
https://en.wikipedia.org/wiki/KHOJ%20%28AM%29 | KHOJ is a radio station broadcasting out of St. Charles, Missouri with a Catholic format. It broadcasts on AM frequency 1460 kHz and is part of the Covenant Network.
KHOJ's studios are located on Hampton Avenue in St. Louis, while its transmitter is located north of St. Charles.
History
KIRL went on the air in 1968, the successor to KADY, which had previously operated on the frequency from 1958 to 1965 (and built the transmitter site used by KHOJ today). It was owned by Contemporary Media, Inc. In 1979, Contemporary Media sold KIRL to the Bronco Broadcasting Company. Bronco relaunched KIRL as a gospel music station for the African American community. Zella Jackson Price and other pioneering announcers were on its air staff.
In 2005, Bronco sold KIRL to the Covenant Network for $730,000. The sale marked the end of KIRL's gospel programming as of April 30 and scattered many of the religious programs it carried. Covenant immediately relaunched the station as KHOJ with its programming.
References
External links
The Covenant Network
WRYT / KHOJ Programming Schedule
FCC History Cards for KHOJ
HOJ (AM)
Catholic radio stations
Radio stations established in 1968
1968 establishments in Missouri |
https://en.wikipedia.org/wiki/Cletocamptoides%20helobius | Cletocamptoides helobius is a species of copepod found in brackish waters of North America first described by John W. Fleeger in 1980. The species has been used in a study of the evolution of the DNA of the related species Cletocamptus deitersi.
References
Harpacticoida
Freshwater crustaceans of North America
Crustaceans described in 1980 |
https://en.wikipedia.org/wiki/Vespertilioninae | The Vespertilioninae are a subfamily of vesper bats from the family Vespertilionidae.
Classification
Subfamily Vespertilioninae
Tribe Antrozoini
Genus Antrozous
Pallid bat, Antrozous pallidus
Genus Bauerus
Van Gelder's bat, Bauerus dubiaquercus
Genus Rhogeessa - Rhogeessa bats
Yucatan yellow bat, Rhogeessa aenea
Allen's yellow bat, Rhogeessa alleni
Bickham's yellow bat, Rhogeessa bickhami
Genoways's yellow bat, Rhogeessa genowaysi
Slender yellow bat, Rhogeessa gracilis
Husson's yellow bat, Rhogeessa hussoni
Thomas's yellow bat, Rhogeessa io
Menchu's yellow bat, Rhogeessa menchuae
Tiny yellow bat, Rhogeessa minutilla
Least yellow bat, Rhogeessa mira
Northern little yellow bat, Rhogeessa parvula
Nicaraguan little yellow bat, Rhogeessa permutandis
Black-winged little yellow bat, Rhogeessa tumida
Ecuadorian little yellow bat, Rhogeessa velilla
Tribe Eptesicini
Genus Arielulus
Bronze sprite, Arielulus circumdatus
Coppery sprite, Arielulus cuprosus
Social sprite, Arielulus societatis
Genus Eptesicus – house bats
Anatolian serotine, Eptesicus anatolicus
Little black serotine, Eptesicus andinus
Bobrinski's serotine, Eptesicus bobrinskoi
Botta's serotine, Eptesicus bottae
Brazilian brown bat, Eptesicus brasiliensis
Chiriquinan serotine, Eptesicus chiriquinus
Diminutive serotine, Eptesicus diminutus
Horn-skinned bat, Eptesicus floweri
Argentine brown bat, Eptesicus furinalis
Big brown bat, Eptesicus fuscus
Gobi big brown bat, Eptesicus gobiensis
Guadeloupe big |
https://en.wikipedia.org/wiki/Immigration%20and%20crime | Immigration and crime refers to the relationship between criminal activity and the phenomenon of immigration. The academic literature and official statistics provide mixed findings for the relationship between immigration and crime. Research in the United States tends to suggest that immigration either has no impact on the crime rate or even that immigrants are less prone to crime. A meta-analysis of 51 studies from 1994–2014 on the relationship between immigration and crime in the United States found that, overall, the immigration-crime association is negative, but the relationship is very weak and there is significant variation in findings across studies. This is in line with a 2009 review of high-quality studies conducted in the United States that also found a negative relationship.
Research and statistics in some other, mainly European countries suggest a positive link between immigration and crime: immigrants from particular countries are often overrepresented in crime figures. The over-representation of immigrants in the criminal justice systems of several countries may be due to socioeconomic factors, imprisonment for migration offenses, and racial and ethnic discrimination by police and the judicial system. The relationship between immigration and terrorism is understudied, but existing research is inconclusive. Research on the relationship between refugee migration and crime is scarce and existing empirical evidence is often contradictory. According to statistics fr |
https://en.wikipedia.org/wiki/%C4%8Cierna%20Lehota | Čierna Lehota may refer to several places in Slovakia.
Čierna Lehota, Bánovce nad Bebravou District
Čierna Lehota, Rožňava District |
https://en.wikipedia.org/wiki/Cowdry%20bodies | Cowdry bodies are eosinophilic or basophilic nuclear inclusions composed of nucleic acid and protein seen in cells infected with Herpes simplex virus, Varicella-zoster virus, and Cytomegalovirus. They are named after Edmund Cowdry.
There are two types of intranuclear Cowdry bodies:
Type A (as seen in herpes simplex, VZV and measles )
Type B (as seen in infection with poliovirus, CMV and adenovirus), though it may seem that this is an antiquated and perhaps illusory type.
Light microscopy is used for detection of Cowdry bodies.
References
Histopathology |
https://en.wikipedia.org/wiki/Pollaczek%E2%80%93Khinchine%20formula | In queueing theory, a discipline within the mathematical theory of probability, the Pollaczek–Khinchine formula states a relationship between the queue length and service time distribution Laplace transforms for an M/G/1 queue (where jobs arrive according to a Poisson process and have general service time distribution). The term is also used to refer to the relationships between the mean queue length and mean waiting/service time in such a model.
The formula was first published by Felix Pollaczek in 1930 and recast in probabilistic terms by Aleksandr Khinchin two years later. In ruin theory the formula can be used to compute the probability of ultimate ruin (probability of an insurance company going bankrupt).
Mean queue length
The formula states that the mean number of customers in system L is given by
where
is the arrival rate of the Poisson process
is the mean of the service time distribution S
is the utilization
Var(S) is the variance of the service time distribution S.
For the mean queue length to be finite it is necessary that as otherwise jobs arrive faster than they leave the queue. "Traffic intensity," ranges between 0 and 1, and is the mean fraction of time that the server is busy. If the arrival rate is greater than or equal to the service rate , the queuing delay becomes infinite. The variance term enters the expression due to Feller's paradox.
Mean waiting time
If we write W for the mean time a customer spends in the system, then where is the mean w |
https://en.wikipedia.org/wiki/100%25%20Pure%20Love | "100% Pure Love" is a song recorded by American singer and songwriter Crystal Waters from her second studio album, Storyteller (1994). It was released on April 11, 1994 by Mercury and A&M (UK), as the album's lead single. The song was a hit in many countries, reaching the top 20 in Australia, Finland, the Netherlands, Switzerland, the United Kingdom, and the United States. It is certified platinum in Australia and gold in the US. In 1995, it was awarded the prize for Top ASCAP Dance Song. And its accompanying music video, directed by Marcus Nispel, was nominated for Best Dance Video at the 1994 MTV Video Music Awards.
Background and release
The song is inspired by her relationship at the time. The singer says she chose the stylings of the song as a reaction to the popularity of gangsta rap during the mid-1990s in the United States.
Looking to write a positive song, she sent an early draft to her production team Basement Boys who "hated the hook" but "loved the verses." Originally the song was built on the lyrics, "the beat goes boom," before she went back to the drawing board and considered the reasons she was writing the song in the first place. "From the back to the middle and around again, I'm going to be there 'til the end, 100% pure love," emerged as the next draft and became the lyrics in the completed version of the song.
Crystal Waters also signed and debuted as a model with the Ford Modeling Agency in August 1994. They included her as a special guest in fashion co |
https://en.wikipedia.org/wiki/Feed-in%20tariffs%20in%20Germany | Feed-in electricity tariffs (FiT) were introduced in Germany to encourage the use of new energy technologies such as wind power, biomass, hydropower, geothermal power and solar photovoltaics. Feed-in tariffs are a policy mechanism designed to accelerate investment in renewable energy technologies by providing them remuneration (a "tariff") above the retail or wholesale rates of electricity. The mechanism provides long-term security to renewable energy producers, typically based on the cost of generation of each technology. Technologies such as wind power, for instance, are awarded a lower per-kWh price, while technologies such as solar PV and tidal power are offered a higher price, reflecting higher costs.
As of July 2014, feed-in tariffs range from 3.33 ¢/kWh (4.4 ¢/kWh) for hydropower facilities over 50 MW to 12.88 ¢/kWh (17.3 ¢/kWh) for solar installations on buildings up to 30kWp and 19 ¢/kWh (25.5 ¢/kWh) for offshore wind.
On 1 August 2014, a revised Renewable Energy Sources Act or EEG (2014) (colloquially called EEG2.0) entered into force. The government will now stipulate specific deployment corridors to control the uptake of renewables and the feed-in tariffs themselves will be determined by auction.
The aim is to meet Germany's renewable energy goals of 40 to 45% of electricity consumption in 2025 and 55% to 60% in 2035. The policy also aims to encourage the development of renewable technologies, reduce external costs, and increase security of energy supply.
In |
https://en.wikipedia.org/wiki/Biology%20of%20the%20Cell | Biology of the Cell is a peer-reviewed scientific journal in the field of cell biology, cell physiology, and molecular biology of animal and plant cells, microorganisms and protists. Topics covered include development, neurobiology, and immunology, as well as theoretical or biophysical modelling.
The journal is currently published monthly by Wiley-Blackwell on behalf of the Société Française des Microscopies and the Société de Biologie Cellulaire de France.
History
The journal first appeared in 1962 and was originally titled Journal de Microscopie (1962–1974). In 1975 the journal was retitled Journal de Microscopie et de Biologie Cellulaire (; 1975–1976). It was later retitled Biologie Cellulaire (; 1977–1980), becoming Biology of the Cell in 1981.
Articles were originally published in either English or French, with summaries in both languages.
Modern journal
Content from 1988 is available online in PDF format, with papers from 2005 also being available in HTML, and from 2006 in an enhanced full-text format.
The journal's 2014 impact factor was 3.506. Biology of the Cell is indexed by BIOBASE, BIOSIS, CAB International, Cambridge Scientific Abstracts, Chemical Abstracts Service, Current Contents/Life Sciences, EMBASE/Excerpta Medica, MEDLINE/Index Medicus, and ProQuest Information and Learning
Articles are primarily research and reviews. Themed series on specific topics are scheduled. They were: Stem Cells (2005), RNA localization (2005), Aquaporins (2005), Synapses ( |
https://en.wikipedia.org/wiki/Smyrna%20Airport | Smyrna Airport may refer to:
Smyrna Airport (Tennessee) in Smyrna, Tennessee, United States (FAA: MQY)
Smyrna Airport (Delaware) in Smyrna, Delaware, United States (FAA: 38N) |
https://en.wikipedia.org/wiki/Vijayendra%20Varma | Vijayendra Varma is a 2004 Indian Telugu-language action film produced by Konda Krishnam Raju under Aditya Productions banner and directed by Swarna Subba Rao. It features Nandamuri Balakrishna, Laya, Sangeeta, Ankita , with the music composed by Koti. The film was panned both by critics and audience. The core plot of the movie was reported to be inspired by the 2002 movie The Bourne Identity.
Plot
An unnamed man (Balakrishna) lives with his wife (Laya), daughter, and in-laws. He does not have a name nor does he know who he is. He cannot remember anything that has happened 7 years before. However, he realizes that he possesses special combat skills whenever he comes across evil elements. When he forces his wife, to tell the truth, she reveals that he was found in the river in a mutilated state and he was taken care of by her. As the man goes to Hyderabad searching for his identity, a few incidents lead to the answer. He discovers that he is none other than the most respected and committed Indian Army Officer, Vijayendra Varma. The rest of the story is about how he retraces his past and saves the nation from Pakistani Jihadis.
Cast
Nandamuri Balakrishna as Colonel Vijayendra Varma
Laya as Indira
Ankitha as Venkata Lakshmi
Sangeetha as Journalist
Mukesh Rishi as Aslam Khan (Pakistan Terrorists leader)
Ashish Vidyarthi as Naanaji
Brahmanandam
Ahuti Prasad
Chalapathi Rao as Yadav
M. Balayya as Dr.Narayana Rao
Bhupendra Singh as Rahul
M. S. Narayana
Manorama |
https://en.wikipedia.org/wiki/Leandr%C3%A3o%20%28footballer%29 | Leandro Costa Miranda Moraes or simply Leandrão (born 18 July 1983) is a Brazilian professional football manager and former player who is the current head coach of Boavista.
Club statistics
Honours
Internacional
Campeonato Gaúcho: 2002, 2005, 2008, 2009
Sport
Campeonato Pernambucano: 2010
ABC
Campeonato Brasileiro Série C: 2010
Campeonato Potiguar: 2011
Remo
Campeonato Paraense: 2014
Boavista
Copa Rio: 2017
External links
1983 births
Living people
Sportspeople from Uberlândia
Brazilian men's footballers
Brazilian football managers
Men's association football forwards
Boavista Sport Club players
Campeonato Brasileiro Série A players
Campeonato Brasileiro Série B players
Campeonato Brasileiro Série C players
J1 League players
K League 1 players
Israeli Premier League players
Brazilian expatriate men's footballers
Expatriate men's footballers in Japan
Expatriate men's footballers in South Korea
Expatriate men's footballers in Israel
Brazilian expatriate sportspeople in Japan
Brazilian expatriate sportspeople in South Korea
Brazilian expatriate sportspeople in Israel
Sport Club Internacional players
Botafogo de Futebol e Regatas players
Vissel Kobe players
Daejeon Hana Citizen players
Ulsan Hyundai FC players
Jeonnam Dragons players
Esporte Clube Vitória players
Sport Club do Recife players
ABC Futebol Clube players
Associação Atlética Ponte Preta players
Associação Desportiva São Caetano players
Rio Branco Esporte Clube players
Hapoel Acre F.C. players
Clube d |
https://en.wikipedia.org/wiki/Nahk | Nahk may refer to:
N-acetylhexosamine 1-kinase, an enzyme
Konstantin Nahk |
https://en.wikipedia.org/wiki/Gliotransmitter | Gliotransmitters are chemicals released from glial cells that facilitate neuronal communication between neurons and other glial cells. They are usually induced from Ca2+ signaling, although recent research has questioned the role of Ca2+ in gliotransmitters and may require a revision of the relevance of gliotransmitters in neuronal signalling in general.
While gliotransmitters can be released from any glial cell, including oligodendrocytes, astrocytes, and microglia, they are primarily released from astrocytes. Astrocytes rely on gap junctions for coupling, and are star-like in shape, which allows them to come into contact with many other synapses in various regions of the brain. Their structure also makes them capable of bidirectional signaling. It is estimated that astrocytes can make contact with over 100,000 synapses, allowing them to play an essential role in synaptic transmission. While gliotransmission primarily occurs between astrocytes and neurons, gliotransmission is not limited to these two cell types. Besides the central nervous system, gliotransmission also occurs among motor nerve terminals and Schwann cells in the peripheral nervous system. Another occurrence of gliotransmission takes place between glial cells in the retina, called Müller cells, and retinal neurons.
Function
The word “glia”, derived from the Greek words γλία and γλοία ("glue"), illustrates the original belief among scientists that these cells play a passive role in neural signaling, be |
https://en.wikipedia.org/wiki/GJA1 | Gap junction alpha-1 protein (GJA1), also known as connexin 43 (Cx43), is a protein that in humans is encoded by the GJA1 gene on chromosome 6. As a connexin, GJA1 is a component of gap junctions, which allow for gap junction intercellular communication (GJIC) between cells to regulate cell death, proliferation, and differentiation. As a result of its function, GJA1 is implicated in many biological processes, including muscle contraction, embryonic development, inflammation, and spermatogenesis, as well as diseases, including oculodentodigital dysplasia (ODDD), heart malformations, and cancers.
Structure
GJA1 is a 43.0 kDa protein composed of 382 amino acids. GJA1 contains a long C-terminal tail, an N-terminal domain, and multiple transmembrane domains. The protein passes through the phospholipid bilayer four times, leaving its C- and N-terminals exposed to the cytoplasm. The C-terminal tail is composed of 50 amino acids and includes post-translational modification sites, as well as binding sites for transcription factors, cytoskeleton elements, and other proteins. As a result, the C-terminal tail is central to functions such as regulating pH gating and channel assembly. Notably, the DNA region of the GJA1 gene encoding this tail is highly conserved, indicating that it is either resistant to mutations or becomes lethal when mutated. Meanwhile, the N-terminal domain is involved in channel gating and oligomerization and, thus, may control the switch between the channel's open |
https://en.wikipedia.org/wiki/Nahcolite | Nahcolite is a soft, colourless or white carbonate mineral with the composition of sodium bicarbonate (NaHCO3) also called thermokalite. It crystallizes in the monoclinic system.
Nahcolite was first described in 1928 for an occurrence in a lava tunnel at Mount Vesuvius, Italy. Its name refers to the elements which compose it: Na, H, C, and O. It occurs as a hot spring and saline lake precipitate or efflorescence; in differentiated alkalic massifs; in fluid inclusions as a daughter mineral phase and in evaporite deposits.Nahcolite data on Webmineral
It occurs in association with trona, thermonatrite, thenardite, halite, gaylussite, burkeite, northupite and borax. It has been reported in a Roman conduit at Stufe de Nerone, Campi Flegrei, near Naples; in the U. S. from Searles Lake, San Bernardino County, California; in the Green River Formation, Colorado and Utah; in the Tincalayu deposit, Salar del Hombre Muerto,
Salta Province, Argentina; on Mt. Alluaiv, Lovozero Massif and Khibiny Massif, Kola Peninsula, Russia; and around Mount Erebus, Victoria Land, Antarctica.
References
Carbonate minerals
Sodium minerals
Monoclinic minerals
Minerals in space group 14
Industrial minerals |
https://en.wikipedia.org/wiki/Muravanaja%20A%C5%A1mianka | Muravanaya Ashmyanka (, ) is the village in the Hrodna Voblast of Belarus, located 11 km NW from Ashmyany and 28 km from railway station Ashmyany. In 1999, there were 338 villagers and 134 dwellings.
The village is the administrative center of the local rural council and collective farm, has a hospital and a high school. There still remains the ruined printing house, which was owned in beginning of the 17th century by Krzysztof Dorohostajski, and was the printing place of the Salinarius "Censura" in 1615 (the brick building completed possibly in 1590, converted to the palace residence in the 19th century). Also, there's Catholic church of Virgin Mary (wooden structure with a belltower, example of Baroque and Classicism and of folk wooden architecture; built in the end of the 18th — beginning of the 19th century, renewed in 1841 and 1874). During World War II (around May 1944) the village was the site of a battle between Polish resistance and Lithuanian auxiliary Local Lithuanian Detachment.
References
Belarusian Encyclopedia, Vol.11, 2000; Collection of Historical and Cultural Artifacts of Belarus, Hrodna Voblast volume, 1986.
Villages in Belarus
Vilnius Voivodeship
Oshmyansky Uyezd
Wilno Voivodeship (1926–1939) |
https://en.wikipedia.org/wiki/Proper%20zero-signal%20collector%20current | Consider an NPN transistor circuit. During the positive half-cycle of the signal, the base is positive with respect to the emitter and hence the base-emitter junction is forward biased. This causes a base current and much larger collector current to flow. The positive half-cycle of the signal is amplified in the collector. During the negative half-cycle, the base-emitter junction is reverse biased and hence no current flows. No output flows during the negative half-cycle of the signal. Thus the positive-only amplified output is unfaithful.
A sufficient battery source in the base circuit keeps the input circuit forward biased even during the peak of
the negative half-cycle. When no signal is applied, a DC current I C will flow in the collector circuit due to the battery. This is known as zero signal collector current.
The value of zero signal collector current should be at least equal to the maximum collector current due to AC signal alone.
References
Transistors
Semiconductor devices |
https://en.wikipedia.org/wiki/Statistical%20epidemiology | Statistical epidemiology is an emerging branch of the disciplines of epidemiology and biostatistics that aims to:
Bring more statistical rigour to bear in the field of epidemiology
Recognise the importance of applied statistics, especially with respect to the context in which statistical methods are appropriate and inappropriate
Aid and improve our interpretation of observations
Introduction
The science of epidemiology has had enormous growth, particularly with charity and government funding. Many researchers have been trained to conduct studies, requiring multiple skills ranging from liaising with clinical staff to the statistical analysis of complex data, such as using Bayesian methods. The role of a Statistical Epidemiologist is to bring the most appropriate methods available to bear on observational study from medical research, requiring a broad appreciation of the underpinning methods and their context of applicability and interpretation.
The earliest mention of this phrase was in an article by EB Wilson, taking a critical look at the way in which statistical methods were developing and being applied in the science of epidemiology.
Academic recognition
There are two Professors of Statistical Epidemiology in the United Kingdom (University of Leeds and Imperial College, London) and a Statistical Epidemiology group (Oxford University).
Related fields
Statistical epidemiology draws upon quantitative methods from fields such as: statistics, operations research |
https://en.wikipedia.org/wiki/Engage%20the%20Enzyme | Engage the Enzyme is the sixth album by rapper, Young MC. The album was released in 2002 for Stimulus Records. The album did not make it to the album charts; however it did feature the hit single "Heatseeker."
Track listing
"Intro"- 1:10
"Stress Test"- 5:36
"Feel the Love"- 3:45
"Heatseeker"- 4:03
"Whop de Whoop"- 4:34
"Flows"- 5:14
"Unsigned Diva"- 4:34
"Babe"- 6:03
"Crucial"- 6:41
"One Time for Your Mind"- 4:39
"Ain't No Way in the World"- 4:22
"In Case"- 4:22
"Without Doubt"- 4:26
"Easier"- 5:37
"Heatseeker" (Remix)- 4:29
"Feel the Love" (Remix)- 4:12
Young MC albums
2002 albums |
https://en.wikipedia.org/wiki/4-Hydroxybutyrate%20dehydrogenase | In enzymology, a 4-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-hydroxybutanoate + NAD+ succinate semialdehyde + NADH + H+
The two substrates of this enzyme are therefore 4-hydroxybutanoic acid, and NAD+, whereas its 3 products are succinate semialdehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxybutanoate:NAD+ oxidoreductase. This enzyme is also called gamma-hydroxybutyrate dehydrogenase. This enzyme participates in butanoate metabolism and the degradation of the neurotransmitter 4-hydroxybutanoic acid.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Baytown%20Nature%20Center | The Baytown Nature Center is located in Baytown, Texas, east of Houston. It is located on a peninsula along the Houston Ship Channel and surrounded on three sides by Burnet Bay, Crystal Bay, and Scott Bay.
The Baytown Nature Center is both a recreation area and a wildlife sanctuary that is home to hundreds of bird species, mammals, reptiles, and aquatic species. The City of Baytown created this Nature Center in 1994. The SWA Group's Houston office provided land planning and landscape architectural services.
History
The Baytown Nature Center was, for many years, a highly desirable residential neighborhood known as Brownwood with nearly 400 substantial homes on a peninsula.
In 1961, Hurricane Carla devastated the Texas Gulf Coast, flooding most of Brownwood and ending any new development in the area. Afterwards, subsidence became a serious problem as industrial and municipal water users along the Houston Ship Channel and in the general Houston area pumped out groundwater faster than natural forces could replenish the aquifer(s). Thus, during the 1970s and 1980s, much of the Texas Gulf Coast (including most of Brownwood) sank a total of 10 to . Brownwood, which had previously been high and dry, was repeatedly inundated by high tides and storms.
In 1983, extensive damage from Hurricane Alicia finally led to the abandonment of most of Brownwood's homes. The City of Baytown started buying out the properties of neighborhood residents. In 1984, the City prepared its first ma |
https://en.wikipedia.org/wiki/Johns%20Hopkins%20Beast | The Johns Hopkins Beast was a mobile automaton, an early pre-robot, built in the 1960s at the Johns Hopkins University Applied Physics Laboratory. The machine had a rudimentary intelligence and the ability to survive on its own. As it wandered through the white halls of the laboratory, it would seek black wall outlets. When it found one it would plug in and recharge.
The robot was cybernetic. It did not use a computer. Its control circuitry consisted of dozens of transistors controlling analog voltages. It used photocell optics and sonar to navigate. The 2N404 transistors were used to create NOR logic gates that implemented the Boolean logic to tell it what to do when a specific sensor was activated. The 2N404 transistors were also used to create timing gates to tell it how long to do something. 2N1040 Power transistors were used to control the power to the motion treads, the boom, and the charging mechanism.
The original sensors in Mod I were physical touch only. The wall socket was detected by physical switches on the arm that followed the wall. Once detected, two electrical prongs were extended until they entered the wall socket and made the electrical connection to charge the vehicle. The stairway, doors, and pipes on the hall wall were also detected by physical switches and recognized by appropriate logic.
The sonar guidance system was developed for Mod I and improved for Mod II. It used two ultrasonic transducers to determine distance, location within the halls, a |
https://en.wikipedia.org/wiki/Flamencology | Flamencology, from the Spanish word Flamencología, is an academic discipline pertaining to the Flamenco arts. It combines research, documentation, and other techniques to achieve the diffusion and preservation of the art.
Etymology
The term was coined in 1955 by Spanish Argentine author Anselmo González Clement in a publication of the same year utilizing the term as its title. The Real Academia Española included the term in a revision of the Spanish dictionary through the efforts of the Granadine writer Luis Rosales. The term was diffused as early as 1958 by a group of erudites known as the Cátedra de Jerez in Jerez de la Frontera, Spain.
Institutionalization
The Discipline is institutionalized throughout the Andalucía region in southern Spain. Institutions such as the Universidad de Sevilla (University of Seville) and the Universidad de Córdoba (Córdoba University) offer specialization in this discipline.
In Modern Practice
The discipline is put into practice through various publications or lectures. Some examples of publications are Revista Alma 100, Revista El Olivo, and Flamenco World.com.
Propagation
The extent to which the discipline is practiced varies on the growth of general knowledge of the Flamenco arts. Since the beginning, it has been the purpose of Flamencologists to diffuse the art both locally and abroad, and with the diffusion of the art later come the methods of documenting and researching the art thus putting Flamencology into practice.
In practice |
https://en.wikipedia.org/wiki/Georgetown%20Hoyas%20women%27s%20lacrosse | The Georgetown Hoyas women's lacrosse team competes in the Big East Conference, an NCAA Division I conference. The first team was formed in 1977.
Historical statistics
*Statistics through 2018 season
Current team
The current head coach is Ricky Fried, who took over after Kim Simons retired following the 2004 season. Previously, Fried held the positions of assistant coach from 2002 to 2003 and associate head coach from 2003 to 2004, both under Simons.
The current assistant coaches are Erin Wellner-Hellmold and Michi Ellers. Hellmold played for Fried at Johns Hopkins University. Ellers played under Simons, with Fried as assistant coach, at Georgetown from 2002 to 2004.
History
The Georgetown Women's Lacrosse team advanced to two National Championship games in 2001 and 2002. The team appeared in 9 consecutive NCAA tournaments from 1998 to 2006 and advanced to 3 NCAA Final Four games in 2001, 2002, and 2004. The team had an undefeated record in the Big East from 2001 to 2006, earning them 6 consecutive Conference Championships. In 2007, the women's lacrosse team was defeated by Syracuse University in the first ever Big East women's lacrosse tournament. However, the Hoyas had previously been crowned the Big East Regular-Season Champions.
2006 season
In 2006, the Georgetown Women's lacrosse team continued to be a household name on the national scene. The team started the 2006 season ranked number 10/12 in National Polls and climbed all the way to earn the number 3 see |
https://en.wikipedia.org/wiki/Rafael%20Bruschweiler | Rafael Brüschweiler is a scientist who studies nuclear magnetic resonance (NMR). He is credited for the development of Covariance NMR, which shortens the NMR measurement time for multidimensional spectra of both solution and solid-state NMR. It also allows for easier analysis and interpretation. For this achievement he was awarded the Laukien Prize in NMR Spectroscopy at the 47th Experimental Nuclear Magnetic Resonance Conference (ENC). He is also a leading scientist in NMR-based metabolomics and protein NMR.
Rafael Brüschweiler is currently a professor of Dept. Chemistry & Biochemistry, executive chair of Campus Chemical Instrument Center (CCIC)-NMR at Ohio State University since 2013 summer, and associate director for biophysics at the National High Magnetic Field Laboratory since 2004. He was a George M. Edgar Professor of Dept. Chemistry & Biochemistry at The Florida State University from 2004 to 2013. Prior to this he was a professor of chemistry at Clark University where he held the Gustaf H. Carlson Chair.
Rafael Brüschweiler obtained his Ph.D. in physical chemistry from ETH, Zürich under supervision of Nobel Laureate Richard R. Ernst, and did his postdoctoral research at the Scripps Research Institute (Advisor: P. E. Wright and D. A. Case). He is a fellow of the American Association for the Advancement of Science (AAAS) and a fellow of the American Physical Society (APS).
References
Brüschweiler Research Group | Brüschweiler Research Group at OSU Department of Che |
https://en.wikipedia.org/wiki/Chapman%E2%80%93Robbins%20bound | In statistics, the Chapman–Robbins bound or Hammersley–Chapman–Robbins bound is a lower bound on the variance of estimators of a deterministic parameter. It is a generalization of the Cramér–Rao bound; compared to the Cramér–Rao bound, it is both tighter and applicable to a wider range of problems. However, it is usually more difficult to compute.
The bound was independently discovered by John Hammersley in 1950, and by Douglas Chapman and Herbert Robbins in 1951.
Statement
Let be the set of parameters for a family of probability distributions on .
For any two , let be the -divergence from to . Then:
A generalization to the multivariable case is:
Proof
By the variational representation of chi-squared divergence:
Plug in , to obtain: Switch the denominator and the left side and take supremum over to obtain the single-variate case. For the multivariate case, we define for any . Then plug in in the variational representation to obtain: Take supremum over , using the linear algebra fact that , we obtain the multivariate case.
Relation to Cramér–Rao bound
Usually, is the sample space of independent draws of a -valued random variable with distribution from a by parameterized family of probability distributions, is its -fold product measure, and is an estimator of . Then, for , the expression inside the supremum in the Chapman–Robbins bound converges to the Cramér–Rao bound of when , assuming the regularity conditions of the Cramér–Rao bound hold. This impli |
https://en.wikipedia.org/wiki/Siegel%E2%80%93Tukey%20test | In statistics, the Siegel–Tukey test, named after Sidney Siegel and John Tukey, is a non-parametric test which may be applied to data measured at least on an ordinal scale. It tests for differences in scale between two groups.
The test is used to determine if one of two groups of data tends to have more widely dispersed values than the other. In other words, the test determines whether one of the two groups tends to move, sometimes to the right, sometimes to the left, but away from the center (of the ordinal scale).
The test was published in 1960 by Sidney Siegel and John Wilder Tukey in the Journal of the American Statistical Association, in the article "A Nonparametric Sum of Ranks Procedure for Relative Spread in Unpaired Samples."
Principle
The principle is based on the following idea:
Suppose there are two groups A and B with n observations for the first group and m observations for the second (so there are N = n + m total observations). If all N observations are arranged in ascending order, it can be expected that the values of the two groups will be mixed or sorted randomly, if there are no differences between the two groups (following the null hypothesis H0). This would mean that among the ranks of extreme (high and low) scores, there would be similar values from Group A and Group B.
If, say, Group A were more inclined to extreme values (the alternative hypothesis H1), then there will be a higher proportion of observations from group A with low or high values, |
https://en.wikipedia.org/wiki/Dynamic%20frequency%20scaling | Dynamic frequency scaling (also known as CPU throttling) is a power management technique in computer architecture whereby the frequency of a microprocessor can be automatically adjusted "on the fly" depending on the actual needs, to conserve power and reduce the amount of heat generated by the chip. Dynamic frequency scaling helps preserve battery on mobile devices and decrease cooling cost and noise on quiet computing settings, or can be useful as a security measure for overheated systems (e.g. after poor overclocking).
Dynamic frequency scaling almost always appear in conjunction with dynamic voltage scaling, since higher frequencies require higher supply voltages for the digital circuit to yield correct results. The combined topic is known as dynamic voltage and frequency scaling (DVFS).
Processor throttling is also known as "automatic underclocking". Automatic overclocking (boosting) is also technically a form of dynamic frequency scaling, but it's relatively new and usually not discussed with throttling.
Operation
The dynamic power (switching power) dissipated by a chip is C·V2·A·f, where C is the capacitance being switched per clock cycle, V is voltage, A is the Activity Factor indicating the average number of switching events per clock cycle by the transistors in the chip (as a unitless quantity) and f is the clock frequency.
Voltage is therefore the main determinant of power usage and heating. The voltage required for stable operation is determined by the freque |
https://en.wikipedia.org/wiki/Interpolis | Interpolis is one of largest insurance companies in the Netherlands. The company has gained wide recognition with its advertising campaign "Interpolis.Crystal clear". Besides financial compensation, Interpolis also offers compensation in kind.
Interpolis Office Concept
In addition to insurance, Interpolis is also known for its special outlook on work. No one at Interpolis has their own fixed place of work. The employees can select a place of work that is best suited to them and to the work that they do. Special areas called ‘club houses’ have also been created at the Interpolis head office, each with its own particular atmosphere. In these club houses the Interpolis employees can combine various daily activities, such as working, consulting, meeting people, relaxing and eating. The flexible working concept, of Activity Based Working, led to a cultural transition at Interpolis. That is because flexible working is not just a matter of moving some furniture around. Flexible working must also become embedded in the way you think and act. Employees at Interpolis do not have to clock in. The motto at Interpolis is: as long as the work gets done. Whether that is done from home or at the office is something the employees can decide for themselves. Interpolis is a pioneer of teleworking in the Netherlands. At the moment about 2,500 employees work from home several days a week.
History
Interpolis came into existence in 1969 after a merger between the life insurance company BTL and |
https://en.wikipedia.org/wiki/KdV%20hierarchy | In mathematics, the KdV hierarchy is an infinite sequence of partial differential equations which contains the Korteweg–de Vries equation.
Details
Let be translation operator defined on real valued functions as . Let be set of all analytic functions that satisfy , i.e. periodic functions of period 1. For each , define an operator
on the space of smooth functions on . We define the Bloch spectrum to be the set of such that there is a nonzero function with and . The KdV hierarchy is a sequence of nonlinear differential operators such that for any we have an analytic function and we define to be and
,
then is independent of .
The KdV hierarchy arises naturally as a statement of Huygens' principle for the D'Alembertian.
Explicit equations for first three terms of hierarchy
The first three partial differential equations of the KdV hierarchy are
where each equation is considered as a PDE for for the respective .
The first equation identifies and as in the original KdV equation. These equations arise as the equations of motion from the (countably) infinite set of independent constants of motion by choosing them in turn to be the Hamiltonian for the system. For , the equations are called higher KdV equations and the variables higher times.
Application to periodic solutions of KdV
One can consider the higher KdVs as a system of overdetermined PDEs for
Then solutions which are independent of higher times above some fixed and with periodic boundary conditio |
https://en.wikipedia.org/wiki/Turbine%20%28disambiguation%29 | A turbine is a rotary mechanical device that extracts energy from a fluid flow.
Turbine may also refer to:
In software
Turbine, Inc., a software company
Apache Turbine, a rapid development web application framework
Ships
Turbine-class destroyer, a class of Italian warships mainly used during World War II
Italian destroyer Turbine, a World War I destroyer of the Nembo class
Other uses
TURBINE (US government project)
Turbine, Ontario
1. FFC Turbine Potsdam, a women's football team in Potsdam, Germany
Mohamed Tabarsi, a character nicknamed Turbine in the Japanese Shaman King manga series
Turbine interchange, a road interchange between two freeways
Sunday Tribune, a defunct Irish newspaper, informally called the Turbine
Turbine (album), a 1994 album by The Walk
Turbines (album), a 2013 album by Tunng
A former roller coaster at Walibi Belgium |
https://en.wikipedia.org/wiki/IEEE%20Transactions%20on%20Semiconductor%20Manufacturing | The IEEE Transactions on Semiconductor Manufacturing is a quarterly peer-reviewed scientific journal published by the IEEE. It covers research on semiconductor device fabrication, including simulation and modeling from the factory to the detailed process level, defect control, yield analysis and optimization, production planning and scheduling, environmental issues in semiconductor manufacturing, and manufacturability improvement. The editor-in-chief is Reha Uzsoy (North Carolina State University). According to the Journal Citation Reports, the journal has a 2020 impact factor of 2.874.
The journal is a joint publication of the IEEE Solid-State Circuits Society, IEEE Components, Packaging & Manufacturing Technology Society, IEEE Electron Devices Society, and the IEEE Reliability Society.
References
External links
Transactions on Semiconductor Manufacturing
Semiconductor journals
Quarterly journals
Academic journals established in 1988
English-language journals |
https://en.wikipedia.org/wiki/Strombine%20dehydrogenase | In enzymology, a strombine dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-(carboxymethyl)-D-alanine + NAD+ + H2O glycine + pyruvate + NADH + H+
The 3 substrates of this enzyme are N-(carboxymethyl)-D-alanine, NAD+, and H2O, whereas its 4 products are glycine, pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-(carboxymethyl)-D-alanine:NAD+ oxidoreductase (glycine-forming). Other names in common use include strombine[N-(carboxymethyl)-D-alanine]dehydrogenase, and N-(carboxymethyl)-D-alanine: NAD+ oxidoreductase.
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xanthine%20dehydrogenase | Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.
Function
Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The enzyme is a homodimer. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification.
Xanthine dehydrogenase catalyzes the following chemical reaction:
xanthine + NAD+ + H2O urate + NADH + H+
The three substrates of this enzyme are xanthine, NAD+, and H2O, whereas its three products are urate, NADH, and H+.
This enzyme participates in purine metabolism.
Nomenclature
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xanthine:NAD+ oxidoreductase. Other names in common use include NAD+-xanthine dehydrogenase, xanthine-NAD+ oxidoreductase, xanthine/NAD+ oxidoreductase, and xanthine oxidoreductase.
Clinical significance
Defects in xanthine dehydrogenase cause xanthinuria, may contribute to adult respiratory stress syndrome, and may potentiate influenza infection through an oxygen metabolite-dependent mechanism. It has been shown that patients with lung adenocarcinoma tumors which have high levels of XDH gene expression have lower survivals. Addiction to XDH protein has been used to target NSCLC tumors and cell lines in a prec |
https://en.wikipedia.org/wiki/Xanthoxin%20dehydrogenase | In enzymology, a xanthoxin dehydrogenase () is an enzyme that catalyzes the chemical reaction
xanthoxin + NAD+ abscisic aldehyde + NADH + H+
Thus, the two substrates of this enzyme are xanthoxin and NAD+, whereas its 3 products are abscisic aldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xanthoxin:NAD+ oxidoreductase. Other names in common use include xanthoxin oxidase, and ABA2. This enzyme participates in carotenoid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Salicylaldehyde%20dehydrogenase | In enzymology, a salicylaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
salicylaldehyde + NAD+ + H2O salicylate + NADH + 2 H+
The 3 substrates of this enzyme are salicylaldehyde, NAD+, and H2O, whereas its 3 products are salicylate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is salicylaldehyde:NAD+ oxidoreductase. This enzyme participates in naphthalene and anthracene degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sarcosine%20dehydrogenase | In enzymology, sarcosine dehydrogenase () is a mitochondrial enzyme that catalyzes the chemical reaction N-demethylation of sarcosine to give glycine. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is sarcosine:acceptor oxidoreductase (demethylating). Other names in common use include sarcosine N-demethylase, monomethylglycine dehydrogenase, and sarcosine:(acceptor) oxidoreductase (demethylating). Sarcosine dehydrogenase is closely related to dimethylglycine dehydrogenase, which catalyzes the demethylation reaction of dimethylglycine to sarcosine. Both sarcosine dehydrogenase and dimethylglycine dehydrogenase use FAD as a cofactor. Sarcosine dehydrogenase is linked by electron-transferring flavoprotein (ETF) to the respiratory redox chain.
The general chemical reaction catalyzed by sarcosine dehydrogenase is:
sarcosine + acceptor + H2O glycine + formaldehyde + reduced acceptor
Structure
There is no crystal structure available for sarcosine dehydrogenase. Sarcosine dehydrogenase contains a covalently bound FAD group " linked via the 8 alpha position of the isoalloxazine ring to an imidazole N(3) of a histidine residue". The enzyme, according to Freisell Wr. et al., also contains non-heme iron in a ratio of 1 or 2 iron per 300000g of enzyme, and 0.5 mol of acid soluble sulfur suggesting that the electron transfer during the first step in the rea |
https://en.wikipedia.org/wiki/Sequoyitol%20dehydrogenase | In enzymology, a sequoyitol dehydrogenase () is an enzyme that catalyzes the chemical reaction
5-O-methyl-myo-inositol + NAD+ 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
Thus, the two substrates of this enzyme are 5-O-methyl-myo-inositol and NAD+, whereas its 3 products are 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5-O-methyl-myo-inositol:NAD+ oxidoreductase. This enzyme is also called D-pinitol dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Serine%202-dehydrogenase | In enzymology, a serine 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-serine + H2O + NAD+ 3-hydroxypyruvate + NH3 + NADH + H+
The 3 substrates of this enzyme are L-serine, H2O, and NAD+, whereas its 4 products are 3-hydroxypyruvate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-serine:NAD+ 2-oxidoreductase (deaminating). Other names in common use include L-serine:NAD+ oxidoreductase (deaminating), and serine dehydrogenase.
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Serine%203-dehydrogenase | In enzymology, a serine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-serine + NADP+ 2-ammoniomalonate semialdehyde + NADPH + H+
Thus, the two substrates of this enzyme are L-serine and NADP+, whereas its 3 products are 2-ammoniomalonate semialdehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-serine:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Shikimate%20dehydrogenase | In enzymology, a shikimate dehydrogenase () is an enzyme that catalyzes the chemical reaction
shikimate + NADP+ 3-dehydroshikimate + NADPH + H+
Thus, the two substrates of this enzyme are shikimate and NADP+, whereas its 3 products are 3-dehydroshikimate, NADPH, and H+. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
Function
Shikimate dehydrogenase is an enzyme that catalyzes one step of the shikimate pathway. This pathway is found in bacteria, plants, fungi, algae, and parasites and is responsible for the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) from the metabolism of carbohydrates. In contrast, animals and humans lack this pathway hence products of this biosynthetic route are essential amino acids that must be obtained through an animal's diet.
There are seven enzymes that play a role in this pathway. Shikimate dehydrogenase (also known as 3-dehydroshikimate dehydrogenase) is the fourth step of the seven step process. This step converts 3-dehydroshikimate to shikimate as well as reduces NADP+ to NADPH.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is shikimate:NADP+ 3-oxidoreductase. Other names in common use include:
dehydroshikimic reductase,
shikimate oxidoreductase,
shikimate:NADP+ oxidoreductase,
5-dehydroshikimate reductase,
shikimate 5 |
https://en.wikipedia.org/wiki/Sorbitol-6-phosphate%202-dehydrogenase | In enzymology, a sorbitol-6-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-sorbitol 6-phosphate + NAD+ D-fructose 6-phosphate + NADH + H+
Thus, the two substrates of this enzyme are D-sorbitol 6-phosphate and NAD+, whereas its 3 products are D-fructose 6-phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase. Other names in common use include ketosephosphate reductase, ketosephosphate reductase, D-sorbitol 6-phosphate dehydrogenase, D-sorbitol-6-phosphate dehydrogenase, sorbitol-6-P-dehydrogenase, and D-glucitol-6-phosphate dehydrogenase. This enzyme participates in fructose and mannose metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sorbose%20dehydrogenase | In enzymology, a sorbose dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-sorbose + acceptor 5-dehydro-D-fructose + reduced acceptor
Thus, the two substrates of this enzyme are L-sorbose and acceptor, whereas its two products are 5-dehydro-D-fructose and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is L-sorbose:acceptor 5-oxidoreductase. This enzyme is also called L-sorbose:(acceptor) 5-oxidoreductase.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Spermidine%20dehydrogenase | In enzymology, a spermidine dehydrogenase () is an enzyme that catalyzes the chemical reaction
spermidine + acceptor + H2O propane-1,3-diamine + 4-aminobutanal + reduced acceptor
The 3 substrates of this enzyme are spermidine, acceptor, and H2O, whereas its 3 products are propane-1,3-diamine, 4-aminobutanal, and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is spermidine:acceptor oxidoreductase. This enzyme is also called spermidine:(acceptor) oxidoreductase. This enzyme participates in urea cycle and metabolism of amino groups and beta-alanine metabolism. It has 2 cofactors: FAD, and Heme.
References
EC 1.5.99
Flavoproteins
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinate-semialdehyde%20dehydrogenase | In enzymology, a succinate-semialdehyde dehydrogenase (SSADH) () is an enzyme that catalyzes the chemical reaction
succinate semialdehyde + NAD+ + H2O succinate + NADH + 2 H+
The 3 substrates of this enzyme are succinate semialdehyde, NAD+, and H2O, whereas its 3 products are succinate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate-semialdehyde:NAD+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase, succinic semialdehyde dehydrogenase, succinyl semialdehyde dehydrogenase, and succinate semialdehyde:NAD+ oxidoreductase. This enzyme participates in glutamate and butyrate metabolism.
Succinate-semialdehyde dehydrogenase is found in organisms ranging across the tree of life from bacteria to humans. It is important in the degradation of γ-aminobutyric acid in humans, and deficiency of the enzyme causes serious health effects (succinic semialdehyde dehydrogenase deficiency).
In bacteria, the enzyme is also involved in γ-aminobutyric acid degradation, but can be recruited to facilitate other functions, such as converting succinate-semialdehyde formed during fission of the pyridine ring to succinic acid for entry into the Krebs Cycle.
References
Further reading
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinylglutamate-semialdehyde%20dehydrogenase | In enzymology, a succinylglutamate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O N-succinyl-L-glutamate + NADH + 2 H+
The 3 substrates of this enzyme are N-succinyl-L-glutamate 5-semialdehyde, NAD+, and H2O, whereas its 3 products are N-succinyl-L-glutamate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-succinyl-L-glutamate 5-semialdehyde:NAD+ oxidoreductase. Other names in common use include succinylglutamic semialdehyde dehydrogenase, N-succinylglutamate 5-semialdehyde dehydrogenase, SGSD, AruD, and AstD. This enzyme participates in arginine and proline metabolism.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfite%20dehydrogenase | In enzymology, a sulfite dehydrogenase () is an enzyme that catalyzes the chemical reaction
sulfite + 2 ferricytochrome c + H2O sulfate + 2 ferrocytochrome c + 2 H+
The 3 substrates of this enzyme are sulfite, ferricytochrome c, and H2O, whereas its 3 products are sulfate, ferrocytochrome c, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is sulfite:ferricytochrome-c oxidoreductase. Other names in common use include sulfite cytochrome c reductase, sulfite-cytochrome c oxidoreductase, and sulfite oxidase. This enzyme participates in sulfur metabolism.
References
EC 1.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ephedrine%20dehydrogenase | In enzymology, an ephedrine dehydrogenase () is an enzyme that catalyzes the chemical reaction
(-)-ephedrine + NAD+ (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
Thus, the two substrates of this enzyme are (-)-ephedrine and NAD+, whereas its 3 products are (R)-2-methylimino-1-phenylpropan-1-ol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-ephedrine:NAD+ 2-oxidoreductase.
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Erythrose-4-phosphate%20dehydrogenase | In enzymology, an erythrose-4-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-erythrose 4-phosphate + NAD+ + H2O 4-phosphoerythronate + NADH + 2 H+
The 3 substrates of this enzyme are D-erythrose 4-phosphate, NAD+, and H2O, whereas its 3 products are 4-phosphoerythronat, NADH, and H+.
[explainpolicedepartment]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-erythrose 4-phosphate:NAD+ oxidoreductase. Other names in common use include erythrose 4-phosphate dehydrogenase, E4PDH, GapB, Epd dehydrogenase, and E4P dehydrogenase. This enzyme participates in vitamin B6 metabolism (see DXP-dependent biosynthesis of pyridoxal phosphate).
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Estradiol%2017alpha-dehydrogenase | In enzymology, an estradiol 17alpha-dehydrogenase () is an enzyme that catalyzes the chemical reaction
estradiol-17alpha + NAD(P)+ estrone + NAD(P)H + H+
The three substrates of this enzyme are estradiol-17alpha, NAD+, and NADP+, whereas its four products are estrone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17alpha-hydroxysteroid:NAD(P)+ 17-oxidoreductase. Other names in common use include 17alpha-estradiol dehydrogenase, 17alpha-hydroxy steroid dehydrogenase, 17alpha-hydroxy steroid oxidoreductase, 17alpha-hydroxysteroid oxidoreductase, and estradiol 17alpha-oxidoreductase. This enzyme participates in androgen and estrogen metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Estradiol%2017beta-dehydrogenase | In enzymology, an estradiol 17beta-dehydrogenase () is an enzyme that catalyzes the chemical reaction
estradiol-17beta + NAD(P)+ estrone + NAD(P)H + H+
The 3 substrates of this enzyme are estradiol-17beta, NAD+, and NADP+, whereas its 4 products are estrone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is estradiol-17beta:NAD(P)+ 17-oxidoreductase. Other names in common use include 20alpha-hydroxysteroid dehydrogenase, 17beta,20alpha-hydroxysteroid dehydrogenase, 17beta-estradiol dehydrogenase, estradiol dehydrogenase, estrogen 17-oxidoreductase, and 17beta-HSD. This enzyme participates in androgen and estrogen metabolism.
Structural studies
As of late 2007, 29 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure
Steroid hormone biosynthesis |
https://en.wikipedia.org/wiki/Vellosimine%20dehydrogenase | In enzymology, a vellosimine dehydrogenase () is an enzyme that catalyzes the chemical reaction
10-deoxysarpagine + NADP+ vellosimine + NADPH + H+
Thus, the two substrates of this enzyme are 10-deoxysarpagine and NADP+, whereas its 3 products are vellosimine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-deoxysarpagine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vomifoliol%20dehydrogenase | In enzymology, a vomifoliol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(6S,9R)-6-hydroxy-3-oxo-alpha-ionol + NAD+ (6R)-6-hydroxy-3-oxo-alpha-ionone + NADH + H+
Thus, the two substrates of this enzyme are (6S,9R)-6-hydroxy-3-oxo-alpha-ionol and NAD+, whereas its 3 products are (6R)-6-hydroxy-3-oxo-alpha-ionone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vomifoliol:NAD+ oxidoreductase. Other names in common use include vomifoliol 4'-dehydrogenase, and vomifoliol:NAD+ 4'-oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetoacetyl-CoA%20reductase | In enzymology, an acetoacetyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
(R)-3-hydroxyacyl-CoA + NADP+ 3-oxoacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are (R)-3-hydroxyacyl-CoA and NADP+, whereas its 3 products are 3-oxoacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase. Other names in common use include acetoacetyl coenzyme A reductase, hydroxyacyl coenzyme-A dehydrogenase, NADP+-linked acetoacetyl CoA reductase, NADPH:acetoacetyl-CoA reductase, D(−)-beta-hydroxybutyryl CoA-NADP+ oxidoreductase, short chain beta-ketoacetyl(acetoacetyl)-CoA reductase, beta-ketoacyl-CoA reductase, D-3-hydroxyacyl-CoA reductase, and (R)-3-hydroxyacyl-CoA dehydrogenase. This enzyme participates in butanoate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acylglycerone-phosphate%20reductase | In enzymology, an acylglycerone-phosphate reductase () is an enzyme that catalyzes the chemical reaction
1-palmitoylglycerol 3-phosphate + NADP+ palmitoylglycerone phosphate + NADPH + H+
Thus, the two substrates of this enzyme are 1-palmitoylglycerol 3-phosphate and NADP+, whereas its 3 products are palmitoylglycerone phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase. Other names in common use include palmitoyldihydroxyacetone-phosphate reductase, palmitoyl dihydroxyacetone phosphate reductase, palmitoyl-dihydroxyacetone-phosphate reductase, acyldihydroxyacetone phosphate reductase, and palmitoyl dihydroxyacetone phosphate reductase. This enzyme participates in glycerophospholipid and ether lipid metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldose%201-dehydrogenase | In enzymology, an aldose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-aldose + NAD+ D-aldonolactone + NADH + H+
Thus, the two substrates of this enzyme are D-aldose and NAD+, whereas its 3 products are D-aldonolactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-aldose:NAD+ 1-oxidoreductase. Other names in common use include aldose dehydrogenase, and dehydrogenase, D-aldohexose.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldose-6-phosphate%20reductase%20%28NADPH%29 | In enzymology, an aldose-6-phosphate reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
D-sorbitol 6-phosphate + NADP+ D-glucose 6-phosphate + NADPH + H+
Thus, the two substrates of this enzyme are D-sorbitol 6-phosphate and NADP+, whereas its 3 products are D-glucose 6-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-aldose-6-phosphate:NADP+ 1-oxidoreductase. Other names in common use include aldose 6-phosphate reductase, NADP+-dependent aldose 6-phosphate reductase, A6PR, aldose-6-P reductase, aldose-6-phosphate reductase, alditol 6-phosphate:NADP+ 1-oxidoreductase, and aldose-6-phosphate reductase (NADPH).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allyl-alcohol%20dehydrogenase | In enzymology, an allyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
allyl alcohol + NADP+ acrolein + NADPH + H+
Thus, the two substrates of this enzyme are allyl alcohol and NADP+, whereas its 3 products are acrolein, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Apiose%201-reductase | In enzymology, an apiose 1-reductase () is an enzyme that catalyzes the chemical reaction
D-apiitol + NAD+ D-apiose + NADH + H+
Thus, the two substrates of this enzyme are D-apiitol and NAD+, whereas its 3 products are D-apiose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-apiitol:NAD+ 1-oxidoreductase. Other names in common use include D-apiose reductase, and D-apiitol reductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-alcohol%20dehydrogenase | In enzymology, an aryl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
an aromatic alcohol + NAD+ an aromatic aldehyde + NADH + H+
Thus, the two substrates of this enzyme are aromatic alcohol and NAD+, whereas its 3 products are aromatic aldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-alcohol:NAD+ oxidoreductase. Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol dehydrogenase. This enzyme participates in 5 metabolic pathways: tyrosine metabolism, phenylalanine metabolism, biphenyl degradation, toluene and xylene degradation, and caprolactam degradation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aryl-alcohol%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Aryl-alcohol dehydrogenase (NADP+)}}
In enzymology, an aryl-alcohol dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
an aromatic alcohol + NADP+ an aromatic aldehyde + NADPH + H+
Thus, the two substrates of this enzyme are aromatic alcohol and NADP+, whereas its 3 products are aromatic aldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-alcohol:NADP+ oxidoreductase. Other names in common use include aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide, phosphate), coniferyl alcohol dehydrogenase, NADPH-linked benzaldehyde reductase, and aryl-alcohol dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzyl-2-methyl-hydroxybutyrate%20dehydrogenase | In enzymology, a benzyl-2-methyl-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP+ benzyl 2-methyl-3-oxobutanoate + NADPH + H+
Thus, the two substrates of this enzyme are benzyl (2R,3S)-2-methyl-3-hydroxybutanoate and NADP+, whereas its 3 products are benzyl 2-methyl-3-oxobutanoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzyl-(2R,3S)-2-methyl-3-hydroxybutanoate:NADP+ 3-oxidoreductase. This enzyme is also called benzyl 2-methyl-3-hydroxybutyrate dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carbonyl%20reductase%20%28NADPH%29 | In enzymology, a carbonyl reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
R-CO-R' + NADPH + H+ :R-CHOH-R' + NADP+
Thus, the two products of this enzyme are R-CHOH-R' and NADP+, whereas its 3 substrates are R-CO-R', NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is secondary-alcohol:NADP+ oxidoreductase. Other names in common use include aldehyde reductase 1, prostaglandin 9-ketoreductase, xenobiotic ketone reductase, NADPH-dependent carbonyl reductase, ALR3, carbonyl reductase, nonspecific NADPH-dependent carbonyl reductase, aldehyde reductase 1, and carbonyl reductase (NADPH). This enzyme participates in arachidonic acid metabolism, and has recently been shown to catabolize S-Nitrosoglutathione, as a means to degrade NO in an NADPH-dependent manner.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Carnitine%203-dehydrogenase | In enzymology, a carnitine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
carnitine + NAD+ 3-dehydrocarnitine + NADH + H+
Thus, the two substrates of this enzyme are carnitine and NAD+, whereas its 3 products are 3-dehydrocarnitine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is carnitine:NAD+ 3-oxidoreductase.
References
External links
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carveol%20dehydrogenase | In enzymology, a carveol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(-)-trans-carveol + NADP+ (-)-carvone + NADPH + H+
Thus, the two substrates of this enzyme are (-)-trans-carveol and NADP+, whereas its 3 products are (-)-carvone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-carveol:NADP+ oxidoreductase. This enzyme is also called (-)-trans-carveol dehydrogenase. This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chlordecone%20reductase | In enzymology, a chlordecone reductase () is an enzyme that catalyzes the chemical reaction
chlordecone alcohol + NADP+ chlordecone + NADPH + H+
Thus, the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cholest-5-ene-3beta%2C7alpha-diol%203beta-dehydrogenase | In enzymology, a cholest-5-ene-3β,7α-diol 3β-dehydrogenase () is an enzyme that catalyzes the chemical reaction
cholest-5-ene-3β,7α-diol + NAD+ 7α-hydroxycholest-4-en-3-one + NADH + H+
Thus, the two substrates of this enzyme are cholest-5-ene-3β,7α-diol and NAD+, whereas its 3 products are 7α-hydroxycholest-4-en-3-one, NADH, and H+.
The systematic name of this enzyme class is cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase. This enzyme is also called 3β-hydroxy-Δ5-C27-steroid oxidoreductase. The human version of this enzyme is known as hydroxy-Δ-5-steroid dehydrogenase, 3 β- and steroid delta-isomerase 7 or HSD3B7 which is encoded by the HSD3B7 gene.
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme is involved in the initial stages of the synthesis of bile acids from cholesterol and a member of the short-chain dehydrogenase/reductase superfamily. This enzyme is a membrane-associated endoplasmic reticulum protein which is active against 7-alpha hydrosylated sterol substrates.
Clinical significance
Mutations in the HSD3B7 gene are associated with a congenital bile acid synthesis defect which leads to neonatal cholestasis, a form of progressive liver disease.
See also
3-beta-HSD
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cholestanetetraol%2026-dehydrogenase | In enzymology, a cholestanetetraol 26-dehydrogenase () is an enzyme that catalyzes the chemical reaction
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NAD+ (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NADH + H+
Thus, the two substrates of this enzyme are (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol and NAD+, whereas its 3 products are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+ 26-oxidoreductase. Other names in common use include cholestanetetraol 26-dehydrogenase, 5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol dehydrogenase, TEHC-NAD oxidoreductase, 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+, and 26-oxidoreductase. This enzyme participates in bile acid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cinnamyl-alcohol%20dehydrogenase | In enzymology, a cinnamyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cinnamyl alcohol + NADP+ cinnamaldehyde + NADPH + H+
Thus, the two substrates of this enzyme are cinnamyl alcohol and NADP+, whereas its 3 products are cinnamaldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cinnamyl-alcohol:NADP+ oxidoreductase. Other names in common use include cinnamyl alcohol dehydrogenase, and CAD. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure
Phenylpropanoids metabolism |
https://en.wikipedia.org/wiki/Codeinone%20reductase%20%28NADPH%29 | In enzymology, a codeinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
codeine + NADP+ codeinone + NADPH + H+
Thus, the two substrates of this enzyme are codeine and NADP+, whereas its 3 products are codeinone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is codeine:NADP+ oxidoreductase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coniferyl-alcohol%20dehydrogenase | In enzymology, a coniferyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
coniferyl alcohol + NADP+ coniferyl aldehyde + NADPH + H+
Thus, the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexane-1%2C2-diol%20dehydrogenase | In enzymology, a cyclohexane-1,2-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
trans-cyclohexane-1,2-diol + NAD+ 2-hydroxycyclohexan-1-one + NADH + H+
Thus, the two substrates of this enzyme are trans-cyclohexane-1,2-diol and NAD+, whereas its 3 products are 2-hydroxycyclohexan-1-one, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trans-cyclohexane-1,2-diol:NAD+ 1-oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexanol%20dehydrogenase | In enzymology, a cyclohexanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cyclohexanol + NAD+ cyclohexanone + NADH + H+
Thus, the two substrates of this enzyme are cyclohexanol and NAD+, whereas its 3 products are cyclohexanone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclohexanol:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclopentanol%20dehydrogenase | In enzymology, a cyclopentanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cyclopentanol + NAD+ cyclopentanone + NADH + H+
Thus, the two substrates of this enzyme are cyclopentanol and NAD+, whereas its 3 products are cyclopentanone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclopentanol:NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinitol%202-dehydrogenase | In enzymology, a D-arabinitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-arabinitol + NAD+ ⇌ D-ribulose + NADH + H+
Thus, the two substrates of this enzyme are D-arabinitol and NAD+, whereas its 3 products are D-ribulose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming). This enzyme is also called D-arabinitol 2-dehydrogenase (ribulose-forming).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinitol%204-dehydrogenase | In enzymology, a D-arabinitol 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-arabinitol + NAD+ D-xylulose + NADH + H+
Thus, the two substrates of this enzyme are D-arabinitol and NAD+, whereas its 3 products are D-xylulose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinitol:NAD+ 4-oxidoreductase. Other names in common use include D-arabitol dehydrogenase and arabitol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
References
Characterization of Arabitol Dehyrogenase in Transplastomic Plants. LAP Lambert Academic Publishing.
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinose%201-dehydrogenase | In enzymology, a D-arabinose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-arabinose + NAD+ D-arabinono-1,4-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-arabinose and NAD+, whereas its 3 products are D-arabinono-1,4-lactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinose:NAD+ 1-oxidoreductase. Other names in common use include NAD+-pentose-dehydrogenase, and arabinose(fucose)dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-iditol%202-dehydrogenase | In enzymology, a -iditol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
-iditol + NAD+ -sorbose + NADH + H+
Thus, the two substrates of this enzyme are -iditol and NAD+, whereas its 3 products are -sorbose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is -iditol:NAD+ 2-oxidoreductase. This enzyme is also called -sorbitol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diethyl%202-methyl-3-oxosuccinate%20reductase | In enzymology, a diethyl 2-methyl-3-oxosuccinate reductase () is an enzyme that catalyzes the chemical reaction
diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP+ diethyl 2-methyl-3-oxosuccinate + NADPH + H+
Thus, the two substrates of this enzyme are diethyl (2R,3R)-2-methyl-3-hydroxysuccinate and NADP+, whereas its 3 products are diethyl 2-methyl-3-oxosuccinate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is diethyl-(2R,3R)-2-methyl-3-hydroxysuccinate:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrobunolol%20dehydrogenase | In enzymology, a dihydrobunolol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1- naphthol + NADP+ (+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)- naphthalenone + NADPH + H+
The three substrates of this enzyme are [[(+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-naphthol]], and NADP+, whereas its 4 products are [[(+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)-]], naphthalenone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-n aphthol:NADP+ oxidoreductase. This enzyme is also termed bunolol reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrokaempferol%204-reductase | In enzymology, a dihydrokaempferol 4-reductase () is an enzyme that catalyzes the chemical reaction
cis-3,4-leucopelargonidin + NADP+ (+)-dihydrokaempferol + NADPH + H+
Thus, the two substrates of this enzyme are cis-3,4-leucopelargonidin and NADP+, whereas its 3 products are (+)-dihydrokaempferol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include dihydroflavanol 4-reductase (DFR), dihydromyricetin reductase, NADPH-dihydromyricetin reductase, and dihydroquercetin reductase. This enzyme participates in flavonoid biosynthesis.
Function
Anthocyanidins, common plant pigments, are further reduced by the enzyme dihydroflavonol 4-reductase (DFR) to the corresponding colorless leucoanthocyanidins.
DFR uses dihydromyricetin (ampelopsin) NADPH and 2 H+ to produce leucodelphinidin and NADP.
A cDNA for DFR has been cloned from the orchid Bromheadia finlaysoniana.
Researchers in Japan have genetically manipulated roses by using RNA interference to knock out endogenous DFR, adding a gene DFR from an iris, and adding a gene for the blue pigment, delphinidin, in an effort to create a blue rose, which is being sold worldwide.
Dihydroflavonol 4-reductase is an enzyme part of the lignin biosynthesis pathway. In Arabidopsis thaliana, the enzyme uses sinap |
https://en.wikipedia.org/wiki/Diiodophenylpyruvate%20reductase | In enzymology, a diiodophenylpyruvate reductase () is an enzyme that catalyzes the chemical reaction
3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH + H+
Thus, the two substrates of this enzyme are 3-(3,5-diiodo-4-hydroxyphenyl)lactate and NAD+, whereas its 3 products are 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-(3,5-diiodo-4-hydroxyphenyl)lactate:NAD+ oxidoreductase. Other names in common use include aromatic alpha-keto acid, KAR, and 2-oxo acid reductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylmalate%20dehydrogenase | In enzymology, a dimethylmalate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-3,3-dimethylmalate + NAD+ 3-methyl-2-oxobutanoate + CO2 + NADH
Thus, the two substrates of this enzyme are (R)-3,3-dimethylmalate and NAD+, whereas its 3 products are 3-methyl-2-oxobutanoate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating). This enzyme is also called beta,beta-dimethylmalate dehydrogenase. This enzyme participates in pantothenate and coa biosynthesis. It has 5 cofactors: ammonia, manganese, cobalt, potassium, and NH4+.
References
EC 1.1.1
NADH-dependent enzymes
Manganese enzymes
Cobalt enzymes
Potassium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-malate%20dehydrogenase%20%28decarboxylating%29 | In enzymology, a D-malate dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
(R)-malate + NAD+ pyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are (R)-malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of a donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-malate:NAD+ oxidoreductase (decarboxylating). Other names in common use include D-malate dehydrogenase, D-malic enzyme, bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). This enzyme participates in butanoate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-pinitol%20dehydrogenase | In enzymology, a D-pinitol dehydrogenase () is an enzyme that catalyzes the chemical reaction
1D-3-O-methyl-chiro-inositol + NADP+ 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+
Thus, the two substrates of this enzyme are 1D-3-O-methyl-chiro-inositol and NADP+, whereas its 3 products are 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase. This enzyme is also called 5D-5-O-methyl-chiro-inositol:NADP+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-dehydro-6-deoxyglucose%20reductase | In enzymology, a dTDP-4-dehydro-6-deoxyglucose reductase () is an enzyme that catalyzes the chemical reaction
dTDP-D-fucose + NADP+ dTDP-4-dehydro-6-deoxy-D-glucose + NADPH + H+
Thus, the two substrates of this enzyme are dTDP-D-fucose and NADP+, whereas its 3 products are dTDP-4-dehydro-6-deoxy-D-glucose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-D-fucose:NADP+ oxidoreductase. This enzyme is also called dTDP-4-keto-6-deoxyglucose reductase. This enzyme participates in polyketide sugar unit biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-dehydrorhamnose%20reductase | In enzymology, a dTDP-4-dehydrorhamnose reductase () is an enzyme that catalyzes the chemical reaction
dTDP-6-deoxy-L-mannose + NADP+ dTDP-4-dehydro-6-deoxy-L-mannose + NADPH + H+
Thus, the two substrates of this enzyme are dTDP-6-deoxy-L-mannose and NADP+, whereas its 3 products are dTDP-4-dehydro-6-deoxy-L-mannose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase. Other names in common use include dTDP-4-keto-L-rhamnose reductase, reductase, thymidine diphospho-4-ketorhamnose, dTDP-4-ketorhamnose reductase, TDP-4-keto-rhamnose reductase, and thymidine diphospho-4-ketorhamnose reductase. This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/DTDP-6-deoxy-L-talose%204-dehydrogenase | In enzymology, a dTDP-6-deoxy-L-talose 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
dTDP-6-deoxy-L-talose + NADP+ dTDP-4-dehydro-6-deoxy-L-mannose + NADPH + H+
Thus, the two substrates of this enzyme are dTDP-6-deoxy-L-talose and NADP+, whereas its 3 products are dTDP-4-dehydro-6-deoxy-L-mannose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase. Other names in common use include thymidine diphospho-6-deoxy-L-talose dehydrogenase, TDP-6-deoxy-L-talose dehydrogenase, thymidine diphospho-6-deoxy-L-talose dehydrogenase, and dTDP-6-deoxy-L-talose dehydrogenase (4-reductase). This enzyme participates in nucleotide sugars metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-galactose%206-dehydrogenase | In enzymology, a dTDP-galactose 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
dTDP-D-galactose + 2 NADP+ + H2O dTDP-D-galacturonate + 2 NADPH + 2 H+
The 3 substrates of this enzyme are dTDP-D-galactose, NADP+, and H2O, whereas its 3 products are dTDP-D-galacturonate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-D-galactose:NADP+ 6-oxidoreductase. This enzyme is also called thymidine-diphosphate-galactose dehydrogenase. This enzyme participates in nucleotide sugars metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
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