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https://en.wikipedia.org/wiki/PDCD6 | Programmed cell death protein 6 is a protein that in humans is encoded by the PDCD6 gene.
This gene encodes a calcium-binding protein belonging to the penta-EF-hand protein family. Calcium binding is important for homodimerization and for conformational changes required for binding to other protein partners. This gene product participates in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death. In mice deficient for this gene product, however, apoptosis was not blocked suggesting this gene product is functionally redundant.
Interactions
PDCD6 has been shown to interact with ASK1, PDCD6IP, Fas receptor, ANXA11 and PEF1.
References
Further reading
External links
Penta-EF-hand proteins |
https://en.wikipedia.org/wiki/Transferrin%20receptor%201 | Transferrin receptor protein 1 (TfR1), also known as Cluster of Differentiation 71 (CD71), is a protein that in humans is encoded by the TFRC gene. TfR1 is required for iron import from transferrin into cells by endocytosis.
Structure and function
TfR1 is a transmembrane glycoprotein composed of two disulfide-linked monomers joined by two disulfide bonds. Each monomer binds one holo-transferrin molecule creating an iron-Tf-TfR complex which enters the cell by endocytosis.
Clinical significance
TfR1 as a potential new target in cases of human leukemia & lymphoma. InatherYs, in Évry, France, developed a candidate drug, INA01 antibody (anti-CD71) that showed efficacy in pre-clinical studies in the therapy of two incurable orphan oncohematological diseases: the adult T cell leukemia (ATLL) caused by HTLV-1 and the Mantle cell lymphoma (MCL).
TfR1 expressed on the endothelial cells of the blood-brain barrier (BBB) is used also in preclinical research to allow the delivery of large molecules including antibodies into the brain. Some of the TfR1 targeting antibodies have been shown to cross the blood-brain barrier, without interfering with the uptake of iron. Amongst those are the mouse anti rat-TfR antibody OX26 and the rat anti mouse-TfR antibody 8D3. The affinity of the antibody-TfR interaction seems to be important determining the success of transcytotic transport over endothelial cells of the BBB. Monovalent TfR interaction favors BBB transport due to altered intracellular |
https://en.wikipedia.org/wiki/Platelet%20membrane%20glycoprotein | Platelet membrane glycoproteins are surface glycoproteins found on platelets (thrombocytes) which play a key role in hemostasis. When the blood vessel wall is damaged, platelet membrane glycoproteins interact with the extracellular matrix.
Receptors involved in platelet adhesion to collagen
Membrane glycoproteins GPIa/IIa, GPVI and probably GPIV as well, function as collagen receptors, engaged in platelet adhesion to collagen. The leading role in the elimination of high-stress injury is taken by the glycoprotein Ib-IX-V complex.
Interactions of the platelet surface glycoproteins
The binding of von Willebrand factor (vWF) results in conformational changes within the GPIb-V-IX complex. In consequence, this complex activates GPIIb / IIIa membrane glycoproteins, allowing them to bind fibrinogen. Fibrinogen molecules then interconnect the platelets, serving as the basis for platelet aggregation. In the absence of fibrinogen, the platelets are joined by vWF due to its ability to bind the activated GPIIb / IIIa complex.
Membrane glycoproteins
Glycoprotein Ib-IX-V complex (GPIb-IX-V)
This transmembrane glycoprotein complex is composed of four subunits: GPIbα, GPIbβ, GPV and GPIX. Each of them has a variable number of leucine-rich repeats. GPIbα and GPIbβ are linked by disulfide bridges, while the GPV and GPIX associate non-covalently with the complex. The GPIbα subunit bears the binding site for von Willebrand factor (vWF), α-thrombin, leukocyte integrin αMβ2 and P-selectin. Th |
https://en.wikipedia.org/wiki/Moving%20average%20crossover | In the statistics of time series, and in particular the stock market technical analysis, a moving-average crossover occurs when, on plotting two moving averages each based on different degrees of smoothing, the traces of these moving averages cross. It does not predict future direction but shows trends. This indicator uses two (or more) moving averages, a slower moving average and a faster moving average. The faster moving average is a short term moving average. For end-of-day stock markets, for example, it may be 5-, 10- or 25-day period while the slower moving average is medium or long term moving average (e.g. 50-, 100- or 200-day period). A short term moving average is faster because it only considers prices over short period of time and is thus more reactive to daily price changes. On the other hand, a long term moving average is deemed slower as it encapsulates prices over a longer period and is more lethargic. However, it tends to smooth out price noises which are often reflected in short term moving averages.
A moving average, as a line by itself, is often overlaid in price charts to indicate price trends. A crossover occurs when a faster moving average (i.e., a shorter period moving average) crosses a slower moving average (i.e. a longer period moving average). In other words, this is when the shorter period moving average line crosses a longer period moving average line. In stock investing, this meeting point is used either to enter (buy or sell) or exit (sell or b |
https://en.wikipedia.org/wiki/Malgrange%20preparation%20theorem | In mathematics, the Malgrange preparation theorem is an analogue of the Weierstrass preparation theorem for smooth functions. It was conjectured by René Thom and proved by .
Statement of Malgrange preparation theorem
Suppose that f(t,x) is a smooth complex function of t∈R and x∈Rn near the origin, and let k be the smallest integer such that
Then one form of the preparation theorem states that near the origin f can be written as the product of a smooth function c that is nonzero at the origin and a smooth function that as a function of t is a polynomial of degree k. In other words,
where the functions c and a are smooth and c is nonzero at the origin.
A second form of the theorem, occasionally called the Mather division theorem, is a sort of "division with remainder" theorem: it says that if f and k satisfy the conditions above and g is a smooth function near the origin, then we can write
where q and r are smooth, and as a function of t, r is a polynomial of degree less than k. This means that
for some smooth functions rj(x).
The two forms of the theorem easily imply each other: the first form is the special case of the "division with remainder" form where g is tk, and the division with remainder form follows from the first form of the theorem as we may assume that f as a function of t is a polynomial of degree k.
If the functions f and g are real, then the functions c, a, q, and r can also be taken to be real. In the case of the Weierstrass preparation theorem the |
https://en.wikipedia.org/wiki/5-HT1B%20receptor | {{DISPLAYTITLE:5-HT1B receptor}}
5-hydroxytryptamine receptor 1B also known as the 5-HT1B receptor is a protein that in humans is encoded by the HTR1B gene. The 5-HT1B receptor is a 5-HT receptor subtype.
Tissue distribution and function
5-HT1B receptors are widely distributed throughout the central nervous system with the highest concentrations found in the frontal cortex, basal ganglia, striatum, and the hippocampus.
The function of the 5-HT1B receptor differs depending upon its location. In the frontal cortex, it is believed to act as a postsynaptic receptor inhibiting the release of dopamine. In the basal ganglia and the striatum, evidence suggests 5-HT signaling acts on an autoreceptor, inhibiting the release of serotonin and decreasing glutamatergic transmission by reducing miniature excitatory postsynaptic potential (mEPSP) frequency, respectively. In the hippocampus, a recent study has demonstrated that activation of postsynaptic 5-HT1B heteroreceptors produces a facilitation in excitatory synaptic transmission which is altered in depression.
When the expression of 5-HT1B in human cortex was traced throughout life, significant changes during adolescence were observed, in a way that is strongly correlated with the expression of 5-HT1E.
Outside of the CNS, the 5-HT1B receptor is also expressed on the endothelium of blood vessels, particularly in the meninges. Activation of these receptors results in vasoconstriction. The high distribution of vasoconstrictive 5-HT |
https://en.wikipedia.org/wiki/5-HT1D%20receptor | {{DISPLAYTITLE:5-HT1D receptor}}
5-hydroxytryptamine (serotonin) receptor 1D, also known as HTR1D, is a 5-HT receptor, but also denotes the human gene encoding it. 5-HT1D acts on the central nervous system, and affects locomotion and anxiety. It also induces vasoconstriction in the brain.
Tissue distribution and function
5HT1D receptors are found at low levels in the basal ganglia (globus pallidus, substantia nigra, caudate putamen), the hippocampus, and in the cortex.
Structure
5HT1D receptor is a G protein linked receptor that activates an intracellular messenger cascade to produce an inhibitory response by decreasing cellular levels of cAMP. The 5HT1D is a 7-TM receptor. A large intercellular loop between TM-5 and TM-6 is believed to be associated with coupling to a second messenger. Agonists might bind in a manner that utilizes an aspartate residue in TM-3 and residues in the TM-4, TM-5 and TM-6. A human clone containing an intronless open reading frame was found to encode 377 amino acids of the 5HT1D receptor. The gene has been localized on chromosome 1, region 1p34.3-36.3
Ligands
Agonists
Molecular modelling has provided a picture of the agonistic binding site of 5HT1D. The amino acid residues within the receptor binding site region have been identified. This is a valuable guide to design potential 5HT1D receptor agonists.
When sumatriptan binds there is major conformational change in both ligand and receptor in the binding pocket.
5-(Nonyloxy)tryptamine
Sumatri |
https://en.wikipedia.org/wiki/List%20of%20Shorea%20species | This is a complete listing of Shorea species as accepted in Plants of the World Online as of July 2019. The subgeneric classification follows Ashton (2004) and covers only species native to northern Borneo, with some Sri Lankan species added. The timber groups classified according to the system proposed by Symington in the early 1940s.
Based on phylogenomic analyses showing that genus Shorea sensu Ashton (1982) is polyphyletic, in 2022 Ashton and Heckenhauer proposed reviving the former genera Doona Thwaites, Pentacme A.DC., and Richetia F.Heim, and raising Shorea section Anthoshorea to genus rank. Plants of the World Online currently recognizes Anthoshorea, Doona, and Pentacme as separate genera.
Shorea classification
References
Ashton, P.S. Dipterocarpaceae. In Tree Flora of Sabah and Sarawak, Volume 5, 2004. Soepadmo, E., Saw, L.G. and Chung, R.C.K. eds. Government of Malaysia, Kuala Lumpur, Malaysia.
Sorting Shorea names
Shorea |
https://en.wikipedia.org/wiki/Farangbaia%20Forest%20Reserve | Farangbaia Forest Reserve is a forest reserve with a rainforest ecosystem in Sierra Leone. The Reserve covers an area of 1,260 hectares, is located approximately 10 km to the south-east of the town of Bumbuna and forms part of the catchment area for the Seli River. Since the outbreak of Sierra Leone civil war in 1991 much of the reserve has become farmland and bush forest and there a number sawmills operating there.
References
See also
Protected areas of Sierra Leone
Northern Province, Sierra Leone
Forest reserves of Sierra Leone |
https://en.wikipedia.org/wiki/7P | 7P may refer to:
7P
7P/Pons-Winnecke, comet
Batavia Air, IATA-Code, Indonesian Airline
7p, an arm of Chromosome 7 (human)
7P, a Classification of steam locomotives by British Railways, denoting a locomotive rated for the largest of Passenger trains
7P, the production code for the 1989 Doctor Who serial Survival
7Ps
Seven Ps marketing terminology
See also
P7 (disambiguation) |
https://en.wikipedia.org/wiki/Robert%20B.%20Dome | Robert B. Dome (October 12, 1905 - January 18, 1996) was an American electrical engineer credited with inventing frequency interlace color television modulation, which was compatible with existing black and white television sets.
Dome received his BSEE in 1926 from Purdue University, and worked for General Electric in Syracuse, New York. He also invented techniques for audio transmission, and received the 1951 IEEE Morris N. Liebmann Memorial Award "for many technical contributions to the profession, but notably his contributions to the inter-carrier sound system of television reception, wide band phase shift networks, and various simplifying innovations in FM receiver circuits." He was also a licensed radio amateur and a respected technical contributor to that community as W2WAM and may have held other call signs at other times (help needed).
Selected works
"Wide band phase shift networks", Electronics, vol. 19, pages 112-115. December 1946.
"Frequency interlace color television", Electronics, pages 70–75. September 1950.
Television principles, New York, McGraw-Hill, 1951.
"Spectrum Utilization in Color Television", Proceedings of the IRE, volume 39, issue 10, pages 1323-1331, October 1951.
"The delta sound system for television receivers", IRE Transactions on Audio, volume 7, issue 1, January 1959, Pages 16–21.
References
US Patent 2,635,140: Frequency Interlace Television System
US Patent 2,831,916: Single-carrier Color Television Systems
Early Days of Color |
https://en.wikipedia.org/wiki/National%20Bureau%20of%20Statistics%20of%20China | The National Bureau of Statistics () is a deputy-cabinet level agency directly under the State Council of China. Established in August 1952, the bureau is responsible for collection, investigation, research and publication of statistics concerning the nation's economy, population and other aspects of the society.
Kang Yi has served as the commissioner of the bureau since 3 March 2022.
Responsibilities
The bureau's authority and responsibilities are defined in Statistics Law of the People's Republic of China. It is responsible for the research of the nation's overall statistics and oversee the operations of its local counterparts.
Organizations
The bureau is led by a commissioner, with several deputy commissioners (currently four), a chief methodologist, a chief economist, and a chief information officer. It is composed of 18 departments, oversees 12 affiliated institutions and manages 32 survey organizations stationed in respective provinces. It also operates China Statistics Press (), which was founded in 1955.
The national bureau has 535 employees as authorized by the State Council.
Commissioner
Xue Muqiao (August 1952 – November 1958)
Jia Qiyun (November 1958 – June 1961)
Wang Sihua (June 1961 – December 1969)
Chen Xian (September 1974 – October 1981)
Li Chengrui (October 1981 – May 1984)
Zhang Sai (May 1984 – February 1997)
Liu Hong (February 1997 – June 2000)
Zhu Zhixin (June 2000 – March 2003)
Li Deshui (March 2003 – March 2006)
Qiu Xiaohua (March 2006 – Octobe |
https://en.wikipedia.org/wiki/National%20Bureau%20of%20Statistics | National Bureau of Statistics may refer to:
National Bureau of Statistics of China
National Bureau of Statistics of Moldova
National Bureau of Statistics, Nigeria
National Bureau of Statistics of Tanzania
Australian Bureau of Statistics
See also
List of national and international statistical services |
https://en.wikipedia.org/wiki/Nylsvley%20Nature%20Reserve | Nylsvley Nature Reserve is a protected area, located on and beside the seasonally-inundated floodplain of the Nyl River, the uppermost section of the Mogalakwena which has a very shallow gradient. It is located near Mookgophong in the Limpopo Province of South Africa. The area has been declared a Ramsar wetland site because of its international conservation importance. The floodplain is made up of extensive reedbeds and grassveld surrounded by open woodland.
Situated in the upper catchment area of the Nyl River, and covering about 20% of the floodplain, the area boasts some 370 bird species – of which more than 100 are waterfowl – and during peak floods, over 80,000 birds are to be seen. The reserve is also home to roan antelope and tsessebe. The only stands of wild rice in South Africa, Oryza longistaminata, are to be found here.
The name 'Nylsvley' originated in vlei, a pan or seasonally flooded area, and in the word for "Nile". In the 1860s, a Voortrekker group of farmers saw a large flooded plain and a river flowing northwards and according to legend considered it to be the Nylrivier (Nile river).
Pictures
References
External links
Friends of Nylsvley
Nylsvley Nature Reserve, Limpopo
Protected areas of Limpopo
Nature reserves in South Africa
Floodplains of Africa
Mogalakwena River
Ramsar sites in South Africa |
https://en.wikipedia.org/wiki/PIK3CG | Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform is an enzyme that in humans is encoded by the PIK3CG gene.
Function
This gene encodes a protein that belongs to the pi3/pi4-kinase family of proteins. The gene product is an enzyme that phosphorylates phosphoinositides on the 3-hydroxyl group of the inositol ring. It is an important modulator of extracellular signals, including those elicited by E-cadherin-mediated cell-cell adhesion, which plays an important role in maintenance of the structural and functional integrity of epithelia. In addition to its role in promoting assembly of adherens junctions, the protein is thought to play a pivotal role in the regulation of cytotoxicity in NK cells. The gene is located in a commonly deleted segment of chromosome 7 previously identified in myeloid leukemias.
Interactions
PIK3CG has been shown to interact with:
BCR gene,
KRAS,
PIK3CD, and
PIK3R5.
See also
Class I PI 3-kinases
p87PIKAP
References
Further reading
Cell signaling
EC 2.7.1 |
https://en.wikipedia.org/wiki/Four%20occupations | The four occupations (), or "four categories of the people" (), was an occupation classification used in ancient China by either Confucian or Legalist scholars as far back as the late Zhou dynasty and is considered a central part of the fengjian social structure (c. 1046–256 BC). These were the shi (gentry scholars), the nong (peasant farmers), the gong (artisans and craftsmen), and the shang (merchants and traders).
The four occupations were not always arranged in this order. The four categories were not socioeconomic classes; wealth and standing did not correspond to these categories, nor were they hereditary.
The system did not factor in all social groups present in premodern Chinese society, and its broad categories were more an idealization than a practical reality. The commercialization of Chinese society in the Song and Ming periods further blurred the lines between these four occupations. The definition of the identity of the shi class changed over time—from warriors, to aristocratic scholars, and finally to scholar-bureaucrats. There was also a gradual fusion of the wealthy merchant and landholding gentry classes, culminating in the late Ming dynasty.
In some manner this system of social order was adopted throughout the Chinese cultural sphere. In Japanese it is called , although in Japan it became a hereditary caste system. In Korean it is called "Sa, nong, gong, sang" (사농공상), and in Vietnamese is called "Sĩ, nông, công, thương (士農工商). The main difference in ada |
https://en.wikipedia.org/wiki/PSEN2 | Presenilin-2 is a protein that (in humans) is encoded by the PSEN2 gene.
Function
Alzheimer's disease (AD) patients with an inherited form of the disease carry mutations in the presenilin proteins (PSEN1; PSEN2) or the amyloid precursor protein (APP). These disease-linked mutations result in increased production of the longer form of amyloid-beta (main component of amyloid deposits found in AD brains). Presenilins are postulated to regulate APP processing through their effects on gamma-secretase, an enzyme that cleaves APP. Also, it is thought that the presenilins are involved in the cleavage of the Notch receptor, such that they either directly regulate gamma-secretase activity or themselves are protease enzymes. Two alternative transcripts of PSEN2 have been identified.
In melanocytic cells PSEN2 gene expression may be regulated by MITF.
Interactions
PSEN2 has been shown to interact with:
BCL2-like 1,
CAPN1,
CIB1,
Calsenilin,
FHL2,
FLNB,
KCNIP4,
Nicastrin, and
UBQLN1.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Early-Onset Familial Alzheimer Disease
Alzheimer's disease |
https://en.wikipedia.org/wiki/Proto-oncogene%20tyrosine-protein%20kinase%20Src | Proto-oncogene tyrosine-protein kinase Src, also known as proto-oncogene c-Src, or simply c-Src (cellular Src; pronounced "sarc", as it is short for sarcoma), is a non-receptor tyrosine kinase protein that in humans is encoded by the SRC gene. It belongs to a family of Src family kinases and is similar to the v-Src (viral Src) gene of Rous sarcoma virus. It includes an SH2 domain, an SH3 domain and a tyrosine kinase domain. Two transcript variants encoding the same protein have been found for this gene.
c-Src phosphorylates specific tyrosine residues in other tyrosine kinases. It plays a role in the regulation of embryonic development and cell growth. An elevated level of activity of c-Src is suggested to be linked to cancer progression by promoting other signals. Mutations in c-Src could be involved in the malignant progression of colon cancer. c-Src should not be confused with CSK (C-terminal Src kinase), an enzyme that phosphorylates c-Src at its C-terminus and provides negative regulation of Src's enzymatic activity.
c-Src was originally discovered by American scientists J. Michael Bishop and Harold E. Varmus, for which they were awarded the 1989 Nobel Prize in Physiology or Medicine.
Discovery
In 1979, J. Michael Bishop and Harold E. Varmus discovered that normal chickens possess a gene that is structurally closely related to v-Src. The normal cellular gene was called c-src (cellular-src). This discovery changed the current thinking about cancer from a model wherein |
https://en.wikipedia.org/wiki/UDPGT | UDPGT may refer to:
Glucuronosyltransferase, an enzyme
UDP glucuronosyltransferase 1 family, polypeptide A1, an enzyme |
https://en.wikipedia.org/wiki/HBD | Hemoglobin subunit delta is a protein that in humans is encoded by the HBD gene.
Function
The delta (HBD) and beta (HBB) genes are normally expressed in the adult: two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin. Two alpha chains plus two delta chains constitute HbA2, which with HbF comprises the remaining 3% of adult hemoglobin. Five beta-like globin genes are found within a 45 kb cluster on chromosome 11 in the following order: 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'.
Clinical significance
Mutations in the delta-globin gene are associated with Delta-thalassemia.
See also
Hemoglobin
Human β-globin locus
Thalassemia
References
Further reading
Hemoglobins |
https://en.wikipedia.org/wiki/Sp3%20transcription%20factor | Sp3 transcription factor, also known as SP3, refers to both a protein and the gene it is encoded by.
This gene belongs to a family of Sp1 related genes that encode transcription factors that regulate transcription by binding to consensus GC- and GT-box regulatory elements in target genes. This protein contains a zinc finger DNA-binding domain and several transactivation domains, and has been reported to function as a bifunctional transcription factor that either stimulates or represses the transcription of numerous genes. Transcript variants encoding different isoforms have been described for this gene, and one has been reported to initiate translation from a non-AUG (AUA) start codon. Additional isoforms, resulting from the use of alternate downstream translation initiation sites, have also been noted.
Interactions
Sp3 transcription factor has been shown to interact with Histone deacetylase 2, PIAS1, E2F1 and GABPA.
References
Further reading
Transcription factors |
https://en.wikipedia.org/wiki/Muscarinic%20acetylcholine%20receptor%20M4 | {{DISPLAYTITLE:Muscarinic acetylcholine receptor M4}}
The muscarinic acetylcholine receptor M4, also known as the cholinergic receptor, muscarinic 4 (CHRM4), is a protein that, in humans, is encoded by the CHRM4 gene.
Function
M4 muscarinic receptors are coupled to Gi/o heterotrimeric proteins.
They function as inhibitory autoreceptors for acetylcholine. Activation of M4 receptors inhibits acetylcholine release in the striatum. The M2 subtype of acetylcholine receptor functions similarly as an inhibitory autoreceptor to acetylcholine release, albeit functioning actively primarily in the hippocampus and cerebral cortex.
Muscarinic acetylcholine receptors possess a regulatory effect on dopaminergic neurotransmission. Activation of M4 receptors in the striatum inhibit D1-induced locomotor stimulation in mice. M4 receptor-deficient mice exhibit increased locomotor simulation in response to D1 agonists, amphetamine and cocaine. Neurotransmission in the striatum influences extrapyramidal motor control, thus alterations in M4 activity may contribute to conditions such as Parkinson's disease.
Ligands
Orthosteric agonists
acetylcholine
carbachol
oxotremorine
Positive allosteric modulators
LY-2033298
VU-0152100 (ML-108)
VU-0152099
Antagonists
AFDX-384 (mixed M2/M4 antagonist, N-[2-[2-[(Dipropylamino)methyl]-1-piperidinyl]ethyl]-5,6-dihydro-6-oxo-11H-pyrido[2,3-b][1,4]benzodiazepine-11-carboxamide, CAS# 118290-27-0)
Dicycloverine
Himbacine
Mamba toxin 3
PD-102,807 |
https://en.wikipedia.org/wiki/Victor%20H.%20Rumsey | Victor Henry Rumsey (November 22, 1919 – March 11, 2015) was an electrical engineer, best known for his studies of frequency-independent antennas.
Rumsey was born in Devizes, Wiltshire, England, on Saint Cecilia's day, and received his BA in mathematics (1941) and Sc.D. in physics from Cambridge University. From 1941–1945 he performed radar research at the Telecommunications Research Establishment in England and the Naval Research Laboratory, Washington, D.C. After three years at the Canadian Atomic Research Laboratory he became director of the Antenna Laboratory at Ohio State University. In 1954 he moved to the University of Illinois, in 1957 to the University of California, Berkeley, and in 1966 to the University of California, San Diego where he was a professor and, later, professor emeritus.
Starting in the 1950s, Rumsey suggested the basic principles for frequency-independent antennas which culminated in the writing of a book on the topic (see selected works below).
Rumsey is a member of the National Academy of Engineering, and has received an honorary Doctor of Engineering degree from Tohoku University, Japan, the 1962 IEEE Morris N. Liebmann Memorial Award, and the 2004 John Kraus Antenna Award.
Selected works
"Frequency-Independent Antennas", IRE National Convention Record, vol. 5, part 1, 1957, pages 114-118.
Frequency Independent Antennas, New York: Academic Press, Inc., 1966.
References
IEEE Transactions on Antennas and Propagation, vol. 52, no. 12, Decem |
https://en.wikipedia.org/wiki/Ian%20Munro%20Ross | Ian Munro Ross FREng (15 August 1927 – 10 March 2013) was an early pioneer in transistors, and for 12 years President of Bell Labs.
Ross was born in Southport, England, and in 1948 received his bachelor's degree in electrical engineering from Gonville and Caius College, Cambridge University. In 1952 he received his M.A. and PhD degrees in electrical engineering from Cambridge.
In 1952 William Shockley hired him to work in semiconductors at Bell Labs, and he arrived in Murray Hill just after John Bardeen and Walter Houser Brattain had left. Shockley's group focused exclusively on transistor improvements, and Ross and G. C. Dacey were instrumental in the early stages of development of the field-effect transistor. In 1960 Ross and others invented epitaxy. He subsequently rose through managerial ranks, ultimately serving as the sixth President of Bell Labs 1979–1991 and overseeing its reorganization following the breakup of the Bell System.
In 1979, he was a resident of Rumson, New Jersey.
Ross was a member of the National Academy of Engineering, National Academy of Sciences, and Royal Academy of Engineering, and a fellow of the American Association for the Advancement of Science and the Institute of Electrical and Electronics Engineers. He received the 1963 IEEE Morris N. Liebmann Memorial Award "for contributions to the development of the epitaxial transistor and other semiconductor devices", the 1987 IRI Medal from the Industrial Research Institute in recognition for his c |
https://en.wikipedia.org/wiki/Paul%20K.%20Weimer | Dr. Paul K. Weimer (November 5, 1914 – January 6, 2005) was a noted contributor to the development of television and the thin-film transistor (TFT).
Weimer was born in Wabash, Indiana. He received a B.A. in math and physics from Manchester University (Indiana) in 1936, an M.A. in physics from the University of Kansas in 1938, and a Ph.D. in physics from Ohio State University in 1942. He then joined the RCA laboratory in Princeton, New Jersey, where he worked until retirement in 1981.
His first assignment was to develop an electron multiplier to go with the Image Orthicon. This tube, which proved to be 100 times more sensitive than its predecessors, was used for the first 20 years of television broadcasting in the United States. In 1961, Weimer began making thin-film transistors in a coplanar process on glass substrates. In a typical process, he would deposit a gold source and drain, then deposit polycrystalline semiconductor material, and place a gate on top. After he placed an insulator between the gate and semiconductor, he got excellent results, as published in his 1962 paper, "The TFT: A New Thin-Film Transistor", in the Proceedings of the IRE.
Weimer held over 90 patents, and was a member of the National Academy of Engineering and fellow of the Institute for Radio Engineers. He received the IRE Television Prize, the 1966 IEEE Morris N. Liebmann Memorial Award, an individual RCA David Sarnoff Outstanding Achievement Award in Science, and the 1986 Kultur Preis of the Ge |
https://en.wikipedia.org/wiki/Fatkat | Fatkat Animation was an animation studio located in Miramichi, New Brunswick.
History
The company was formed from animators who left Helix Animation in 1999. It was owned and operated by Gene Fowler and his employees. This company was started in Halifax, Nova Scotia, and was taken over by Trainingscape, which saw the creation of over 40 training films for various companies, but as of 2009, it's now known as Oasis Animation.
In the winter of 2003, Trainingscape disbanded and that was when Fowler decided to move Fatkat to his hometown of Miramichi, New Brunswick. Fatkat worked on the film Curious George (2006), television shows such as Happy Tree Friends, Caillou (Season 3 only), Carl², Family Guy, Odd Job Jack, Skunk Fu!, Supernormal, Chaotic, Jimmy Two-Shoes, and Three Delivery. They had major clients such as I Can't Believe It's Not Butter!, Pepsi, Microsoft, and Toyota.
Setbacks
Fatkat was, at one point, considered the largest animation studio in Atlantic Canada and the fastest growing animation studio in Canada. However, after government funding for the studio dried up under the Harper government, the 2007-2010 economic crisis occurred and the fact that the business plan didn't actually set a goal of making money, Fatkat eventually dwindled until its closure was announced in May 2009.
At the time of closure, the company was down to employing only 3 people, even though it had received $1 million in government grants since 2005 under the government.
2009–present
Fowler |
https://en.wikipedia.org/wiki/Dipterocarp%20timber%20classification | The following table associates tree species, wood name and wood colour.
Dipterocarpaceae
Wood |
https://en.wikipedia.org/wiki/Meneghinite | Meneghinite is a sulfosalt mineral with the chemical formula CuPb13 Sb7S24.
In the orthorhombic crystal system, meneghinite has a Mohs hardness of , one perfect cleavage and a conchoidal fracture. It is a blackish lead-grey in colour and gives a black shining streak. Its lustre is metallic.
Discovered in the Italian Province of Lucca in 1852, it is named after Giuseppe Meneghini (1811–1889) of the University of Pisa, who first observed the species. The Bottino Mine in Lucca is the type locality.
References
Sulfosalt minerals
Lead minerals
Copper(I) minerals
Antimony minerals
Orthorhombic minerals
Minerals in space group 62 |
https://en.wikipedia.org/wiki/Climate%20of%20Zambia | The climate of Zambia in Central and Southern Africa is definitely tropical modified by altitude (elevation). In the Köppen climate classification, most of the country is classified as humid subtropical or tropical wet and dry, with small patches of semi-arid steppe climate in the south-west.
Climate and specifically rainfall amount is the chief determinant of type and distribution of the ecoregions of Zambia. So technically, Zambia is a very arid country with a humid and subtropical year with small patches of semi arid steppe.
Seasons
There are two main seasons: the rainy season (November to April) corresponding to summer, and the dry season (May to October/November), corresponding to winter. The dry season is subdivided into the cool dry season (May to August), and the hot dry season (September to October/November). The modifying influence of altitude gives the country pleasant subtropical weather rather than tropical conditions for most of the year.
Rainy season
Rainfall varies over a range of per year (most areas fall into the range of ). The distinction between rainy and dry seasons is marked with no rain at all falling in June, July and August. Much of the economic, cultural and social life of the country is dominated by the onset and end of the rainy season, and the amount of rain it brings. Failure of the rains causes hunger in most cases. The average temperature in Zambia in the summer season is 30 °C and in the winter (colder season) it can get as low as 5 °C. T |
https://en.wikipedia.org/wiki/Podocalyxin | Podocalyxin, a sialoglycoprotein, is thought to be the major constituent of the glycocalyx of podocytes in the glomerulus (Bowman's capsule) in the kidneys. It is a member of the CD34 family of transmembrane sialomucins. It coats the secondary foot processes of the podocytes. It is negatively charged and thus functions through charge repulsion to keep adjacent foot processes separated, thereby keeping the urinary filtration barrier open. This function is further supported by knockout studies in mice which reveal an essential role in podocyte morphogenesis and a role in the opening of vascular lumens and regulation of vascular permeability. Of note, this is the only cell surface sialomucin knockout known to display a lethal phenotype.
Podocalyxin is also upregulated in a number of cancers and is frequently associated with poor prognosis. Podocalyxin is important for us to potentially provide a better understanding of cancer development and its aggressiveness through induced cell migration and the invasion from interacting with the actin-binding protein EZR. Affects of the EZR-dependent signaling events, among many other signal disturbances, can lead to increased activity in other vital pathways of cancer cells. Sialylated, O-glycosylated glycoforms of podocalyxin expressed by colon carcinoma cells possess L-selectin and E-selectin binding activity, and the affinity of the binding may be pivotal to the metastatic spread of colon carcinoma cells. At the cellular level podocal |
https://en.wikipedia.org/wiki/%28a%2Cb%2C0%29%20class%20of%20distributions | In probability theory, a member of the (a, b, 0) class of distributions is any distribution of a discrete random variable N whose values are nonnegative integers whose probability mass function satisfies the recurrence formula
for some real numbers a and b, where .
Only the Poisson, binomial and negative binomial distributions satisfy the full form of this relationship. These are also the three discrete distributions among the six members of the natural exponential family with quadratic variance functions (NEF–QVF).
More general distributions can be defined by fixing some initial values of pj and applying the recursion to define subsequent values. This can be of use in fitting distributions to empirical data. However, some further well-known distributions are available if the recursion above need only hold for a restricted range of values of k: for example the logarithmic distribution and the discrete uniform distribution.
The (a, b, 0) class of distributions has important applications in actuarial science in the context of loss models.
Properties
Sundt proved that only the binomial distribution, the Poisson distribution and the negative binomial distribution belong to this class of distributions, with each distribution being represented by a different sign of a. Furthermore, it was shown by Fackler that there is a universal formula for all three distributions, called the (united) Panjer distribution.
The more usual parameters of these distributions are determined |
https://en.wikipedia.org/wiki/Falerno%20del%20Massico | Falerno del Massico is an Italian red wine of DOC produced in the province of Caserta in the region of Campania. It received DOC classification in 1989. Falerno is produced in the same region as the highly regarded falernian wine of ancient Rome. As of 2012, there are forty-four Falerno del Massico Wines produced in this DOC region.
References
Wines of Campania |
https://en.wikipedia.org/wiki/Epitympanic%20recess | The epitympanic recess is the portion of the tympanic cavity (of the middle ear) situated superior to the tympanic membrane. The recess lodges the head of malleus, and the body of incus.
The mastoid antrum is situated posterior to the recess and opens into the recess at the posterior wall of the recess via the aditus to mastoid antrum. The ampulla of the lateral semicircular canal creates a prominence upon the medial wall of the recess.
Clinical significance
This recess is a possible route of spread of infection to the mastoid air cells located in the mastoid process of the temporal bone of the skull. Inflammation which has spread to the mastoid air cells is very difficult to drain and causes considerable pain. Before the advent of antibiotics, it could only be drained by drilling a hole in the mastoid bone, a process known as mastoidectomy.
References
Foramina of the skull |
https://en.wikipedia.org/wiki/Sequence%20step%20algorithm | A sequence step algorithm (SQS-AL) is an algorithm implemented in a discrete event simulation system to maximize resource utilization. This is achieved by running through two main nested loops: A sequence step loop and a replication loop. For each sequence step, each replication loop is a simulation run that collects crew idle time for activities in that sequence step. The collected crew idle times are then used to determine resource arrival dates for user-specified confidence levels. The process of collecting the crew idle times and determining crew arrival times for activities on a considered sequence step is repeated from the first to the last sequence step.
See also
Computational resource
Linear scheduling method
References
Further reading
Photios G. Ioannou and Chachrist Srisuwanrat Sequence Step Algorithm for Continuous Resource Utilization in Probabilistic Repetitive Projects
Scheduling algorithms
Network theory |
https://en.wikipedia.org/wiki/Case%20mix%20group | A case mix group (CMG) is used in patient classification system to group together patients with similar characteristics. This provides a basis for describing the types of patients a hospital or other health care provider treats (its case mix). Case mix groups are used as the basis for the Health Insurance Prospective Payment System (HIPPS) rate codes used by Medicare in its prospective payment systems.
Case mix groups are designed to aggregate acute care inpatients that are similar clinically and in terms of resource use. Acute care inpatients are assigned to groups based on clinical and administrative data collected via the Discharge Abstract Database (DAD).
References
Medicare and Medicaid (United States) |
https://en.wikipedia.org/wiki/Ecoregions%20of%20Zambia | The biomes and ecoregions in the ecology of Zambia are described, listed and mapped here, following the World Wildlife Fund's classification scheme for terrestrial ecoregions, and the WWF freshwater ecoregion classification for rivers, lakes and wetlands.
Zambia is in the Zambezian region of the Afrotropical biogeographic realm (or ecozone). Three terrestrial biomes are well represented in the country (with an additional one extending a few kilometres over the border).
The distribution of the biomes and ecoregions is governed mainly by the physical environment, especially climate.
Physical environment
The main aspects of the physical environment which determine the biomes and ecoregions of Zambia are: climate, specifically rainfall amount, length of the dry season, and temperature, which is related to elevation; and soils and bushfires.
Climate
Rainfall
Rainfall amount is the most important determinant of the type and distribution of ecoregions. Zambia experiences good rainfall, with extremes of 500 to 1400 mm (most areas fall into the range 700 to ) in a distinct rainy season of four to six months centred on January, when the moist intertropical convergence zone is over the country. The highest rainfall is in the north (about 1200 mm –- all figures are annual amounts), especially the north-west (1400 mm), decreasing towards the south (around 700 mm); the driest areas are in the Luangwa and middle Zambezi valleys (500 mm). None of the country is arid.
Dry season and droug |
https://en.wikipedia.org/wiki/LSH | LSH may refer to:
Computing
LSH (hash function), in cryptography
lsh, a UNIX secure shell
Locality-sensitive hashing, in algorithms
Ship types
Landing Ship Headquarters, UK Royal Navy
Landing Ship, Heavy, a hull classification symbol, Australian and US Navy
Other uses
Lashio Airport, Myanmar (IATA: LSH)
Legion of Super-Heroes, a fictional team in DC Comics
Lysergic acid hydroxyethylamide, an alkaloid
See also
Lash (disambiguation)
Lish (disambiguation)
LSHS (disambiguation)
Lush (disambiguation) |
https://en.wikipedia.org/wiki/Eosphorite | Eosphorite is a brown (occasionally pink) manganese hydrous phosphate mineral with chemical formula: MnAl(PO4)(OH)2·H2O. It is used as a gemstone.
Eosphorite crystallizes in the monoclinic crystal system. It forms slender prismatic crystals which often form radiating or spherical clusters. The crystals often show pseudo–orthorhombic forms due to twinning.
Eosphorite forms a series with childrenite, the iron rich member, with divalent iron replacing most of the manganese in the crystal lattice. The two endmembers are isostructural but differ in their properties, such as crystal habit, coloration, and optical properties.
It was first described in 1878 for an occurrence in the Branchville Mica Mine in Branchville, Fairfield County, Connecticut, US. Its name is derived from the Greek έωσφορος for "dawn-bearing," because of its pink color. It occurs worldwide typically as a secondary mineral in phosphate rich granitic pegmatites in association with rhodochrosite, lithiophilite, triphylite, triploidite, dickinsonite, albite, cookeite, apatite, beryllonite, hydroxyl-herderite, and tourmaline. An attractive combination of eosphorite and rose quartz occurs at Taquaral, Minas Gerais, Brazil.
References
Phosphate minerals
Orthorhombic minerals
Minerals in space group 64
Gemstones |
https://en.wikipedia.org/wiki/Squamous%20cell%20papilloma | A squamous cell papilloma is a generally benign papilloma that arises from the stratified squamous epithelium of the skin, lip, oral cavity, tongue, pharynx, larynx, esophagus, cervix, vagina or anal canal. Squamous cell papillomas are typically associated with human papillomavirus (HPV) while sometimes the cause is unknown.
Types
Oral squamous cell papilloma
Squamous cell papilloma of the mouth or throat is generally diagnosed in people between the ages of 30 and 50, and is normally found on the inside of the cheek, on the tongue, or inside of lips. Oral papillomas are usually painless, and not treated unless they interfere with eating or are causing pain. They do not generally mutate to cancerous growths, nor do they normally grow or spread. Oral papillomas are most usually a result of the infection with types HPV-6 and HPV-11.
Conjunctival squamous cell papilloma
Normally found in children or young adults, a common cause of conjunctival squamous cell papilloma is during childbirth, when the mother passes the virus to her child.
Diagnosis
It appears as an exophytic mass made of cauliflower appearance. The lesion may be white, red, or normal in color. It appears as sessile or pedunculated mass. Histopathology typically shows papillomatous protrusions and/or dysplasia.
Treatment
While most cases require no treatment, therapy options include cryotherapy, application of a topical salicylic acid compound, surgical excision and laser ablation.
References
External links
|
https://en.wikipedia.org/wiki/Dimedone | Dimedone is an organic compound with the formula . Classified as a cyclic diketone, it is a derivative of 1,3-cyclohexanedione. It is a white solid that is soluble in water, as well as ethanol and methanol. It once was used as a reagent to test for the aldehyde functional group.
Synthesis
Dimedone is prepared from mesityl oxide and diethyl malonate via a Michael addition reaction.
Chemical properties
Tautomerism
Dimedone is in equilibrium with its tautomer in solution — in a 2:1 keto to enol ratio in chloroform.
Crystalline dimedone contains chains of molecules, in the enol form, linked by hydrogen bonds:
Reaction with aldehydes
Dimedone reacts with aldehydes to give crystalline derivatives, whose melting points can be used to distinguish between aldehydes.
References
Diketones
3-Hydroxypropenals |
https://en.wikipedia.org/wiki/16-hydroxysteroid%20epimerase | In enzymology, a 16-hydroxysteroid epimerase () is an enzyme that catalyzes the chemical reaction
16alpha-hydroxysteroid 16beta-hydroxysteroid
Hence, this enzyme has one substrate, 16alpha-hydroxysteroid, and one product, 16beta-hydroxysteroid.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on other compounds. The systematic name of this enzyme class is 16-hydroxysteroid 16-epimerase.
References
EC 5.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-acetolactate%20mutase | In enzymology, a 2-acetolactate mutase () is an enzyme that catalyzes the chemical reaction
2-acetolactate 3-hydroxy-3-methyl-2-oxobutanoate
Hence, this enzyme has one substrate, 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-acetolactate methylmutase. Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. This enzyme participates in valine, leucine and isoleucine biosynthesis.
References
EC 5.4.99
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-aminohexano-6-lactam%20racemase | In enzymology, a 2-aminohexano-6-lactam racemase () is an enzyme that catalyzes the chemical reaction
L-2-aminohexano-6-lactam D-2-aminohexano-6-lactam
Hence, this enzyme has one substrate, L-2-aminohexano-6-lactam, and one product, D-2-aminohexano-6-lactam.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is 2-aminohexano-6-lactam racemase. This enzyme is also called alpha-amino-epsilon-caprolactam racemase.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-chloro-4-carboxymethylenebut-2-en-1%2C4-olide%20isomerase | In enzymology, a 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase () is an enzyme that catalyzes the chemical reaction
cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide
Hence, this enzyme has one substrate, cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide, and one product, trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 2-chloro-4-carboxymethylenebut-2-en-1,4-olide cis-trans-isomerase. Other names in common use include 2-chlorocarboxymethylenebutenolide isomerase, and chlorodienelactone isomerase. This enzyme participates in 1,4-dichlorobenzene degradation.
References
EC 5.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-methyleneglutarate%20mutase | In enzymology, a 2-methyleneglutarate mutase () is an enzyme that catalyzes the chemical reaction
2-methyleneglutarate 2-methylene-3-methylsuccinate
Hence, this enzyme has one substrate, 2-methyleneglutarate, and one product, 2-methylene-3-methylsuccinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methyleneglutarate carboxy-methylenemethylmutase. This enzyme is also called alpha-methyleneglutarate mutase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.
References
EC 5.4.99
Cobamide enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-carboxy-cis%2Ccis-muconate%20cycloisomerase | In enzymology, a 3-carboxy-cis,cis-muconate cycloisomerase () is an enzyme that catalyzes the chemical reaction
2-carboxy-2,5-dihydro-5-oxofuran-2-acetate cis,cis-butadiene-1,2,4-tricarboxylate
Hence, this enzyme has one substrate, 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate, and one product, cis,cis-butadiene-1,2,4-tricarboxylate.
This enzyme belongs to the family of isomerases, specifically intramolecular lyases. The systematic name of this enzyme class is 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). Other names in common use include beta-carboxymuconate lactonizing enzyme, and 3-carboxymuconolactone hydrolase. This enzyme participates in benzoate degradation via hydroxylation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-%28hydroxyamino%29phenol%20mutase | In enzymology, a 3-(hydroxyamino)phenol mutase () is an enzyme that catalyzes the chemical reaction
3-hydroxyaminophenol aminohydroquinone
Hence, this enzyme has one substrate, 3-hydroxyaminophenol, and one product, aminohydroquinone.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is 3-(hydroxyamino)phenol hydroxymutase. Other names in common use include 3-hydroxylaminophenol mutase, and 3HAP mutase.
References
EC 5.4.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxybutyryl-CoA%20epimerase | In enzymology, a 3-hydroxybutyryl-CoA epimerase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxybutanoyl-CoA (R)-3-hydroxybutanoyl-CoA
Hence, this enzyme has one substrate, (S)-3-hydroxybutanoyl-CoA, and one product, (R)-3-hydroxybutanoyl-CoA.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is 3-hydroxybutanoyl-CoA 3-epimerase. Other names in common use include 3-hydroxybutyryl coenzyme A epimerase, and 3-hydroxyacyl-CoA epimerase. This enzyme participates in fatty acid metabolism and butanoate metabolism.
Structural studies
As of late 2007, four structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 5.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-carboxymethyl-4-methylbutenolide%20mutase | In enzymology, a 4-carboxymethyl-4-methylbutenolide mutase () is an enzyme that catalyzes the chemical reaction
4-carboxymethyl-4-methylbut-2-en-1,4-olide 4-carboxymethyl-3-methylbut-2-en-1,4-olide
Hence, this enzyme has one substrate, 4-carboxymethyl-4-methylbut-2-en-1,4-olide, and one product, 4-carboxymethyl-3-methylbut-2-en-1,4-olide.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 4-carboxymethyl-4-methylbut-2-en-1,4-olide methylmutase. Other names in common use include 4-methyl-2-enelactone isomerase, 4-methylmuconolactone methylisomerase, and 4-methyl-3-enelactone methyl isomerase.
References
EC 5.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-deoxy-L-threo-5-hexosulose-uronate%20ketol-isomerase | In enzymology, a 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase () is an enzyme that catalyzes the chemical reaction
4-deoxy-L-threo-5-hexosulose uronate 3-deoxy-D-glycero-2,5-hexodiulosonate
Hence, this enzyme has one substrate, 4-deoxy-L-threo-5-hexosulose uronate, and one product, 3-deoxy-D-glycero-2,5-hexodiulosonate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is 4-deoxy-L-threo-5-hexosulose-uronate aldose-ketose-isomerase. This enzyme is also called 4-deoxy-L-threo-5-hexulose uronate isomerase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-hydroxyproline%20epimerase | In enzymology, a 4-hydroxyproline epimerase () is an enzyme that catalyzes the chemical reaction
trans-4-hydroxy-L-proline cis-4-hydroxy-D-proline
Hence, this enzyme has one substrate, trans-4-hydroxy-L-proline, and one product, cis-4-hydroxy-D-proline.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is 4-hydroxyproline 2-epimerase. Other names in common use include hydroxyproline epimerase, hydroxyproline 2-epimerase, and L-hydroxyproline epimerase. This enzyme participates in arginine and proline metabolism.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-%28carboxyamino%29imidazole%20ribonucleotide%20mutase | In enzymology, a 5-(carboxyamino)imidazole ribonucleotide mutase () is an enzyme that catalyzes the chemical reaction
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Hence, this enzyme has one substrate, 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole, and one product, 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase. Other names in common use include N5-CAIR mutase, PurE, N5-carboxyaminoimidazole ribonucleotide mutase, and class I PurE.
References
EC 5.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-carboxymethyl-2-hydroxymuconate%20Delta-isomerase | In enzymology, a 5-carboxymethyl-2-hydroxymuconate Delta-isomerase () is an enzyme that catalyzes the chemical reaction
5-carboxymethyl-2-hydroxymuconate 5-carboxy-2-oxohept-3-enedioate
Hence, this enzyme has one substrate, 5-carboxymethyl-2-hydroxymuconate, and one product, 5-carboxy-2-oxohept-3-enedioate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is 5-carboxymethyl-2-hydroxymuconate Delta2,Delta4-2-oxo,Delta3-isomerase. This enzyme participates in tyrosine metabolism and benzoate degradation via hydroxylation.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 5.3.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acetoin%20racemase | In enzymology, an acetoin racemase () is an enzyme that catalyzes the chemical reaction
(S)-acetoin (R)-acetoin
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is acetoin racemase. This enzyme is also called acetylmethylcarbinol racemase. This enzyme participates in butanoate metabolism.
References
EC 5.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aconitate%20Delta-isomerase | In enzymology, an aconitate Δ-isomerase () is an enzyme that catalyzes the chemical reaction
trans-aconitate cis-aconitate
Hence, this enzyme has one substrate, trans-aconitate, and one product, cis-aconitate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is aconitate Delta2-Delta3-isomerase. This enzyme is also called aconitate isomerase.
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ADP-glyceromanno-heptose%206-epimerase | In enzymology, an ADP-L-glycero-D-manno-heptose 6-epimerase () is an enzyme that catalyzes the chemical reaction
ADP-D-glycero-D-manno-heptose ADP-L-glycero-D-manno-heptose
Hence, this enzyme has one substrate, ADP-D-glycero-D-manno-heptose, and one product, ADP-L-glycero-D-manno-heptose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is ADP-L-glycero-D-manno-heptose 6-epimerase. This enzyme participates in lipopolysaccharide biosynthesis. It employs one cofactor, NADP+ in a direct oxidation mechanism.
Structural studies
As of 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.1.3
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alanine%20racemase | In enzymology, an alanine racemase () is an enzyme that catalyzes the chemical reaction
L-alanine D-alanine
Hence, this enzyme has one substrate, L-alanine, and one product, D-alanine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is alanine racemase. This enzyme is also called L-alanine racemase. This enzyme participates in alanine and aspartate metabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit this enzyme.
The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of all bacteria, including many which are harmful to humans. The enzyme is absent in higher eukaryotes but found everywhere in prokaryotes, making alanine racemase a great target for antimicrobial drug development. Alanine racemase can be found in some invertebrates.
Bacteria can have one (alr gene) or two alanine racemase genes. Bacterial species with two genes for alanine racemase have one that is continually expressed and one that is inducible, which makes it difficult to target both genes for drug studies. However, knockout studies have shown that without the alr gene being expressed, the bacteria would need an external source of D-alanine in order to survive. Therefore, the alr gene is a feasible targe |
https://en.wikipedia.org/wiki/Aldose%201-epimerase | In enzymology, an aldose 1-epimerase () is an enzyme that catalyzes the chemical reaction
alpha-D-glucose beta-D-glucose
Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is aldose 1-epimerase. Other names in common use include mutarotase, and aldose mutarotase. This enzyme participates in glycolysis and gluconeogenesis.
Structural studies
As of late 2007, 23 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 5.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Allantoin%20racemase | In enzymology, an allantoin racemase ({) is an enzyme that catalyzes the chemical reaction
(S)(+)-allantoin (R)(-)-allantoin
Hence, this enzyme has one substrate, (S)(+)-allantoin, and one product, (R)(-)-allantoin.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on other compounds. The systematic name of this enzyme class is allantoin racemase. This enzyme participates in purine metabolism.
References
EC 5.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allene%20oxide%20cyclase | In enzymology, an allene-oxide cyclase () is an enzyme that belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate isomerase (cyclizing).
The allene oxide of linolenic acid (i.e., (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate) is converted by allene oxide cyclase to jasmonic acid ((15Z)-12-oxophyto-10,15-dienoate).
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 5.3.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alpha-methylacyl-CoA%20racemase | α-Methylacyl-CoA racemase (AMACR, ) is an enzyme that in humans is encoded by the AMACR gene. AMACR catalyzes the following chemical reaction:
(2R)-2-methylacyl-CoA (2S)-2-methylacyl-CoA
In mammalian cells, the enzyme is responsible for converting (2R)-methylacyl-CoA esters to their (2S)-methylacyl-CoA epimers and known substrates, including coenzyme A esters of pristanic acid (mostly derived from phytanic acid, a 3-methyl branched-chain fatty acid that is abundant in the diet) and bile acids derived from cholesterol. This transformation is required in order to degrade (2R)-methylacyl-CoA esters by β-oxidation, which process requires the (2S)-epimer. The enzyme is known to be localised in peroxisomes and mitochondria, both of which are known to β-oxidize 2-methylacyl-CoA esters.
Nomenclature
This enzyme belongs to the family of isomerases, specifically the racemases and epimerases which act on other compounds. The systematic name of this enzyme class is 2-methylacyl-CoA 2-epimerase. In vitro experiments with the human enzyme AMACR 1A show that both (2S)- and (2R)-methyldecanoyl-CoA esters are substrates and are converted by the enzyme with very similar efficiency. Prolonged incubation of either substrate with the enzyme establishes an equilibrium with both substrates or products present in a near 1:1 ratio. The mechanism of the enzyme requires removal of the α-proton of the 2-methylacyl-CoA to form a deprotonated intermediate (which is probably the enol or enolate) fol |
https://en.wikipedia.org/wiki/Alpha-pinene-oxide%20decyclase | In enzymology, an α-pinene-oxide decyclase () is an enzyme that catalyzes the chemical reaction
α-pinene oxide (Z)-2-methyl-5-isopropylhexa-2,5-dienal
Hence, this enzyme has one substrate, α-pinene oxide, and one product, (Z)-2-methyl-5-isopropylhexa-2,5-dienal.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is α-pinene-oxide lyase (decyclizing). This enzyme is also called α-pinene oxide lyase. This enzyme participates in limonene and pinene degradation.
References
EC 5.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Amino-acid%20racemase | In enzymology, an amino-acid racemase () is an enzyme that catalyzes the chemical reaction
an L-amino acid a D-amino acid
Hence, this enzyme has one substrate, L-amino acid, and one product, D-amino acid.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is amino-acid racemase. This enzyme is also called L-amino acid racemase. This enzyme participates in 4 metabolic pathways: glycine, serine and threonine metabolism, cysteine metabolism, D-glutamine and D-glutamate metabolism, and D-arginine and D-ornithine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 5.1.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arabinose-5-phosphate%20isomerase | In enzymology, an arabinose-5-phosphate isomerase () is an enzyme that catalyzes the chemical reaction
D-arabinose 5-phosphate D-ribulose 5-phosphate
Hence, this enzyme has one substrate, D-arabinose 5-phosphate, and one product, D-ribulose 5-phosphate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-arabinose-5-phosphate aldose-ketose-isomerase. Other names in common use include arabinose phosphate isomerase, phosphoarabinoisomerase, and D-arabinose-5-phosphate ketol-isomerase.
References
EC 5.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arabinose%20isomerase | In enzymology, an arabinose isomerase () is an enzyme that catalyzes the chemical reaction
D-arabinose D-ribulose
Hence, this enzyme has one substrate, D-arabinose, and one product, D-ribulose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-arabinose aldose-ketose-isomerase. Other names in common use include D-arabinose(L-fucose) isomerase, D-arabinose isomerase, L-fucose isomerase, and D-arabinose ketol-isomerase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arginine%20racemase | In enzymology, an arginine racemase () is an enzyme that catalyzes the chemical reaction
L-arginine D-arginine
Hence, this enzyme has one substrate, L-arginine, and one product, D-arginine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is arginine racemase. This enzyme participates in 3 metabolic pathways: lysine degradation, D-glutamine and D-glutamate metabolism, and D-arginine and D-ornithine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 5.1.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ascopyrone%20tautomerase | In enzymology, an ascopyrone tautomerase () is an enzyme that catalyzes the chemical reaction
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose
Hence, this enzyme has one substrate, 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose, and one product, 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
The enzyme is involved with the anhydrofructose pathway.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto- and enol-groups. The systematic name of this enzyme class is 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose Delta3-Delta1-isomerase. Other names in common use include ascopyrone isomerase, ascopyrone intramolecular oxidoreductase, 1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase, APM tautomerase, ascopyrone P tautomerase, and APTM.
See also
Anhydrofructose pathway
1,5-anhydro-D-fructose dehydratase
exo-(1→4)-α-D-glucan lyase
References
EC 5.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%20racemase | In enzymology, an aspartate racemase () is an enzyme that catalyzes the following chemical reaction:
L-aspartate D-aspartate
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and amino acid derivatives, including glutamate racemase, proline racemase, and diaminopimelate epimerase.
The systematic name of this enzyme class is aspartate racemase. Other names in common use include D-aspartate racemase, and McyF.
Discovery
Aspartate racemase was first discovered in the gram-positive bacteria Streptococcus faecalis by Lamont et al. in 1972. It was then determined that aspartate racemase also racemizes L-alanine around half as quickly as it does L-aspartate, but does not show racemase activity in the presence of L-glutamate.
Structure
The crystallographic structure of bacterial aspartate racemase has been solved in Pyrococcus horikoshii OT3, Escherichia coli, Microcystis aeruginosa, and Picrophilus torridus DSM 9790.
Homodimer
In most bacteria for which the structure is known, aspartate racemase exists as a homodimer, where each subunit has a molecular weight of approximately 25 kDa. The complex consists primarily of alpha helices, and additionally features a Rossmann fold in the center of the dimer. The catalytic pocket lies at the cleft formed by the intersection of the two domains. A citrate molecule can fit inside the binding pocket, leading to a contraction of the cleft to make the "closed form" of asp |
https://en.wikipedia.org/wiki/Beta-lysine%205%2C6-aminomutase | In enzymology, a beta-lysine 5,6-aminomutase () is an enzyme that catalyzes the chemical reaction
(3S)-3,6-diaminohexanoate (3S,5S)-3,5-diaminohexanoate
Hence, this enzyme has one substrate, (3S)-3,6-diaminohexanoate, and one product, (3S,5S)-3,5-diaminohexanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (3S)-3,6-diaminohexanoate 5,6-aminomutase. Other names in common use include beta-lysine mutase, and L-beta-lysine 5,6-aminomutase. This enzyme participates in lysine degradation. It employs one cofactor, cobamide.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.4.3
Cobamide enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Beta-phosphoglucomutase | In enzymology, a β-phosphoglucomutase () is an enzyme that catalyzes the chemical reaction
β-D-glucose 1-phosphate β-D-glucose 6-phosphate
Hence, this enzyme has one substrate, β-D-glucose 1-phosphate, and one product, β-D-glucose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is beta-D-glucose 1,6-phosphomutase. This enzyme participates in starch and sucrose metabolism.
Structural studies
20 structures have been solved for this enzyme PDB. Some of the accession codes are , , , , , and . Most of these structures detail metal fluoride analogue complexes which are used to mimic different states along the reaction coordinate.
References
EC 5.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Bornyl%20diphosphate%20synthase | In enzymology, bornyl diphosphate synthase (BPPS) () is an enzyme that catalyzes the chemical reaction
geranyl diphosphate (+)-bornyl diphosphate
Bornyl diphosphate synthase is involved in the biosynthesis of the cyclic monoterpenoid bornyl diphosphate. As seen from the reaction above, BPPS takes geranyl diphosphate as its only substrate and isomerizes into the product, (+)- bornyl diphosphate. This reaction comes from a general class of enzymes called terpene synthases that cyclize a universal precursor, geranyl diphosphate, to form varying monocyclic and bicyclic monoterpenes. The biochemical transformation of geranyl diphosphate to cyclic products occurs in a variety of aromatic plants, including both angiosperms and gymnosperms, and is used for various purposes described in sections below. Terpene synthases like BPPS are the primary enzymes in the formation of low-molecular-weight terpene metabolites. The organization of terpene synthases, their characteristic ability to form multiple products, and regulation in response to biotic and abiotic factors contribute to the formation of a diverse group of terpene metabolites. The structural diversity and complexity of terpenes generates an enormous potential for mediating plant–environment interactions.
The systematic name of this enzyme class is (+)-bornyl-diphosphate lyase (decyclizing). Other names in common use include bornyl pyrophosphate synthase, bornyl pyrophosphate synthetase, (+)-bornylpyrophosphate cyclase, and g |
https://en.wikipedia.org/wiki/Carboxy-cis%2Ccis-muconate%20cyclase | In enzymology, a carboxy-cis,cis-muconate cyclase () is an enzyme that catalyzes the chemical reaction
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate 3-carboxy-cis,cis-muconate
Hence, this enzyme has one substrate, 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate, and one product, 3-carboxy-cis,cis-muconate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme is also called 3-carboxymuconate cyclase. This enzyme participates in benzoate degradation via hydroxylation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/CDP-paratose%202-epimerase | In enzymology, a CDP-paratose 2-epimerase () is an enzyme that catalyzes the chemical reaction
CDP-3,6-dideoxy-D-glucose CDP-3,6-dideoxy-D-mannose
Hence, this enzyme has one substrate, CDP-3,6-dideoxy-D-glucose, and one product, CDP-3,6-dideoxy-D-mannose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is CDP-3,6-dideoxy-D-glucose 2-epimerase. Other names in common use include CDP-paratose epimerase, cytidine diphosphoabequose epimerase, cytidine diphosphodideoxyglucose epimerase, cytidine diphosphoparatose epimerase, and cytidine diphosphate paratose-2-epimerase. It is also incorrectly known as CDP-abequose epimerase, and CDP-D-abequose 2-epimerase. This enzyme participates in starch and sucrose metabolism. It employs one cofactor, NAD+.
References
EC 5.1.3
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cellobiose%20epimerase | In enzymology a cellobiose epimerase () is an enzyme that catalyzes the chemical reaction
cellobiose D-glucosyl-D-mannose
Hence, this enzyme has one substrate, cellobiose, and one product, D-glucosyl-D-mannose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and their derivatives. The systematic name of this enzyme class is cellobiose 2-epimerase. Enzymes like these can produce a more rapid syndrome that can speed up the process of many life-threatening diseases such as Necrotizing Fasciitis.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chalcone%20isomerase | In enzymology, a chalcone isomerase () is an enzyme that catalyzes the chemical reaction
a chalcone a flavanone
Hence, this enzyme has one substrate, a chalcone, and one product, a flavanone.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is flavanone lyase (decyclizing). This enzyme is also called chalcone-flavanone isomerase. This enzyme participates in flavonoid biosynthesis.
The Petunia hybrida (Petunia) genome contains two genes coding for very similar enzymes, ChiA and ChiB, but only the first seems to encode a functional chalcone isomerase.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
Chalcone isomerase has a core 2-layer alpha/beta structure consisting of beta(3)-alpha(2)-beta-alpha(2)-beta(3).
References
Further reading
Protein domains
EC 5.5.1
Enzymes of known structure
Chalconoids metabolism
Flavanones metabolism |
https://en.wikipedia.org/wiki/Chloromuconate%20cycloisomerase | In enzymology, a chloromuconate cycloisomerase () is an enzyme that catalyzes the chemical reaction
2-chloro-2,5-dihydro-5-oxofuran-2-acetate 3-chloro-cis,cis-muconate
Hence, this enzyme has one substrate, 2-chloro-2,5-dihydro-5-oxofuran-2-acetate, and one product, 3-chloro-cis,cis-muconate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme is also called muconate cycloisomerase II. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation. It employs one cofactor, manganese.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 5.5.1
Manganese enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cholestenol%20Delta-isomerase | In enzymology, a cholestenol Δ-isomerase () is an enzyme that catalyzes the chemical reaction
5alpha-cholest-7-en-3beta-ol 5alpha-cholest-8-en-3beta-ol
Hence, this enzyme has one substrate, 5alpha-cholest-7-en-3beta-ol, and one product, 5alpha-cholest-8-en-3beta-ol.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is Delta7-cholestenol Delta7-Delta8-isomerase. This enzyme participates in biosynthesis of steroids.
See also
Emopamil binding protein
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondroitin-glucuronate%205-epimerase | In enzymology, a chondroitin-glucuronate 5-epimerase () is an enzyme that catalyzes the chemical reaction
chondroitin D-glucuronate dermatan L-iduronate
Hence, this enzyme has one substrate, chondroitin D-glucuronate, and one product, dermatan L-iduronate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is chondroitin-D-glucuronate 5-epimerase. Other names in common use include polyglucuronate 5-epimerase, dermatan-sulfate 5-epimerase, urunosyl C-5 epimerase, and chondroitin D-glucuronosyl 5-epimerase. This enzyme participates in chondroitin sulfate biosynthesis.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chorismate%20mutase | In enzymology, chorismate mutase () is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to prephenate in the pathway to the production of phenylalanine and tyrosine, also known as the shikimate pathway.
Hence, this enzyme has one substrate, chorismate, and one product, prephenate. Chorismate mutase is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis of tyrosine and phenylalanine and away from tryptophan. Its role in maintaining the balance of these aromatic amino acids in the cell is vital. This is the single known example of a naturally occurring enzyme catalyzing a pericyclic reaction. Chorismate mutase is only found in fungi, bacteria, and higher plants. Some varieties of this protein may use the morpheein model of allosteric regulation.
Protein family
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases that transfer functional groups. The systematic name of this enzyme class is chorismate pyruvatemutase. Chorismate mutase, also known as hydroxyphenylpyruvate synthase, participates in phenylalanine, tyrosine and tryptophan biosynthesis. The structures of chorismate mutases vary in different organisms, but the majority belong to the AroQ family and are characterized by an intertwined homodimer of 3-helical subunits. Most chorismate mutases in this family look similar to that of Escherichia coli. For example, the secondary structure of the |
https://en.wikipedia.org/wiki/Copalyl%20diphosphate%20synthase | In enzymology, a copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction
geranylgeranyl diphosphate (+)-copalyl diphosphate
Hence, this enzyme has one substrate, geranylgeranyl diphosphate, and one product, (+)-copalyl diphosphate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is (+)-copalyl-diphosphate lyase (decyclizing). This enzyme participates in diterpenoid biosynthesis.
References
EC 5.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Corticosteroid%20side-chain-isomerase | In enzymology, a corticosteroid side-chain-isomerase () is an enzyme that catalyzes the chemical reaction
11-deoxycorticosterone 20-hydroxy-3-oxopregn-4-en-21-al
Hence, this enzyme has one substrate, 11-deoxycorticosterone, and one product, 20-hydroxy-3-oxopregn-4-en-21-al.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is 11-deoxycorticosterone aldose-ketose-isomerase.
References
EC 5.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cycloartenol%20synthase | In enzymology, a cycloartenol synthase () is an enzyme that catalyzes the chemical reaction
(S)-2,3-epoxysqualene cycloartenol
Hence, this enzyme has one substrate, (S)-2,3-epoxysqualene, and one product, cycloartenol.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming). Other names in common use include 2,3-epoxysqualene cycloartenol-cyclase, squalene-2,3-epoxide-cycloartenol cyclase, 2,3-epoxysqualene cycloartenol-cyclase, 2,3-epoxysqualene-cycloartenol cyclase, and 2,3-oxidosqualene-cycloartenol cyclase. This enzyme participates in biosynthesis of steroids.
References
EC 5.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cycloeucalenol%20cycloisomerase | In enzymology, a cycloeucalenol cycloisomerase () is an enzyme that catalyzes the chemical reaction
cycloeucalenol obtusifoliol
Hence, this enzyme has one substrate, cycloeucalenol, and one product, obtusifoliol.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is cycloeucalenol lyase (cyclopropane-decyclizing). This enzyme is also called cycloeucalenol---obtusifoliol isomerase. This enzyme participates in biosynthesis of steroids.
References
EC 5.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diaminopimelate%20epimerase | In enzymology, a diaminopimelate epimerase () is an enzyme that catalyzes the chemical reaction
LL-2,6-diaminoheptanedioate meso-diaminoheptanedioate
Hence, this enzyme has one substrate, LL-2,6-diaminoheptanedioate, and one product, meso-diaminoheptanedioate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate 2-epimerase. This enzyme participates in lysine biosynthesis.
Background
Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids - lysine, threonine, methionine and isoleucine - in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential component of bacterial cell wall biosynthesis, and dipicolinic acid, which is involved in sporulation (spore production) in Gram-positive bacteria. Members of the animal kingdom do not possess this pathway and must therefore acquire these essential amino acids through their diet. Research into improving the metabolic flux through this pathway has the potential to increase the yield of the essential amino acids in important crops, thus improving their nutritional value. Additionally, since the enzymes are not present in animals, inhibitors of them are promising targets for the development of novel antibiotics and herbicides.
The ly |
https://en.wikipedia.org/wiki/Dichloromuconate%20cycloisomerase | In enzymology, a dichloromuconate cycloisomerase () is an enzyme that catalyzes the chemical reaction
2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate 2,4-dichloro-cis,cis-muconate
Hence, this enzyme has one substrate, 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate, and one product, 2,4-dichloro-cis,cis-muconate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme participates in 1,4-dichlorobenzene degradation. It employs one cofactor, manganese.
References
EC 5.5.1
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-lysine%205%2C6-aminomutase | In enzymology, D-lysine 5,6-aminomutase () is an enzyme that catalyzes the chemical reaction
D-lysine 2,5-diaminohexanoate
Hence, this enzyme has one substrate, D-lysine, and one product, 2,5-diaminohexanoate.
This enzyme participates in lysine degradation. It employs one cofactor, cobamide.
Background
D-lysine 5,6-aminomutase belongs to the isomerase family of enzymes, specifically intramolecular transferases, which transfers amino groups. Its systematic name is D-2,6-diaminohexanoate 5,6-aminomutase. Other names in common use include D-α-lysine mutase and adenosylcobalamin-dependent D-lysine 5,6-aminomutase, which can be abbreviated as 5,6-LAM.
5,6-LAM is capable of reversibly catalyzing the migration of an amino group from ε-carbon to δ-carbon in both D-lysine and L-β-lysine, and catalyzing the migration of hydrogen atoms from δ-carbon to ε-carbon at the same time. It demonstrates greatest catalytic activity in 20mM Tris•HCl at pH 9.0-9.2.
In the early 1950s, 5,6-LAM was discovered in the amino-acid-fermenting bacteria Clostridium sticklandii, in which lysine undergoes degradation under anaerobic conditions to equimolar amounts of acetate and butyrate.
Later, isotopic studies uncovered two possible pathways. In pathway A, both acetate and butyrate are generated from C2-C3 cleavage of D-lysine. Unlike pathway A, pathway B involves C5-C4 degradation, producing the same products.
D-lysine 5,6-aminomutase (5,6-LAM) is responsible for the first conversion in pathway |
https://en.wikipedia.org/wiki/D-lyxose%20ketol-isomerase | In enzymology, a D-lyxose ketol-isomerase () is an enzyme that catalyzes the chemical reaction
D-lyxose D-xylulose
Hence, this enzyme has one substrate, D-lyxose, and one product, D-xylulose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-lyxose aldose-ketose-isomerase. Other names in common use include D-lyxose isomerase, and D-lyxose ketol-isomerase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-ornithine%204%2C5-aminomutase | In enzymology, a D-ornithine 4,5-aminomutase () is an enzyme that catalyzes the chemical reaction
D-ornithine (2R,4S)-2,4-diaminopentanoate
Hence, this enzyme has one substrate, D-ornithine, and one product, (2R,4S)-2,4-diaminopentanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is D-ornithine 4,5-aminomutase. Other names in common use include D-alpha-ornithine 5,4-aminomutase, and D-ornithine aminomutase. This enzyme participates in d-arginine and d-ornithine metabolism. It has 3 cofactors: pyridoxal phosphate, Cobamide coenzyme, and Dithiothreitol.
References
EC 5.4.3
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-dehydrorhamnose%203%2C5-epimerase | In enzymology, a dTDP-4-dehydrorhamnose 3,5-epimerase () is an enzyme that catalyzes the chemical reaction
dTDP-4-dehydro-6-deoxy-D-glucose dTDP-4-dehydro-6-deoxy-L-mannose
Hence, this enzyme has one substrate, dTDP-4-dehydro-6-deoxy-D-glucose, and one product, dTDP-4-dehydro-6-deoxy-L-mannose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase. Other names in common use include dTDP-L-rhamnose synthetase, dTDP-L-rhamnose synthetase, thymidine diphospho-4-ketorhamnose 3,5-epimerase, TDP-4-ketorhamnose 3,5-epimerase, dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase, and TDP-4-keto-L-rhamnose-3,5-epimerase. This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.
Structural studies
The crystal structure of RmlC from Methanobacterium thermoautotrophicum was determined in the presence and absence of a substrate analogue. RmlC is a homodimer comprising a central jelly roll motif, which extends in two directions into longer beta-sheets. Binding of dTDP is stabilised by ionic interactions to the phosphate group and by a combination of ionic and hydrophobic interactions with the base. The active site, which is located in the centre of the jelly roll, is formed by residues that are conserved in all known RmlC sequence h |
https://en.wikipedia.org/wiki/Ent-Copalyl%20diphosphate%20synthase | In enzymology, an ent-copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction:
Hence, this enzyme has one substrate, geranylgeranyl pyrophosphate, and one product, ent-copalyl pyrophosphate. This enzyme participates in gibberellin biosynthesis.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is ent-copalyl-diphosphate lyase (decyclizing). Other names in common use include ent-kaurene synthase A, and ent-kaurene synthetase A.
Bifunctionality
ent-Copalyl diphosphate synthases from fungi and mosses also have a distinct ent-kaurene synthase activity associated with the same protein molecule. The reaction catalyzed by ent-kaurene synthase is the next step in the biosynthetic pathway to gibberellins. The two types of enzymic activity are distinct, and site-directed mutagenesis to suppress the ent-kaurene synthase activity of the protein leads to build up of ent-copalyl pyrophosphate. Inhibition of ent-kaurene synthase activity, by replacing Mg2+ in the growth medium with Ni2+, has the same effect.
Higher plants typically have separate proteins for ent-copalyl diphosphate synthase and ent-kaurene synthase, although these may be associated as weakly bound dimers or enzyme complexes. Rice (Oryza sativa) has two distinct ent-copalyl diphosphate synthases, which participate in distinct metabolic pathways. Only one ent-copalyl diphosphate synthase has been isolated fr |
https://en.wikipedia.org/wiki/Farnesol%202-isomerase | In enzymology, a farnesol 2-isomerase () is an enzyme that catalyzes the chemical reaction
2-trans,6-trans-farnesol 2-cis,6-trans-farnesol
Hence, this enzyme has one substrate, 2-trans,6-trans-farnesol, and one product, 2-cis,6-trans-farnesol.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 2-trans,6-trans-farnesol 2-cis-trans-isomerase. This enzyme is also called farnesol isomerase.
References
EC 5.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Furylfuramide%20isomerase | In enzymology, a furylfuramide isomerase () is an enzyme that catalyzes the chemical reaction
(E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide
Hence, this enzyme has one substrate, (E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide, and one product, (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide cis-trans-isomerase. It has 2 cofactors: NAD+, and NADH.
References
EC 5.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactose-6-phosphate%20isomerase | In enzymology, a galactose-6-phosphate isomerase () is an enzyme that catalyzes the chemical reaction
D-galactose 6-phosphate D-tagatose 6-phosphate
Hence, this enzyme has one substrate, D-galactose 6-phosphate, and one product, D-tagatose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-galactose-6-phosphate aldose-ketose-isomerase. This enzyme participates in galactose metabolism.
References
EC 5.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-mannose%203%2C5-epimerase | In enzymology, a GDP-mannose 3,5-epimerase () is an enzyme that catalyzes the chemical reaction
GDP-mannose GDP-L-galactose + GDP-L-gulose - initial reaction overview (updated in 2020, see below)
Hence, this enzyme has one substrate, GDP-mannose, and two products, GDP-L-galactose and GDP-L-gulose
Since only GDP-L-gulose (the C5-epimer of GDP-D-mannose) was found in the reaction mixture, it was postulated that the enzyme performs the C5-epimerization prior to the C3-epimerization. However, GDP-D-altrose was recently found as a reaction product, which means that both reaction routes can occur: C5-prior-to-C3 and C3-prior-to-C5.
This also means that the GDP-mannose 3,5-epimerase has three reaction products, namely the main product GDP-L-galactose (C3,5-epimer) and two sideproducts GDP-L-gulose (C5-epimer) + GDP-D-altrose (C3-epimer).
GDP-D-mannose GDP-L-galactose (C3,5-epimer) + GDP-L-gulose (C5-epimer) + GDP-D-altrose (C3-epimer) - reaction overview update in 2020
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is GDP-mannose 3,5-epimerase. Other names in common use include GDP-D-mannose:GDP-L-galactose epimerase, guanosine 5'-diphosphate D-mannose:guanosine 5'-diphosphate, and L-galactose epimerase. This enzyme participates in ascorbate and aldarate metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this clas |
https://en.wikipedia.org/wiki/Glucose-6-phosphate%201-epimerase | In enzymology, a glucose-6-phosphate 1-epimerase () is an enzyme that catalyzes the chemical reaction
alpha-D-glucose 6-phosphate beta-D-glucose 6-phosphate
Hence, this enzyme has one substrate, alpha-D-glucose 6-phosphate, and one product, beta-D-glucose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is D-glucose-6-phosphate 1-epimerase. This enzyme participates in glycolysis / gluconeogenesis.
Structural studies
As of late 2013, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 5.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucuronate%20isomerase | In enzymology, a glucuronate isomerase () is an enzyme that catalyzes the chemical reaction
D-glucuronate D-fructuronate
Hence, this enzyme has one substrate, D-glucuronate, and one product, D-fructuronate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-glucuronate aldose-ketose-isomerase. Other names in common use include uronic isomerase, uronate isomerase, D-glucuronate isomerase, uronic acid isomerase, and D-glucuronate ketol-isomerase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamate-1-semialdehyde%202%2C1-aminomutase | In enzymology, a glutamate-1-semialdehyde 2,1-aminomutase () is an enzyme that catalyzes the chemical reaction
L-glutamate 1-semialdehyde 5-aminolevulinate
Hence, this enzyme has one substrate, L-glutamate-1-semialdehyde, and one product, 5-aminolevulinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (S)-4-amino-5-oxopentanoate 4,5-aminomutase. This enzyme is also called glutamate-1-semialdehyde aminotransferase. This enzyme participates in porphyrin and chlorophyll biosynthesis. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
EC 5.4.3
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamate%20racemase | In enzymology, glutamate racemase (MurI with a capital i) () is an enzyme that catalyzes the chemical reaction
L-glutamate D-glutamate
Hence, this enzyme RacE has one substrate, L-glutamate, and one product, D-glutamate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives, including proline racemase, aspartate racemase, and diaminopimelate epimerase. This enzyme participates in glutamate metabolism that is essential for cell wall biosynthesis in bacteria. Glutamate racemase performs the additional function of gyrase inhibition, preventing gyrase from binding to DNA.
Glutamate racemase (MurI) serves two distinct metabolic functions: primarily, it is a critical enzyme in cell wall biosynthesis, but also plays a role in gyrase inhibition. The ability of glutamate racemase and other proteins to serve two distinct functions is known as "moonlighting".
Moonlighting background
Before the discovery of moonlighting proteins, it was generally believed by scientists that an enzyme only had one function which led to the concept of "one gene, one enzyme". However, this concept no longer applies in science after the discovery that some proteins consist of both major and minor functions. This led to numerous studies attempting to relate the two functions to each other. The minor functions of these unique enzymes are called moonlighting functions, in which a protein can have a secondary functions not depend |
https://en.wikipedia.org/wiki/%28hydroxyamino%29benzene%20mutase | In enzymology, a (hydroxyamino)benzene mutase () is an enzyme that catalyzes the chemical reaction
(hydroxyamino)benzene 2-aminophenol
Hence, this enzyme has one substrate, (hydroxyamino)benzene, and one product, 2-aminophenol.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is (hydroxyamino)benzene hydroxymutase. Other names in common use include HAB mutase, hydroxylaminobenzene hydroxymutase, and hydroxylaminobenzene mutase. This enzyme participates in naphthalene and anthracene degradation.
References
EC 5.4.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxypyruvate%20isomerase | In enzymology, a hydroxypyruvate isomerase () is an enzyme that catalyzes the chemical reaction
hydroxypyruvate 2-hydroxy-3-oxopropanoate
Hence, this enzyme has one substrate, hydroxypyruvate, and one product, 2-hydroxy-3-oxopropanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is hydroxypyruvate aldose-ketose-isomerase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 5.3.1
Enzymes of unknown structure |
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