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https://en.wikipedia.org/wiki/Dihydroxyphenylalanine%20ammonia-lyase | In enzymology, a dihydroxyphenylalanine ammonia-lyase (, entry deleted) is a non-existing enzyme that catalyzes the chemical reaction
3,4-dihydroxy-L-phenylalanine trans-caffeate + NH3
Hence, this enzyme has one substrate, 3,4-dihydroxy-L-phenylalanine (L-DOPA), and two products, trans-caffeate and NH3.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 3,4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming). Other names in common use include beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ammonia-lyase. This enzyme participates in tyrosine metabolism.
References
EC 4.3.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Dimethylpropiothetin%20dethiomethylase | The enzyme dimethylpropiothetin dethiomethylase (EC 4.4.1.3) catalyzes the chemical reaction
S,S-dimethyl-β-propiothetin dimethyl sulfide + acrylate
The enzyme breaks S,S-dimethyl-β-propiothetin into dimethyl sulfide and acrylate.
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S,S-dimethyl-β-propiothetin dimethyl-sulfide-lyase (acrylate-forming). Other names in common use include desulfhydrase, and ''S,S''-dimethyl-beta-propiothetin dimethyl-sulfide-lyase.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-serine%20ammonia-lyase | The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
D-serine = pyruvate + NH3 (overall reaction)
(1a) D-serine = 2-aminoprop-2-enoate + H2O
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous
Other names in common use include D-hydroxyaminoacid dehydratase, D-serine dehydrase, D-hydroxy amino acid dehydratase, D-serine hydrolase, D-serine dehydratase (deaminating), D-serine deaminase, and D-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Erythro-3-hydroxyaspartate%20ammonia-lyase | The enzyme erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) catalyzes the chemical reaction
erythro-3-hydroxy-L-aspartate oxaloacetate + NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is ''erythro-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use include erythro-β-hydroxyaspartate dehydratase, erythro-3-hydroxyaspartate dehydratase, erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating); erythro''-3-hydroxy-Ls-aspartate ammonia-lyase. It employs one cofactor, pyridoxal phosphate.
References
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ethanolamine%20ammonia-lyase | The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction
ethanolamine acetaldehyde + NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is ethanolamine ammonia-lyase (acetaldehyde-forming). It is also called ethanolamine deaminase. It participates in glycerophospholipid metabolism. It employs one cofactor, adenosylcobalamin.
Structural studies
As of early 2011, several structures have been solved for this class of enzymes. The first structure solved was the active site containing EutB subunit of EAL from Listeria monocytogenes with the PDB accession code . Later, more structures have become available from Escherichia coli that include both EAL subunits bound to various ligands.
References
EC 4.3.1
Cobamide enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/FAD-AMP%20lyase%20%28cyclizing%29 | The enzyme FAD-AMP lyase (cyclizing) (EC 4.6.1.15) catalyzes the reaction
FAD AMP + riboflavin cyclic-4′,5′--phosphate
This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is FAD AMP-lyase (riboflavin-cyclic-4′,5′-phosphate-forming). Other names in common use include FMN cyclase and FAD AMP-lyase (cyclic-FMN-forming).
References
Further reading
EC 4.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formimidoyltetrahydrofolate%20cyclodeaminase | In enzymology, a formimidoyltetrahydrofolate cyclodeaminase () is an enzyme that catalyzes the chemical reaction
5-formimidoyltetrahydrofolate 5,10-methenyltetrahydrofolate + NH3
Hence, this enzyme has one substrate, 5-formimidoyltetrahydrofolate, and two products, 5,10-methenyltetrahydrofolate and NH3.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing 5,10-methenyltetrahydrofolate-forming). Other names in common use include formiminotetrahydrofolate cyclodeaminase, and 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing). This enzyme participates in folate metabolism by catabolising histidine and adding to the C1-tetrahydrofolate pool.
In mammals, this enzyme can be found as part of a bifunctional enzyme in a single polypeptide with glutamate formimidoyltransferase (EC 2.1.2.5), the enzyme activity that catalyses the previous step in the histidine catabolic pathway. This arrangement allows the 5-formimidoyltetrahydrofolate intermediate to move directly from one active site to another without being released into solution, in a process called substrate channeling.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 4.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucosaminate%20ammonia-lyase | The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction
2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH3 (overall reaction)
(1a) 2-amino-2-deoxy-Dgluconate = (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate + H2O
(1b) (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate = (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate (spontaneous)
(1c) (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate + H2O = 2-dehydro-3-deoxyD-gluconate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include glucosaminic dehydrase, D-glucosaminate dehydratase, D-glucosaminic acid dehydrase, aminodeoxygluconate dehydratase, 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating), aminodeoxygluconate ammonia-lyase, 2-amino-2-deoxy-D-gluconate ammonia-lyase, and D-glucosaminate ammonia-lyase. This enzyme participates in the pentose phosphate pathway. It employs one cofactor, pyridoxal phosphate.
References
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Wudaoliang%20railway%20station | Wudaoliang railway station () is a crossing loop on the China Railway line to Lhasa in Tibet.
Climate
Wudaoliang has a tundra climate (Köppen climate classification ET) with long, frigid, very dry winters and short, cool, less dry summers.
Station layout
The station has a crossing loop and a few sidings shuntable in the Lhasa-bound direction.
A subway at the Lhasa end is provided for road traffic, rather than a level crossing.
References
Stations on the Qinghai–Tibet Railway
Railway stations in Qinghai |
https://en.wikipedia.org/wiki/Exatecan | Exatecan is a drug which is a structural analog of camptothecin with antineoplastic activity.
A derivative is used in Trastuzumab deruxtecan.
Synthesis
References
Topoisomerase inhibitors
Amines
Tertiary alcohols
Delta-lactones
Lactams
Fluoroarenes |
https://en.wikipedia.org/wiki/CSNK2B | Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2B gene. It is a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus.
Casein kinase, a ubiquitous, well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Serine or Threonine in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits. However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta'). The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif. The beta subunit is a highly conserved protein of about 25kDa that contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc. The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase.
Interactions
CSNK2B has been shown to interact with CD163, CSNK2A2, Casein kinase 2, |
https://en.wikipedia.org/wiki/HBG1 | Hemoglobin subunit gamma-1 is a protein that in humans is encoded by the HBG1 gene.
Function
The gamma globin genes (HBG1 and HBG2) are normally expressed in the fetal liver, spleen and bone marrow. Two gamma chains together with two alpha chains constitute fetal hemoglobin (HbF) which is normally replaced by adult hemoglobin (HbA) in the year following birth. In the non-pathological condition known as hereditary persistence of fetal hemoglobin (HPFH), gamma globin expression is continued into adulthood. Also, in cases of beta-thalassemia and related conditions, gamma chain production may be maintained, possibly as a mechanism to compensate for the mutated beta-globin. The two types of gamma chains differ at residue 136 where glycine is found in the G-gamma product (HBG2) and alanine is found in the A-gamma product (HBG1). The former is predominant at birth. The order of the genes in the beta-globin cluster is: 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'.
References
Further reading
External links
Hemoglobins |
https://en.wikipedia.org/wiki/Modal%20haplotype | A modal haplotype is an ancestral haplotype derived from the DNA test results of a specific group of people, using genetic genealogy.
The two most commonly discussed modal haplotypes are the Atlantic Modal Haplotype (the most common haplotype in parts of Europe, associated with Haplogroup R1b) and the Cohen Modal Haplotype (the haplotype associated with the Jewish Cohanim tradition). However, a specific modal haplotype may be determined for any genealogical DNA test-based surname project or other test group.
List of modal haplotypes
References
See also
Genealogical DNA test
Genetic genealogy
Genetic genealogy |
https://en.wikipedia.org/wiki/GPR35 | G protein-coupled receptor 35 also known as GPR35 is a G protein-coupled receptor which in humans is encoded by the GPR35 gene. Heightened expression of GPR35 is found in immune and gastrointestinal tissues, including the crypts of Lieberkühn.
Ligands
Endogenous ligands
Although GPR35 is still considered an orphan receptor, there have been attempts to deorphanize it by identifying endogenous molecules that can activate the receptor. All of the currently proposed ligands are either unselective towards GPR35, or they lack high potency, a characteristic feature of natural ligands. The following list includes the most prominent examples:
kynurenic acid
LPA species
cyclic guanosine monophosphate
DHICA
T3
reverse T3
Synthetic agonists
Other synthetic agonists of GPR35 include:
cromoglicic acid
nedocromil
pamoic acid
zaprinast
lodoxamide
bufrolin
Zaprinast is currently the gold standard in the biochemical evaluation of novel synthetic GPR35 agonists, because it remains potent in an animal model. Most other known agonists display high selectivity towards the human GPR35 orthologue. This phenomenon is well established for other GPCRs and complicates the development of pharmaceutical drugs.
Antagonists
Antagonists of GPR35 include:
ML145 (CID-2286812)
ML144 (CID-1542103)
Both ML145 and ML144 unfurl their antagonistic activity through inverse agonism. They are, however, highly species-selective, and practically inactive at the rodent receptor orthologues.
Cli |
https://en.wikipedia.org/wiki/Q-function | In statistics, the Q-function is the tail distribution function of the standard normal distribution. In other words, is the probability that a normal (Gaussian) random variable will obtain a value larger than standard deviations. Equivalently, is the probability that a standard normal random variable takes a value larger than .
If is a Gaussian random variable with mean and variance , then is standard normal and
where .
Other definitions of the Q-function, all of which are simple transformations of the normal cumulative distribution function, are also used occasionally.
Because of its relation to the cumulative distribution function of the normal distribution, the Q-function can also be expressed in terms of the error function, which is an important function in applied mathematics and physics.
Definition and basic properties
Formally, the Q-function is defined as
Thus,
where is the cumulative distribution function of the standard normal Gaussian distribution.
The Q-function can be expressed in terms of the error function, or the complementary error function, as
An alternative form of the Q-function known as Craig's formula, after its discoverer, is expressed as:
This expression is valid only for positive values of x, but it can be used in conjunction with Q(x) = 1 − Q(−x) to obtain Q(x) for negative values. This form is advantageous in that the range of integration is fixed and finite.
Craig's formula was later extended by Behnad (2020) for the Q-function |
https://en.wikipedia.org/wiki/Armin%20Aberle | Armin Aberle (born 13 December 1960) is a German semiconductor scientist and full professor at the National University of Singapore in the field of photovoltaics and solar energy, particularly thin film solar cells.
Aberle was born in Hausach, Germany. In 1988, he attained his undergraduate degree in Physics from the University of Freiburg and in 1992 completed his PhD in Physics at the same university.
He is currently working as Chief Executive Officer, Solar Energy Research Institute of Singapore (SERIS, since April 2012).
Armin has written one book and is the author or co-author of over 240 academic publications and patent applications. Armin has also been involved in attaining over A$26 million in funding for photovoltaic research, including A$12.2 million to create an ARC Centre of Excellence in Photovoltaics and Photonics.
Awards received by Armin Aberle
1992 Postdoctoral Humboldt Fellowship
2002 Member of Editorial Board of the academic journal Progress in Photovoltaics
Marquis Who's Who in the World (19th, 22nd, 23rd Edition)
Marquis Who's Who in Science and Engineering (4th and 9th Edition)
See also
Photovoltaics
Solar Cell
Solar energy
Solar power in Australia
References
People associated with solar power
Australian engineers
University of Freiburg alumni
Academic staff of the University of New South Wales
1960 births
Living people |
https://en.wikipedia.org/wiki/Martin%20Charles%20Golumbic | Martin Charles Golumbic (born 1948) is a mathematician and computer scientist known for his research on perfect graphs, graph sandwich problems, compiler optimization, and spatial-temporal reasoning. He is a professor emeritus of computer science at the University of Haifa, and was the founder of the journal Annals of Mathematics and Artificial Intelligence.
Education and career
Golumbic majored in mathematics at Pennsylvania State University, graduating in 1970 with bachelor's and master's degrees. He completed his Ph.D. at Columbia University in 1975, with the dissertation Comparability Graphs and a New Matroid supervised by Samuel Eilenberg.
He became an assistant professor in the Courant Institute of Mathematical Sciences of New York University from 1975 until 1980, when he moved to Bell Laboratories. From 1983 to 1992 he worked for IBM Research in Israel, and from 1992 to 2000 he was a professor of mathematics and computer science at Bar-Ilan University. He moved to the University of Haifa in 2000, where he founded the Caesarea Edmond Benjamin de Rothschild Institute for Interdisciplinary Applications of Computer Science.
In 1989, Golumbic founded the Bar-Ilan Symposium in Foundations of Artificial Intelligence, a leading artificial intelligence conference in Israel. In 1990 Golumbic became the founding editor-in-chief of the journal Annals of Mathematics and Artificial Intelligence, published by Springer.
Recognition
Golumbic is a fellow of the European Association |
https://en.wikipedia.org/wiki/S100B | S100 calcium-binding protein B (S100B) is a protein of the S-100 protein family.
S100 proteins are localized in the cytoplasm and nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21; however, this gene is located at 21q22.3.
Function
S100B is glial-specific and is expressed primarily by astrocytes, but not all astrocytes express S100B. It has been shown that S100B is only expressed by a subtype of mature astrocytes that ensheath blood vessels and by NG2-expressing cells.
This protein may function in neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. In the developing CNS it acts as a neurotrophic factor and neuronal survival protein. In the adult organism it is usually elevated due to nervous system damage, which makes it a potential clinical marker.
Clinical significance
Chromosomal rearrangements and altered expression of this gene have been implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer disease, Down syndrome, epilepsy, amyotrophic lateral sclerosis, schwannoma, melanoma, and type I diabetes mellitus.
It has been suggested that the regulation of S100B by melittin has potential for t |
https://en.wikipedia.org/wiki/CEBPA | CCAAT/enhancer-binding protein alpha is a protein encoded by the CEBPA gene in humans. CCAAT/enhancer-binding protein alpha is a transcription factor involved in the differentiation of certain blood cells. For details on the CCAAT structural motif in gene enhancers and on CCAAT/Enhancer Binding Proteins see the specific page.
Function
The protein encoded by this intronless gene is a bZIP transcription factor which can bind as a homodimer to certain promoters and gene enhancers. It can also form heterodimers with the related proteins CEBP-beta and CEBP-gamma, as well as distinct transcription factors such as c-Jun. The encoded protein is a key regulator of adipogenesis (the process of forming new fat cells) and the accumulation of lipids in those cells, as well as in the metabolism of glucose and lipids in the liver. The protein has been shown to bind to the promoter and modulate the expression of the gene encoding leptin, a protein that plays an important role in body weight homeostasis. Also, the encoded protein can interact with CDK2 and CDK4, thereby inhibiting these kinases and causing cultured cells to stop dividing. In addition, CEBPA is essential for myeloid lineage commitment and therefore required both for normal mature granulocyte formation and for the development of abnormal acute myeloid leukemia.
Common mutations
There are two major categories which CEBPA mutations can be categorized into. One category of mutations prevent CCAAT/enhancer-binding protein alp |
https://en.wikipedia.org/wiki/CEBP | CEBP may refer to:
CEBPA, a human gene that modulates leptin expression
CCAAT-enhancer-binding proteins or C/EBPs
Communication Enabled Business Process |
https://en.wikipedia.org/wiki/Kozeny%E2%80%93Carman%20equation | The Kozeny–Carman equation (or Carman–Kozeny equation or Kozeny equation) is a relation used in the field of fluid dynamics to calculate the pressure drop of a fluid flowing through a packed bed of solids. It is named after Josef Kozeny and Philip C. Carman. The equation is only valid for creeping flow, i.e. in the slowest limit of laminar flow. The equation was derived by Kozeny (1927) and Carman (1937, 1956) from a starting point of (a) modelling fluid flow in a packed bed as laminar fluid flow in a collection of curving passages/tubes crossing the packed bed and (b) Poiseuille's law describing laminar fluid flow in straight, circular section pipes.
Equation
The equation is given as:
where:
is the pressure drop;
is the total height of the bed;
is the superficial or "empty-tower" velocity;
is the viscosity of the fluid;
is the porosity of the bed;
is the sphericity of the particles in the packed bed;
is the diameter of the volume equivalent spherical particle.
This equation holds for flow through packed beds with particle Reynolds numbers up to approximately 1.0, after which point frequent shifting of flow channels in the bed causes considerable kinetic energy losses.
This equation is a partial case of the Darcy's law stating that "flow is proportional to the pressure drop and inversely proportional to the fluid viscosity".
Combining these equations gives the final Kozeny equation for absolute (single phase) permeability
is the porosity of the bed (or core plug |
https://en.wikipedia.org/wiki/Linomide | Linomide (Roquinimex) is a quinoline derivative immunostimulant which increases NK cell activity and macrophage cytotoxicity. It also inhibits angiogenesis and reduces the secretion of TNF alpha.
Linomide has been investigated as a treatment for some cancers (including as adjuvant therapy after bone marrow transplantation in acute leukemia) and autoimmune diseases, such as multiple sclerosis and recent-onset type I diabetes. Several trials have been terminated due to serious cardiovascular toxicity.
Synthesis
Ethyl 2-(methylamino)benzoate is condensed with ethyl malonate. Amine-ester interchange of that compound with N-methylaniline results in formation of the amide linomide.
References
Immunostimulants
2-Quinolones
Quinolinols
Carboxamides
Anilides
3-Hydroxypropenals |
https://en.wikipedia.org/wiki/PARSEC | PARSEC is a package designed to perform electronic structure calculations of solids and molecules using density functional theory (DFT). The acronym stands for Pseudopotential Algorithm for Real-Space Electronic Calculations. It solves the Kohn–Sham equations in real space, without the use of explicit basis sets.
One of the strengths of this code is that it handles non-periodic boundary conditions in a natural way, without the use of super-cells, but can equally well handle periodic and partially periodic boundary conditions. Another key strength is that it is readily amenable to efficient massive parallelization, making it highly effective for very large systems.
Its development started in early 1990s with James Chelikowsky (now at the University of Texas), Yousef Saad and collaborators at the University of Minnesota. The code is freely available under the GNU GPLv2. Currently, its public version is 1.4.4. Some of the physical/chemical properties calculated by this code are: Kohn–Sham band structure, atomic forces (including molecular dynamics capabilities), static susceptibility, magnetic dipole moment, and many additional molecular and solid state properties.
See also
Density functional theory
Quantum chemistry computer programs
References
External links
Computational chemistry software
Density functional theory software
Physics software |
https://en.wikipedia.org/wiki/Imidazoquinoline | Imidazoquinoline is a tricyclic organic molecule; its derivatives and compounds are often used for antiviral and antiallergic creams.
Derivatives
Dactolisib
Imiquimod
Gardiquimod
Resiquimod
Sumanirole
References |
https://en.wikipedia.org/wiki/Choriogenesis | In developmental biology, choriogenesis is the formation of the chorion, an outer membrane of the placenta that eventually forms chorionic villi that allow the transfer of blood and nutrients from mother to fetus.
Influence on monozygotic twins
Identical twins have identical genomes in the immediate aftermath of twinning. Two-thirds of monozygotic twins share the same placenta, arising by cleavage before the fourth day of development; the other third have separate placentas because cleavage has taken place after the fourth day after choriogenesis has begun.
Placentas vary with respect to the transport of nutrients and hormones, a variance that may influence epigenesis. For example, the pattern of X chromosome inactivation is affected by placental status. There is some evidence that it affects the variance in IQ test findings among identical twins, that is, monochorionic identical twins display less IQ variance one from another than do dichorionic identical twins. There is weak evidence that monozygotic twins sharing a placenta have a higher concordance rate for schizophrenia than monozygotic twins with separate placentas. Sharing a placenta increases the risk for infection, and infection in pregnancy has been shown to be a risk factor for schizophrenia. Equally striking is evidence for increasing difference in genomic expression between identical twins as they are once again implicating environmental intercession.
References
External links
Embryology
Human genetic |
https://en.wikipedia.org/wiki/Outline%20of%20radio | The following outline is provided as an overview of and topical guide to radio:
Radio – transmission of signals by modulation of electromagnetic waves with frequencies below those of visible light. Electromagnetic radiation travels by means of oscillating electromagnetic fields that pass through the air and the vacuum of space. Information is carried by systematically changing (modulating) some property of the radiated waves, such as amplitude, frequency, phase, or pulse width. When radio waves pass an electrical conductor, the oscillating fields induce an alternating current in the conductor. This can be detected and transformed into sound or other signals that carry information.
Essence of radio
Radio
Broadcasting
Wireless
Radio broadcasting
Applications
Amateur radio
Direction finding
Radio broadcasting
AM broadcasting
FM broadcasting
Shortwave broadcasting
Radar
Radio astronomy
Radio navigation
Radiotelephone
Software-defined radio
Two-way radio (Aviation, Land-based commercial, Government, Marine)
Mission critical communication TETRA and P25
Wireless power transfer
Types of radio broadcasting
Campus radio
Commercial radio
Community radio
International broadcasting
Internet radio
Music radio
Pirate radio
Public radio
Radio broadcasting topics
Disc jockey
Radio documentary
Radio format
Radio personality
Radio programming
History of radio
History of radio
Invention of radio
Wireless telegraphy
Spark-gap transmitter
Alexanders |
https://en.wikipedia.org/wiki/Linotype%20%28alloy%29 | Linotype or eutectic alloy is a broad name applied to five categories of lead alloys used in manufacture of type, especially for the Linotype machine, each with three to five sub-classifications.
One alloy is composed of lead with 4% tin and 12% antimony.
References
Lead alloys |
https://en.wikipedia.org/wiki/New%20York%20Knicks%20all-time%20roster | This is a list of players, both past and current, who appeared at least in one game for the New York Knicks NBA franchise.
Players
Note: Statistics are correct through the end of the season.
A to B
|-
|align="left"| || align="center"|G || align="left"|LIU Brooklyn || align="center"|1 || align="center"| || 28 || 220 || 15 || 23 || 43 || 7.9 || 0.5 || 0.8 || 1.5 || align=center|
|-
|align="left"| || align="center"|F/C || align="left"|Baylor || align="center"|1 || align="center"| || 68 || 1,287 || 301 || 68 || 398 || 18.9 || 4.4 || 1.0 || 5.9 || align=center|
|-
|align="left"| || align="center"|G/F || align="left"|UCLA || align="center"|1 || align="center"| || 71 || 2,371 || 266 || 144 || 909 || 33.4 || 3.7 || 2.0 || 12.8 || align=center|
|-
|align="left"| || align="center"|F/C || align="left"|Morehead State || align="center"|1 || align="center"| || 50 || 453 || 120 || 25 || 192 || 9.1 || 2.4 || 0.5 || 3.8 || align=center|
|-
|align="left"| || align="center"|C || align="left"|Kansas || align="center"|2 || align="center"|– || 107 || 1,306 || 467 || 89 || 430 || 12.2 || 4.4 || 0.8 || 4.0 || align=center|
|-
|align="left"| || align="center"|G || align="left"|Arizona || align="center"|2 || align="center"|–|| 29 || 533 || 60 || 97 || 239 || 18.4 || 2.1 || 3.3 || 8.2 || align=center|
|-
|align="left"| || align="center"|F/C || align="left"|UNLV || align="center"|2 || align="center"|– || 70 || 1,062 || 297 || 77 || 300 || 15.2 || 4.2 || 1.1 || 4.3 || align=center|
|-
|align="left" |
https://en.wikipedia.org/wiki/Meanings%20of%20minor%20planet%20names%3A%20166001%E2%80%93167000 |
166001–166100
|-id=028
| 166028 Karikókatalin || || Katalin Karikó (born 1955) is a Hungarian biochemist and researcher of mRNA-technologies for protein therapies. ||
|}
166101–166200
|-bgcolor=#f2f2f2
| colspan=4 align=center |
|}
166201–166300
|-id=229
| 166229 Palanga || || Palanga is a seaside resort town in western Lithuania ||
|}
166301–166400
|-bgcolor=#f2f2f2
| colspan=4 align=center |
|}
166401–166500
|-bgcolor=#f2f2f2
| colspan=4 align=center |
|}
166501–166600
|-id=570
| 166570 Adolfträger || || Adolf Träger (1888–1965), Czech landscape painter ||
|}
166601–166700
|-id=614
| 166614 Zsazsa || || Zsa Zsa Gábor (1917–2016), Hungarian-American actress and socialite ||
|-id=622
| 166622 Sebastien || || Sébastien Rodriguez (born 1976) is an assistant professor at the University of Paris Diderot and specializes in remote sensing of planetary surfaces and atmospheres. ||
|}
166701–166800
|-id=745
| 166745 Pindor || || Bartosz Pindor (born 1975), Canadian astronomer with the Sloan Digital Sky Survey ||
|-id=746
| 166746 Marcpostman || || Marc Postman (born 1958), American astronomer with the Sloan Digital Sky Survey ||
|-id=747
| 166747 Gordonrichards || || Gordon Richards (born 1972), American astronomer with the Sloan Digital Sky Survey who studies the demographics and physics of quasars ||
|-id=748
| 166748 Timrayschneider || || Donald Schneider (born 1955), American astronomer with the Sloan Digital Sky Survey ||
|-id=749
| |
https://en.wikipedia.org/wiki/Copernicia%20macroglossa | Copernicia macroglossa is a palm endemic to western and central Cuba.
Range and biodiversity
Copernicia macroglossa is a palm endemic to Cuba and thrives on the serpentine soil of most of the Cuban provinces, such as La Habana, Las Villas, and Pinar del Río.
However, this tree has been successfully cultivated within some parts of Central America and some Caribbean islands.
Description
Copernicia macroglossa (also known as the Petticoat palm, Jata palm, and Jata de Guanabacoa) obtained its scientific name from the famous astronomer, Copernicus who proposed the sun was the center of the universe centuries ago. Copernicus proposal perfectly fits the plant since the plant itself has become the center of attention for many gardener around the globe for its magnificent "petticoat" and its majestic structure.
The plant has been known to grow on some impoverished soils that contain the necessary nutrients, natural populations are found within the unique serpentine soils of Cuba.
This palm is extremely drought tolerant and grows best with complete sunlight, with blazing heat and humid conditions. It has a single trunk that can grow to be 8 inches in diameter and over 30 feet high. This palm has upright fan-shaped leaves that grow in a spiral formation along the top of the trunk. From the bottom upper stem, a beard like structure made out of dry fan shaped leaves extend to cover approximately half the trunk which is the famous petticoat, an extremely attractive feature to anyone. |
https://en.wikipedia.org/wiki/McGuire%27s%20Motivations | McGuire’s Psychological Motivations is a classification system that organizes theories of motives into 16 categories. The system helps marketers to isolate motives likely to be involved in various consumption situations.
Categories
McGuire first divided the motivation into two main categories using two criteria:
Is the mode of motivation cognitive or affective?
Is the motive focused on preservation of the status quo or on growth?
Then for each division in each category he stated there is two more basic elements.
Is this behavior actively initiated or in response to the environment?
Does this behavior help the individual achieve a new internal or a new external relationship to the environment?
Divisions of categories
Cognitive Preservation Motives
a. Need for Consistency (active, internal)
b. Need for Attribution (active, external)
c. Need to categorize (passive, internal)
d. Need for objectification (passive, external)
Cognitive Growth Motives
a. Need for Autonomy (active, internal)
b. Need for Stimulation (active, external)
c. Teleological Need (passive, internal)
d. Utilitarian Need (passive, external)
Affective Preservation Motives
a. Need for Tension Reduction
b. Need for Expression (active, external)
c. Need for Ego Defense (passive, internal)
d. Need for Reinforcement (passive, external)
Affective Growth Motives
a. Need for Assertion (active, internal)
b. Need for Affiliation (active, external)
c. Need for Identification (passive, internal)
d. |
https://en.wikipedia.org/wiki/Heterotropic | Heterotropic may refer to:
Heterotropic allosteric modulation of enzymes
Heterotropic modulation of the chemical synapse |
https://en.wikipedia.org/wiki/EKA%20%28supercomputer%29 | EKA (abbreviation of Embedded Karmarkar Algorithm, also means the number One in Sanskrit), is a supercomputer built by the Computational Research Laboratories, a company founded by Dr. Narendra Karmarkar, for scaling up a supercomputer architecture he designed at the Tata Institute of Fundamental Research with a group of his students and project assistants over a period of 6 years.
CRL became a subsidiary of Tata Sons after their investment into the company. The hardware platform required for initial software development was built with technical assistance from Hewlett-Packard.
Design
To enable design of new software, a previously proven hardware platform was needed. This was provided in the EKA system using 14,352 cores based on the Intel QuadCore Xeon processors. The primary interconnect is Infiband 4x DDR. EKA occupies about area. It was built using offshelf components from Hewlett-Packard, Mellanox and Voltaire Limited. It was built within a short period of 6 weeks.
Ranking history
At the time of its unveiling, it was the fourth-fastest supercomputer in the world and the fastest in Asia.
See also
SAGA-220, a 220-TeraFLOPS supercomputer built by ISRO
PARAM series of supercomputers by the Centre for Development of Advanced Computing
Supercomputing in India
References
External links
Eka Top 500 Supercomputer list
Computational Research Laboratories
TCS acquires Computational Research Laboratories
X86 supercomputers
Hewlett-Packard supercomputers
Info |
https://en.wikipedia.org/wiki/Bladder%20cancer%20in%20cats%20and%20dogs | Bladder cancer in cats and dogs usually is transitional cell carcinoma, which arises from the epithelial cells that line the bladder. Less often, cancer of the urinary bladder is squamous cell carcinoma, adenocarcinoma, or rhabdomyosarcoma.
Signs and symptoms
The most frequent symptoms of transitional cell carcinoma are blood in the urine, painful urination, frequent urination and/or straining to urinate. This can look very similar to an infection of the urinary system.
Diagnosis
Diagnostic tests typically include complete blood tests, urinalysis, urine culture, X-rays of the abdomen and chest, and bladder imaging. The definitive diagnosis of bladder cancer will require a tissue biopsy and subsequent examination of the cells under the microscope.
Treatment
Because most bladder cancers are invasive into the bladder wall, surgical removal is usually not possible. The majority of transitional cell carcinomas are treated with either traditional chemotherapy or nonsteroidal anti-inflammatory drugs.
Epidemiology
Compared to other breeds of dog, Scottish terriers have a much increased risk of developing transitional cell carcinoma.
References
Types of animal cancers
Cancer in dogs
Cancer in cats
Bladder cancer |
https://en.wikipedia.org/wiki/Glycosylphosphatidylinositol%20diacylglycerol-lyase | The enzyme glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) catalyzes the reaction
6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming]. Other names in common use include (glycosyl)phosphatidylinositol-specific phospholipase C, GPI-PLC, GPI-specific phospholipase C, VSG-lipase, glycosyl inositol phospholipid anchor-hydrolyzing enzyme, glycosylphosphatidylinositol-phospholipase C, glycosylphosphatidylinositol-specific phospholipase C, variant-surface-glycoprotein phospholipase C, 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol, and diacylglycerol-lyase (1,2-cyclic-phosphate-forming).
References
EC 4.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Holocytochrome-c%20synthase | The enzyme holocytochrome-c synthase (EC 4.4.1.17) catalyzes the chemical reaction
holocytochrome c apocytochrome c + heme
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is holocytochrome-c apocytochrome-c-lyase (heme-forming). Other names in common use include cytochrome c heme-lyase, holocytochrome c synthetase, and holocytochrome-c apocytochrome-c-lyase. This enzyme participates in porphyrin and chlorophyll metabolism.
Cytochrome c heme-lyase (CCHL) and cytochrome Cc1 heme-lyase (CC1HL) are mitochondrial enzymes that catalyze the covalent attachment of a heme group on two cysteine residues of cytochrome c and c1. These two enzymes are functionally and evolutionary related. There are two conserved regions, the first is located in the central section and the second in the C-terminal section. Both patterns contain conserved histidine, tryptophan and acidic residues which could be important for the interaction of the enzymes with the apoproteins and/or the heme group.
The human enzyme, HCCS, processes both cytochromes c and c1.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homocysteine%20desulfhydrase | The enzyme homocysteine desulfhydrase (EC 4.4.1.2) catalyzes the chemical reaction
L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate (overall reaction)
(1a) L-homocysteine = hydrogen sulfide + 2-aminobut-2-enoate
(1b) 2-aminobut-2-enoate = 2-iminobutanoate (spontaneous)
(1c) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-homocysteine hydrogen-sulfide-lyase (deaminating; 2-oxobutanoate-forming). Other names in common use include homocysteine desulfurase, L-homocysteine hydrogen-sulfide-lyase (deaminating). This enzyme participates in nitrogen and sulfur metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 4.4.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-2-amino-4-chloropent-4-enoate%20dehydrochlorinase | The enzyme L-2-amino-4-chloropent-4-enoate dehydrochlorinase (EC 4.5.1.4) catalyzes the reaction
L-2-amino-4-chloropent-4-enoate + H2O 2-oxopent-4-enoate + chloride + NH3
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is L-2-amino-4-chloropent-4-enoate chloride-lyase (adding water; deaminating; 2-oxopent-4-enoate-forming). Other names in common use include L-2-amino-4-chloro-4-pentenoate dehalogenase, and L-2-amino-4-chloropent-4-enoate chloride-lyase (deaminating).
References
EC 4.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-3-cyanoalanine%20synthase | The enzyme L-3-cyanoalanine synthase (EC 4.4.1.9) catalyzes the chemical reaction
L-cysteine + hydrogen cyanide L-3-cyanoalanine + hydrogen sulfide
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteine hydrogen-sulfide-lyase (adding hydrogen cyanide L-3-cyanoalanine-forming). Other names in common use include β-cyanoalanine synthase, β-cyanoalanine synthetase, β-cyano-L-alanine synthase, and L-cysteine hydrogen-sulfide-lyase (adding HCN). This enzyme participates in cyanoamino acid metabolism.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactoylglutathione%20lyase | The enzyme lactoylglutathione lyase (EC 4.4.1.5, also known as glyoxalase I) catalyzes the isomerization of hemithioacetal adducts, which are formed in a spontaneous reaction between a glutathionyl group and aldehydes such as methylglyoxal.
(R)-S-lactoylglutathione = glutathione + 2-oxopropanal
Glyoxalase I derives its name from its catalysis of the first step in the glyoxalase system, a critical two-step detoxification system for methylglyoxal. Methylglyoxal is produced naturally as a byproduct of normal biochemistry, but is highly toxic, due to its chemical reactions with proteins, nucleic acids, and other cellular components. The second detoxification step, in which (R)-S-lactoylglutathione is split into glutathione and D-lactate, is carried out by glyoxalase II, a hydrolase. Unusually, these reactions carried out by the glyoxalase system does not oxidize glutathione, which usually acts as a redox coenzyme. Although aldose reductase can also detoxify methylglyoxal, the glyoxalase system is more efficient and seems to be the most important of these pathways. Glyoxalase I is an attractive target for the development of drugs to treat infections by some parasitic protozoa, and cancer. Several inhibitors of glyoxalase I have been identified, such as S-(N-hydroxy-N-methylcarbamoyl)glutathione.
Glyoxalase I is classified as a carbon-sulfur lyase although, strictly speaking, the enzyme does not form or break a carbon-sulfur bond. Rather, the enzyme shifts two hydrogen atoms |
https://en.wikipedia.org/wiki/L-cysteate%20sulfo-lyase | The enzyme L-cysteate sulfo-lyase (EC 4.4.1.25) catalyzes the reaction
L-cysteate + H2O = hydrogensulfite + pyruvate + NH3 (overall reaction)
(1a) L-cysteate = hydrogensulfite + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteate bisulfite-lyase (deaminating; pyruvate-forming). Other names in common use include L-cysteate sulfo-lyase (deaminating), and CuyA.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leukotriene-C4%20synthase | The enzyme leukotriene-C4 synthase (EC 4.4.1.20) catalyzes the reaction
leukotriene C4 leukotriene A4 + glutathione
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is leukotriene-C4 glutathione-lyase (leukotriene-A4-forming). Other names in common use include leukotriene C4 synthetase, LTC4 synthase, LTC4 synthetase, leukotriene A4:glutathione S-leukotrienyltransferase, (7E,9E,11Z,14Z)-(5S,6R)-5,6-epoxyicosa-7,9,11,14-tetraenoate:glutathione leukotriene-transferase, (epoxide-ring-opening), (7E,9E,11Z,14Z)-(5S,6R)-6-(glutathion-S-yl)-5-hydroxyicosa-7,9,11,14-tetraenoate glutathione-lyase (epoxide-forming). This enzyme participates in arachidonic acid metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 4.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-serine%20ammonia-lyase | The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
L-serine = pyruvate + NH3 (overall reaction)
(1a) L-serine = 2-aminoprop-2-enoate + H2O
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Rete%20pegs | Rete pegs (also known as rete processes or rete ridges) are the epithelial extensions that project into the underlying connective tissue in both skin and mucous membranes.
In the epithelium of the mouth, the attached gingiva exhibit rete pegs, while the sulcular and junctional epithelia do not. Scar tissue lacks rete pegs and scars tend to shear off more easily than normal tissue as a result.
Also known as papillae, they are downward thickenings of the epidermis between the dermal papillae.
References
Dermatology |
https://en.wikipedia.org/wiki/Methionine%20gamma-lyase | The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols:
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate (overall reaction)
(1a) L-methionine = methanethiol + 2-aminobut-2-enoate
(1b) 2-aminobut-2-enoate = 2-iminobutanoate (spontaneous)
(1c) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
Because sulfur-containing amino acids play a role in multiple biological processes, the regulation of these amino acids is essential. Additionally, it is crucial to maintain low homocysteine levels for the proper functioning of various pathways and for preventing the toxic effects of the cysteine homologue. Methionine γ-lyase has been found in several bacteria (Clostridiums porogenes, Pseudomonas ovalis, Pseudomonas putida, Aeromonas sp., Citrobacter intermedius, Brevibacterium linens, Citrobacter freundii, Porphyromonas gingivalis, Treponema denticola), parasitic protozoa (Trichomonas vaginalis, Entamoeba histolytica), and plants (Arabidopsis thaliana).
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-methionine methanethiol-lyase (deaminating; 2-oxobutanoate-forming). Other names in common use include L-methioninase, methionine lyase, methioninase, methionine dethiomethylase, L-methionine γ-lyase, and L-methionine methanethiol-lyase (deaminating). This enzyme pa |
https://en.wikipedia.org/wiki/Methylaspartate%20ammonia-lyase | The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction
L-threo-3-methylaspartate mesaconate + NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-threo-3-methylaspartate ammonia-lyase (mesaconate-forming). Other names in common use include β-methylaspartase, 3-methylaspartase, and L-threo-3-methylaspartate ammonia-lyase. This enzyme participates in c5-branched dibasic acid metabolism and nitrogen metabolism. It employs one cofactor, cobamide.
Structural studies
Several structures of this enzyme have been deposited in the Protein Data Bank (linked in the infobox) which show it possesses a TIM barrel domain.
References
EC 4.3.1
Cobamide enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Ornithine%20cyclodeaminase | The enzyme ornithine cyclodeaminase (EC 4.3.1.12) catalyzes the chemical reaction
L-ornithine L-proline + NH4+
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is Lornithine ammonia-lyase (cyclizing; L-proline-forming). Other names in common use include ornithine cyclase, ornithine cyclase (deaminating), and L-ornithine ammonia-lyase (cyclizing). This enzyme participates in arginine and proline biosynthesis. It employs one cofactor, NAD+.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.3.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Peptidylamidoglycolate%20lyase | The enzyme peptidylamidoglycolate lyase (EC 4.3.2.5) catalyzes the chemical reaction
[peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is [peptide]-(2S)-2-hydroxyglycine peptidyl-amide-lyase (glyoxylate-forming). Other names in common use include α-hydroxyglycine amidating dealkylase, peptidyl-α-hydroxyglycine α-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase.
References
EC 4.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylalanine%20ammonia-lyase | The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.:
L-phenylalanine = trans-cinnamate + NH3
Phenylalanine ammonia lyase (PAL) is the first and committed step in the phenyl propanoid pathway and is therefore involved in the biosynthesis of the polyphenol compounds such as flavonoids, phenylpropanoids, and lignin in plants. Phenylalanine ammonia lyase is found widely in plants, as well as some bacteria, yeast, and fungi, with isoenzymes existing within many different species. It has a molecular mass in the range of 270–330 kDa. The activity of PAL is induced dramatically in response to various stimuli such as tissue wounding, pathogenic attack, light, low temperatures, and hormones. PAL has recently been studied for possible therapeutic benefits in humans afflicted with phenylketonuria. It has also been used in the generation of L-phenylalanine as precursor of the sweetener aspartame.
The enzyme is a member of the ammonia lyase family, which cleaves carbon–nitrogen bonds. Like other lyases, PAL requires only one substrate for the forward reaction, but two for the reverse. It is thought to be mechanistically similar to the related enzyme histidine ammonia-lyase (EC:4.3.1.3, HAL). The systematic name of this enzyme class is L-phenylalanine ammonia-lyase (trans-cinnamate-forming). Previously, it was designated as EC 4.3.1.5, but that class has been redesignated as EC 4.3.1.24 (phenylalanine am |
https://en.wikipedia.org/wiki/Phosphatidylinositol%20diacylglycerol-lyase | The enzyme phosphatidylinositol diacylglycerol-lyase (EC 4.6.1.13) catalyzes the following reaction:
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is 1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-1,2-cyclic-phosphate-forming). Other names in common use include monophosphatidylinositol phosphodiesterase, phosphatidylinositol phospholipase C, 1-phosphatidylinositol phosphodiesterase, 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase, (cyclic-phosphate-forming), 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase, and (1,2-cyclic-phosphate-forming). It participates in inositol phosphate metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphosulfolactate%20synthase | The enzyme phosphosulfolactate synthase (EC 4.4.1.19) catalyzes the reaction
(2R)-2-O-phospho-3-sulfolactate phosphoenolpyruvate + sulfite
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is (2R)-2-O-phospho-3-sulfolactate hydrogen-sulfite-lyase (phosphoenolpyruvate-forming). Other names in common use include (2R)-phospho-3-sulfolactate synthase, and (2R)-O-phospho-3-sulfolactate sulfo-lyase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Purine%20imidazole-ring%20cyclase | The enzyme purine imidazole-ring cyclase (EC 4.3.2.4) catalyzes the chemical reaction
DNA 4,6-diamino-5-formamidopyrimidine DNA adenine + H2O
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is DNA-4,6-diamino-5-formamidopyrimidine C8-N9-lyase (cyclizing DNA-adenine-forming). Other names in common use include DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing), DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing, DNA-adenine-forming).
References
EC 4.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/S-alkylcysteine%20lyase | In enzymology, a S-alkylcysteine lyase () is an enzyme that catalyzes the chemical reaction
an S-alkyl-L-cysteine + water an alkyl thiol + ammonia + pyruvate
Thus, the two substrates of this enzyme are S-alkyl-L-cysteine and water, whereas its three products are alkyl thiol, ammonia, and pyruvate.
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S-alkyl-L-cysteine alkyl-thiol-lyase (deaminating; pyruvate-forming). Other names in common use include S-alkylcysteinase, alkylcysteine lyase, S-alkyl-L-cysteine sulfoxide lyase, S-alkyl-L-cysteine lyase, S-alkyl-L-cysteinase, alkyl cysteine lyase, and S-alkyl-L-cysteine alkylthiol-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
EC 4.4.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/S-carboxymethylcysteine%20synthase | The enzyme S-carboxymethylcysteine synthase (EC 4.5.1.5) catalyzes the reaction
3-chloro-L-alanine + thioglycolate S-carboxymethyl-L-cysteine + chloride
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 3-chloro-L-alanine chloride-lyase (adding thioglycolate; S-carboxymethyl-L-cysteine-forming). This enzyme is also called S-carboxymethyl-L-cysteine synthase. It employs one cofactor, pyridoxal phosphate.
References
EC 4.5.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Selenocysteine%20lyase | The enzyme selenocysteine lyase (SCL) (EC 4.4.1.16) catalyzes the chemical reaction
L-selenocysteine + reduced acceptor selenide + L-alanine + acceptor
Nomenclature
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-selenocysteine selenide-lyase (L-alanine-forming). Other names in common use include selenocysteine reductase, and selenocysteine β-lyase.
Function
This enzyme participates in selenoamino acid metabolism by recycling Se from selenocysteine during the degradation of selenoproteins, providing an alternate source of Se for selenocysteine biosynthesis.
Structure and mechanism
Mammalian SCL forms a homodimer while bacterial SCL is monomeric. In mammals, highest SCL activity is found in the liver and kidney.
While selenocysteine lyases generally catalyze the removal of both selenium or sulfur from selenocysteine or cysteine, respectively, human selenocysteine lyases are specific for selenocysteine. Asp146 has been identified as the key residue that preserves specificity in human SCL.
References
Further reading
EC 4.4.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Serine-sulfate%20ammonia-lyase | The enzyme Serine-sulfate ammonia-lyase (EC 4.3.1.10) catalyzes the chemical reaction
L-serine O-sulfate + H2O pyruvate + NH3 + sulfate
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine-O-sulfate ammonia-lyase (pyruvate-forming). It is also called (L-SOS)lyase.
References
EC 4.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/S-%28hydroxymethyl%29glutathione%20synthase | The enzyme S-(hydroxymethyl)glutathione synthase (EC 4.4.1.22) catalyzes the reaction
S-(hydroxymethyl)glutathione glutathione + formaldehyde
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is ''S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming). Other names in common use include glutathione-dependent formaldehyde-activating enzyme, Gfa, and S''-(hydroxymethyl)glutathione formaldehyde-lyase. This enzyme participates in methane metabolism.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/S-ribosylhomocysteine%20lyase | The enzyme S-ribosylhomocysteine lyase (EC 4.4.1.21) catalyzes the reaction
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
Nomenclature
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]. Other names in common use include S-ribosylhomocysteinase, and LuxS. This enzyme participates in methionine metabolism.
Structure and function
LuxS is a homodimeric iron-dependent metalloenzyme containing two identical tetrahedral metal-binding sites similar to those found in peptidases and amidases. Furthermore, LuxS is involved in the synthesis of autoinducer AI-2 (autoinducer-2), which mediates quorum sensing in roughly half of bacterial species. AI-2, a furanosyl borate diester, is a small signaling molecule generated by bacteria. LuxS converts S-ribosylhomocysteine to homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD); DPD can then spontaneously cyclisize to active AI-2. AI-2 is a signalling molecule that is believed to act in cross-species communication by regulating niche-specific genes with diverse functions, such as toxin production, biofilm formation, sporulation, and virulence gene expression, in various bacteria, often in response to population density. The AI-2 formation pathway begins with S-adenosyl-L-homocysteine (AdoHcy), which |
https://en.wikipedia.org/wiki/Strictosidine%20synthase | Strictosidine synthase (EC 4.3.3.2) is an enzyme in alkaloid biosynthesis that catalyses the condensation of tryptamine with secologanin to form strictosidine in a formal Pictet–Spengler reaction:
3-α(S)-strictosidine + H2O = tryptamine + secologanin
Since the condensation of tryptamine and secologanin is the first committed step in alkaloid synthesis, strictosidine synthase plays a fundamental role for the great majority of the indole-alkaloid pathways.
This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. It can be isolated from several alkaloid-producing plants from the family Apocynaceae (e.g. Catharanthus roseus, Voacanga africana). The systematic name of this enzyme class is 3-α(S)-strictosidine tryptamine-lyase (secologanin-forming). Other names in common use include strictosidine synthetase, STR, and 3-α(S)-strictosidine tryptamine-lyase. Originally isolated from the plant Rauvolfia serpentina, a medicinal plant widely used in Indian folk medicine, this enzyme participates in terpenoid biosynthesis and indole and ipecac alkaloid biosynthesis, both of which produce many compounds with significant physiological and medicinal properties.
Mechanism of catalysis
According to structural studies of strictosidine synthase from Rauvolfia serpentina, tryptamine is located at the bottom of the pocket, where Glu 309 forms a hydrogen bond with the substrate's primary amine group. The residues Phe 226 and Tyr 151, which |
https://en.wikipedia.org/wiki/Sulfolactate%20sulfo-lyase | The enzyme (2R)-sulfolactate sulfo-lyase (EC 4.4.1.24) catalyzes the reaction
(2R)-3-sulfolactate pyruvate + hydrogensulfite
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is (2R)-3-sulfolactate hydrogensulfite-lyase (pyruvate-forming). Other names in common use include Suy, SuyAB, and 3-sulfolactate bisulfite-lyase.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Threo-3-hydroxyaspartate%20ammonia-lyase | The enzyme threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction
threo-3-hydroxy-L-aspartate oxaloacetate + NH3
Nomenclature
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is ''threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use include threo-3-hydroxyaspartate dehydratase, L-threo-3-hydroxyaspartate dehydratase, and threo''-3-hydroxy-L-aspartate ammonia-lyase.
References
EC 4.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Threonine%20ammonia-lyase | Threonine ammonia-lyase (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into α-ketobutyrate and ammonia:
L-threonine = 2-oxobutanoate + NH3 (overall reaction)
(1a) L-threonine = 2-aminobut-2-enoate + H2O
(1b) 2-aminobut-2-enoate = 2-iminobutanoate (spontaneous)
(1c) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
α-Ketobutyrate can be converted into L-isoleucine, so threonine ammonia-lyase functions as a key enzyme in BCAA synthesis. It employs a pyridoxal-5'-phosphate cofactor, similar to many enzymes involved in amino acid metabolism. It is found in bacteria, yeast, and plants, though most research to date has focused on forms of the enzyme in bacteria. This enzyme was one of the first in which negative feedback inhibition by the end product of a metabolic pathway was directly observed and studied. The enzyme serves as an excellent example of the regulatory strategies used in amino acid homeostasis.
Structure
Threonine ammonia-lyase is a tetramer of identical subunits, and is arranged as a dimer of dimers. Each subunit has two domains: a domain containing the catalytic active site and a domain with allosteric regulatory sites. The two have been shown to be distinct regions, but the regulatory site of one subunit actually interacts with the catalytic site of another subunit. Bo |
https://en.wikipedia.org/wiki/Ureidoglycolate%20lyase | The enzyme ureidoglycolate lyase (EC 4.3.2.3) catalyzes the chemical reaction
(S)-ureidoglycolate glyoxylate + urea
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is (S)-ureidoglycolate urea-lyase (glyoxylate-forming). Other names in common use include ureidoglycolatase, ureidoglycolase, ureidoglycolate hydrolase, and (S)-ureidoglycolate urea-lyase. This enzyme participates in purine metabolism.
References
EC 4.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Database%20of%20Interacting%20Proteins | The Database of Interacting Proteins (DIP) is a biological database which catalogs experimentally determined interactions between proteins. It combines information from a variety of sources to create a single, consistent set of protein–protein interactions. The data stored within DIP have been curated, both manually, by expert curators, and automatically, using computational approaches that utilize the knowledge about the protein–protein interaction networks extracted from the most reliable, core subset of the DIP data. The database was initially released in 2002. As of 2014, DIP is curated by the research group of David Eisenberg at UCLA.
DIP can be searched through its web interface; searches may be based on the interactions described in a selected journal article, or interactions supported by experimental evidence, amongst others.
DIP is a member of the International Molecular Exchange Consortium (IMEx), a group of the major public providers of interaction data. Other participating databases include the Biomolecular Interaction Network Database (BIND), IntAct, the Molecular Interaction Database (MINT), MIPS, MPact, and BioGRID. The databases of IMEx work together to prevent duplications of effort, collecting data from non-overlapping sources and sharing the curated interaction data. The IMEx consortium also worked to develop the HUPO-PSI-MI XML format, which is now widely implemented.
All of the information within DIP is freely available under a Creative Commons BY-ND 3 |
https://en.wikipedia.org/wiki/Lee%20Kang-jo | Lee Kang-jo (Hangul: 이강조; Hanja: 李康助; born October 27, 1954) is a South Korean football manager.
Club career statistics
Coach & manager career
1985–1986: Yukong Elephants Trainer
1987–1989: Gangneung Jeil High School Manager
1990–2002: Sangmu FC Manager
2003–present: Gwangju Sangmu FC Manager
International goals
Results list South Korea's goal tally first.
External links
1954 births
Living people
Men's association football midfielders
South Korean men's footballers
South Korea men's international footballers
South Korean football managers
K League 1 players
1980 AFC Asian Cup players
1984 AFC Asian Cup players
Gimcheon Sangmu FC managers
jeju United FC managers
Korea University alumni
Asian Games gold medalists for South Korea
Medalists at the 1978 Asian Games
Asian Games medalists in football
Footballers at the 1978 Asian Games |
https://en.wikipedia.org/wiki/Viral%20tegument | A viral tegument or tegument, more commonly known as a viral matrix, is a cluster of proteins that lines the space between the envelope and nucleocapsid of all herpesviruses. The tegument generally contains proteins that aid in viral DNA replication and evasion of the immune response, typically with inhibition of signalling in the immune system and activation of interferons. The tegument is usually released shortly after infection into the cytoplasm. These proteins are usually formed within the late phase of the viral infectious cycle, after viral genes have been replicated. Much information regarding viral teguments has been gathered from studying herpes simplex virus.
Properties of teguments
Viral teguments can be symmetrically arranged via structural and scaffolding protein or can also be asymmetrically arranged, depending on the virus. Teguments are rarely haphazardly placed and usually involve scaffolding proteins in their formation around the nucleocapsid. Non-essential proteins included in the tegument may aid in immune response suppression, suppression of host mRNA transcription or suppression of intrinsic or cellular defenses. Essential proteins will include factors that help in trafficking of the viral capsid to the nucleus (for herpesviruses), recruiting host transcription or translation factors, or directly transcribing or translating viral genes. Tegumental contents are released into the cytoplasm upon entrance into the cell upon which many tegumental proteins |
https://en.wikipedia.org/wiki/3-hydroxymethylcephem%20carbamoyltransferase | In enzymology, a 3-hydroxymethylcephem carbamoyltransferase () is an enzyme that catalyzes the chemical reaction
carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate phosphate + a 3-carbamoyloxymethylcephem
Thus, the two substrates of this enzyme are carbamoyl phosphate and 3-hydroxymethylceph-3-em-4-carboxylate, whereas its two products are phosphate and 3-carbamoyloxymethylcephem.
This enzyme belongs to the family of transferases, that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases.
The systematic name of this enzyme class is carbamoyl-phosphate:3-hydroxymethylceph-3-em-4-carboxylate carbamoyltransferase.
This enzyme has at least one effector, ATP.
References
EC 2.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate%20hydroxymethyltransferase | In enzymology, a 3-methyl-2-oxobutanoate hydroxymethyltransferase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O tetrahydrofolate + 2-dehydropantoate
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, 3-methyl-2-oxobutanoate, and H2O, whereas its two products are tetrahydrofolate and 2-dehydropantoate.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase. Other names in common use include alpha-ketoisovalerate hydroxymethyltransferase, dehydropantoate hydroxymethyltransferase, ketopantoate hydroxymethyltransferase, oxopantoate hydroxymethyltransferase, 5,10-methylene tetrahydrofolate:alpha-ketoisovalerate, and hydroxymethyltransferase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-alanine%202-hydroxymethyltransferase | In enzymology, a D-alanine 2-hydroxymethyltransferase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + D-alanine + H2O tetrahydrofolate + 2-methylserine
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, D-alanine, and H2O, whereas its two products are tetrahydrofolate and 2-methylserine.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase. This enzyme is also called 2-methylserine hydroxymethyltransferase. This enzyme participates in one carbon pool by folate.
References
EC 2.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxycytidylate%205-hydroxymethyltransferase | In enzymology, a deoxycytidylate 5-hydroxymethyltransferase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, H2O, and deoxycytidylate, whereas its two products are tetrahydrofolate and 5-hydroxymethyldeoxycytidylate.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:deoxycytidylate 5-hydroxymethyltransferase. Other names in common use include dCMP hydroxymethylase, d-cytidine 5'-monophosphate hydroxymethylase, deoxyCMP hydroxymethylase, deoxycytidylate hydroxymethylase, and deoxycytidylic hydroxymethylase. This enzyme participates in pyrimidine metabolism and one carbon pool by folate.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycine%20formimidoyltransferase | In enzymology, a glycine formimidoyltransferase () is an enzyme that catalyzes the chemical reaction
5-formimidoyltetrahydrofolate + glycine tetrahydrofolate + N-formimidoylglycine
Thus, the two substrates of this enzyme are 5-formimidoyltetrahydrofolate and glycine, whereas its two products are tetrahydrofolate and N-formimidoylglycine.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5-formimidoyltetrahydrofolate:glycine N-formimidoyltransferase. Other names in common use include formiminoglycine formiminotransferase, FIG formiminotransferase, and glycine formiminotransferase. This enzyme participates in purine metabolism and one carbon pool by folate.
References
EC 2.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysine%20carbamoyltransferase | In enzymology, a lysine carbamoyltransferase () is an enzyme that catalyzes the chemical reaction
carbamoyl phosphate + L-lysine phosphate + L-homocitrulline
Thus, the two substrates of this enzyme are carbamoyl phosphate and L-lysine, whereas its two products are phosphate and L-homocitrulline.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:L-lysine carbamoyltransferase. This enzyme is also called lysine transcarbamylase.
References
EC 2.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methionyl-tRNA%20formyltransferase | In enzymology, a methionyl-tRNA formyltransferase () is an enzyme that catalyzes the chemical reaction
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O tetrahydrofolate + N-formylmethionyl-tRNAfMet
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase. Other names in common use include N10-formyltetrahydrofolic-methionyl-transfer ribonucleic, transformylase, formylmethionyl-transfer ribonucleic synthetase, methionyl ribonucleic formyltransferase, methionyl-tRNA Met formyltransferase, methionyl-tRNA transformylase, methionyl-transfer RNA transformylase, methionyl-transfer ribonucleate methyltransferase, and methionyl-transfer ribonucleic transformylase. This enzyme participates in 3 metabolic pathways: methionine metabolism, one carbon pool by folate, and aminoacyl-tRNA biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylmalonyl-CoA%20carboxytransferase | In enzymology, a methylmalonyl-CoA carboxytransferase () is an enzyme that catalyzes the chemical reaction
(S)-methylmalonyl-CoA + pyruvate propanoyl-CoA + oxaloacetate
Thus, the two substrates of this enzyme are (S)-methylmalonyl-CoA and pyruvate, whereas its two products are propanoyl-CoA and oxaloacetate.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is (S)-methylmalonyl-CoA:pyruvate carboxytransferase. Other names in common use include transcarboxylase, methylmalonyl coenzyme A carboxyltransferase, methylmalonyl-CoA transcarboxylase, oxalacetic transcarboxylase, methylmalonyl-CoA carboxyltransferase, methylmalonyl-CoA carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase, and carboxytransferase [incorrect]. This enzyme participates in propanoate metabolism. It has 3 cofactors: zinc, Biotin, and Cobalt.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
EC 2.1.3
Zinc enzymes
Biotin enzymes
Cobalt enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetylornithine%20carbamoyltransferase | In enzymology, a N-acetylornithine carbamoyltransferase () is an enzyme that catalyzes the chemical reaction
carbamoyl phosphate + N2-acetyl-L-ornithine phosphate + N-acetyl-L-citrulline
Thus, the two substrates of this enzyme are carbamoyl phosphate and N2-acetyl-L-ornithine, whereas its two products are phosphate and N-acetyl-L-citrulline.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase. Other names in common use include acetylornithine transcarbamylase, N-acetylornithine transcarbamylase, AOTC, and carbamoyl-phosphate:2-N-acetyl-L-ornithine carbamoyltransferase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Oxamate%20carbamoyltransferase | In enzymology, an oxamate carbamoyltransferase () is an enzyme that catalyzes the chemical reaction
carbamoyl phosphate + oxamate phosphate + oxalureate
Thus, the two substrates of this enzyme are carbamoyl phosphate and oxamate, whereas its two products are phosphate and oxalureate.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:oxamate carbamoyltransferase. This enzyme is also called oxamic transcarbamylase. This enzyme participates in purine metabolism.
References
EC 2.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoribosylaminoimidazolecarboxamide%20formyltransferase | In enzymology, a phosphoribosylaminoimidazolecarboxamide formyltransferase (), also known by the shorter name AICAR transformylase, is an enzyme that catalyzes the chemical reaction
10-formyltetrahydrofolate + AICAR tetrahydrofolate + FAICAR
Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and AICAR, whereas its two products are tetrahydrofolate and FAICAR.
This enzyme participates in purine metabolism and one carbon pool by folate.
Nomenclature
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazole-carb oxamide N-formyltransferase. Other names in common use include:
10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
5-amino-1-ribosyl-4-imidazolecarboxamide 5-phosphate,
5-amino-4-imidazolecarboxamide ribonucleotide transformylase,
5-amino-4-imidazolecarboxamide ribotide transformylase,
5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase,
AICAR formyltransferase,
AICAR transformylase,
aminoimidazolecarboxamide ribonucleotide transformylase, and
transformylase,
bifunctional purine biosynthesis protein PURH,
ATIC.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 2.1.2
Enzy |
https://en.wikipedia.org/wiki/Putrescine%20carbamoyltransferase | In enzymology, a putrescine carbamoyltransferase () is an enzyme that catalyzes the chemical reaction
carbamoyl phosphate + putrescine phosphate + N-carbamoylputrescine
Thus, the two substrates of this enzyme are carbamoyl phosphate and putrescine, whereas its two products are phosphate and N-carbamoylputrescine.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:putrescine carbamoyltransferase. Other names in common use include PTCase, putrescine synthase, and putrescine transcarbamylase.
References
EC 2.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Scyllo-inosamine-4-phosphate%20amidinotransferase | In enzymology, a scyllo-inosamine-4-phosphate amidinotransferase () is an enzyme that catalyzes the chemical reaction
L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate
Thus, the two substrates of this enzyme are L-arginine and 1-amino-1-deoxy-scyllo-inositol 4-phosphate, whereas its two products are L-ornithine and 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the amidinotransferases. The systematic name of this enzyme class is L-arginine:1-amino-1-deoxy-scyllo-inositol-4-phosphate amidinotransferase. Other names in common use include L-arginine:inosamine-P-amidinotransferase, inosamine-P amidinotransferase, L-arginine:inosamine phosphate amidinotransferase, and inosamine-phosphate amidinotransferase. This enzyme participates in streptomycin biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.1.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aliphatic%20aldoxime%20dehydratase | In enzymology, an aliphatic aldoxime dehydratase () is an enzyme that catalyzes the chemical reaction
an aliphatic aldoxime an aliphatic nitrile + H2O
This dehydratase converts an aldoxime on an aliphatic substrate to a nitrile as the product structure with water as byproduct.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming). Other names in common use include OxdA, and aliphatic aldoxime hydro-lyase.
See also
D-amino acid oxidase, sometimes also referred to as OXDA
References
EC 4.99.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylmercury%20lyase | The enzyme alkylmercury lyase (EC 4.99.1.2) catalyzes the reaction
an alkylmercury + H+ an alkane + Hg2+
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is alkylmercury mercury(II)-lyase (alkane-forming). Other names in common use include organomercury lyase, organomercurial lyase, and alkylmercury mercuric-lyase.
The enzyme converts methyl mercury to the much less toxic elemental form of the metal.
References
EC 4.99.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Indoleacetaldoxime%20dehydratase | In enzymology, an indoleacetaldoxime dehydratase () is an enzyme that catalyzes the chemical reaction
(indol-3-yl)acetaldehyde oxime (indol-3-yl)acetonitrile + H2O
Hence, this enzyme has one substrate, (indol-3-yl)acetaldehyde oxime, and two products, (indol-3-yl)acetonitrile and H2O.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is (indol-3-yl)acetaldehyde-oxime hydro-lyase [(indol-3-yl)acetonitrile-forming]. Other names in common use include indoleacetaldoxime hydro-lyase, 3-indoleacetaldoxime hydro-lyase, indole-3-acetaldoxime hydro-lyase, indole-3-acetaldehyde-oxime hydro-lyase, and (indol-3-yl)acetaldehyde-oxime hydro-lyase. This enzyme participates in cyanoamino acid metabolism.
References
EC 4.99.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylacetaldoxime%20dehydratase | In enzymology, a phenylacetaldoxime dehydratase () is an enzyme that catalyzes the chemical reaction
(Z)-phenylacetaldehyde oxime phenylacetonitrile + H2O
Hence, this enzyme has one substrate, (Z)-phenylacetaldehyde oxime, and two products, phenylacetonitrile and H2O.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is (Z)-phenylacetaldehyde-oxime hydro-lyase (phenylacetonitrile-forming). Other names in common use include PAOx dehydratase, arylacetaldoxime dehydratase, OxdB, and (Z)-phenylacetaldehyde-oxime hydro-lyase. This enzyme participates in styrene degradation.
References
EC 4.99.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sirohydrochlorin%20cobaltochelatase | The enzyme sirohydrochlorin cobaltochelatase (EC 4.99.1.3) catalyzes the reaction
cobalt-sirohydrochlorin + 2 H+ = sirohydrochlorin + Co2+
In the forward direction of reactions towards cobalamin in anaerobic bacteria, the two substrates of this enzyme are sirohydrochlorin and Co2+; its two products are cobalt-sirohydrochlorin and H+.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming). Other names in common use include CbiK, CbiX, CbiXS, anaerobic cobalt chelatase, cobaltochelatase [ambiguous], and sirohydrochlorin cobalt-lyase (incorrect). This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria such as Salmonella typhimurium and Bacillus megaterium. It has also been identified as the enzyme which inserts nickel into sirohydrochlorin in the biosynthesis of cofactor F430, reaction .
See also
Cobalamin biosynthesis
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
Further reading
EC 4.99.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Sirohydrochlorin%20ferrochelatase | The enzyme sirohydrochlorin ferrochelatase (EC 4.99.1.4) catalyzes the following reaction:
siroheme + 2H+ sirohydrochlorin + Fe2+
This enzyme belongs to the family of lyases, to be specific the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is siroheme ferro-lyase (sirohydrochlorin-forming). The enzyme is also known as SirB and present in all plants and nitrate and sulfate assimilating/dissimilating bacteria. Siroheme is a co-factor of both assimilatory and dissimilatory nitrite and sulfite reductases. Siroheme is synthesized from the central tetrapyrrole molecule uroporphyrinogen III, which forms the first branch-point of tetrapyrrole biosynthetic pathway, the other branch being the heme/chlorophyll branch. The siroheme branch consists of three steps: methylation, dehydrogenation, and ferrochelation, with the last step carried out by sirohydrochlorin ferrochelatase.
Sirohydrochlorin ferrochelatase is a class II chelatase, i.e. it does not require ATP for its activity unlike class I chelatases such as Mg-chelatase. In E. coli, all three steps of siroheme biosynthesis are carried out by a single multifunctional enzyme called CysG, while in yeast Saccharomyces cerevisiae the last two steps are carried out by a bifunctional enzyme called Met8p. CysG and Met8p share common folds but are unrelated to SirB and constitute the so-called class III chelatase. SirB belongs to CbiX family protein and the plant SirB is |
https://en.wikipedia.org/wiki/3-mercaptopyruvate%20sulfurtransferase | In enzymology, a 3-mercaptopyruvate sulfurtransferase () is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.
The enzyme is of interest because it provides a pathway for detoxification of cyanide, especially since it occurs widely in the cytosol and distributed broadly.
Nomenclature
The systematic name of this enzyme class is 3-mercaptopyruvate:cyanide sulfurtransferase. This enzyme is also called beta-mercaptopyruvate sulfurtransferase and in the older literature, human liver rhodanese.
Structure
Gene
The MPST gene lies on the chromosome location of 22q12.3 and consists of 6 exons. Alternatively spliced transcript variants encoding the same protein have been identified.
Protein
The encoded cytoplasmic protein is a member of the rhodanese family but is not rhodanese itself, which is found only in mitochondria. MPST protein consists of 317 amino acid residues and weighs 35250Da. MPST contains two rhodanese domains with similar secondary structures suggesting a common evolutionary origin. The catalytic cysteine residue only exists in the C-terminal rhodanese domain. The protein can function as a monomer or as a disulfide-linked homodimer.
Function and mechanism
The biological function of MPST remains unclear. It may be involved in cyanide detoxification, biosynthesis of thiosulf |
https://en.wikipedia.org/wiki/3-oxoacid%20CoA-transferase | In enzymology, a 3-oxoacid CoA-transferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + a 3-oxo acid succinate + a 3-oxoacyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and 3-oxo acid, whereas its two products are succinate and 3-oxoacyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:3-oxo-acid CoA-transferase. Other names in common use include succinyl-CoA-3-ketoacid-CoA transferase, 3-oxoacid coenzyme A-transferase, 3-ketoacid CoA-transferase, 3-ketoacid coenzyme A transferase, 3-oxo-CoA transferase, 3-oxoacid CoA dehydrogenase, acetoacetate succinyl-CoA transferase, acetoacetyl coenzyme A-succinic thiophorase, succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA transferase. This enzyme participates in 3 metabolic pathways: synthesis and degradation of ketone bodies, valine, leucine and isoleucine degradation, and butanoate metabolism.
This protein may use the morpheein model of allosteric regulation.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 2.8.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-oxoadipate%20CoA-transferase | In enzymology, a 3-oxoadipate CoA-transferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + 3-oxoadipate succinate + 3-oxoadipyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and 3-oxoadipate, whereas its two products are succinate and 3-oxoadipyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:3-oxoadipate CoA-transferase. Other names in common use include 3-oxoadipate coenzyme A-transferase, and 3-oxoadipate succinyl-CoA transferase. This enzyme participates in benzoate degradation via hydroxylation.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-hydroxypentanoate%20CoA-transferase | In enzymology, a 5-hydroxypentanoate CoA-transferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 5-hydroxypentanoate acetate + 5-hydroxypentanoyl-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and 5-hydroxypentanoate, whereas its two products are acetate and 5-hydroxypentanoyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:5-hydroxypentanoate CoA-transferase. Other names in common use include 5-hydroxyvalerate CoA-transferase, and 5-hydroxyvalerate coenzyme A transferase.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetate%20CoA-transferase | In enzymology, an acetate CoA-transferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + acetate a fatty acid anion + acetyl-CoA
Thus, the two substrates of this enzyme are acyl-CoA and acetate, whereas its two products are long-chain carboxylate anion and acetyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acyl-CoA:acetate CoA-transferase. Other names in common use include acetate coenzyme A-transferase, butyryl CoA:acetate CoA transferase, butyryl coenzyme A transferase, and succinyl-CoA:acetate CoA transferase.
This enzyme participates in 4 metabolic pathways:
benzoate metabolism via ligation of CoA
propanoate metabolism
butanoate metabolism
two-component system.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
External links
EC 2.8.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Amine%20sulfotransferase | In enzymology, an amine sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + an amine adenosine 3',5'-bisphosphate + a sulfamate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and amine, whereas its two products are adenosine 3',5'-bisphosphate and sulfamate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:amine N-sulfotransferase. Other names in common use include arylamine sulfotransferase, and amine N-sulfotransferase. This enzyme participates in sulfur metabolism.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-sulfate%20sulfotransferase | In enzymology, an aryl-sulfate sulfotransferase () is an enzyme that catalyzes the chemical reaction
an aryl sulfate + a phenol a phenol + an aryl sulfate
Thus, the two substrates of this enzyme are aryl sulfate and phenol, whereas its two products are phenol and aryl sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is aryl-sulfate:phenol sulfotransferase. Other names in common use include arylsulfate-phenol sulfotransferase, arylsulfotransferase, ASST, arylsulfate sulfotransferase, and arylsulfate:phenol sulfotransferase.
See also
Phenol sulfur-transferase deficiency
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl%20sulfotransferase | An aryl sulfotransferase () is an enzyme that
transfers a sulfate group from phenolic sulfate esters to a phenolic acceptor substrate.
3'-phosphoadenylyl sulfate + a phenol adenosine 3',5'-bisphosphate + an aryl sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and phenol, whereas its two products are adenosine 3',5'-bisphosphate and aryl sulfate.
These enzymes are transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:phenol sulfotransferase. Other names in common use include phenol sulfotransferase, sulfokinase, 1-naphthol phenol sulfotransferase, 2-naphtholsulfotransferase, 4-nitrocatechol sulfokinase, arylsulfotransferase, dopamine sulfotransferase, p-nitrophenol sulfotransferase, phenol sulfokinase, ritodrine sulfotransferase, and PST. This enzyme participates in sulfur metabolism.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
Further reading
EC 2.8.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Biotin%20synthase | Biotin synthase (BioB) () is an enzyme that catalyzes the conversion of dethiobiotin (DTB) to biotin; this is the final step in the biotin biosynthetic pathway. Biotin, also known as vitamin B7, is a cofactor used in carboxylation, decarboxylation, and transcarboxylation reactions in many organisms including humans. Biotin synthase is an S-Adenosylmethionine (SAM) dependent enzyme that employs a radical mechanism to thiolate dethiobiotin, thus converting it to biotin.
This radical SAM enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is dethiobiotin:sulfur sulfurtransferase. This enzyme participates in biotin metabolism. It employs one cofactor, iron-sulfur.
Structure
In 2004, the crystal structure of biotin synthase in complex with SAM and dethiobiotin was determined to 3.4 angstrom resolution. The PDB accession code for this structure is . The protein is a homodimer, meaning it is composed of two identical amino acid chains that fold together to form biotin synthase. Each monomer in the structure shown in figure contains a TIM barrel with an [4Fe-4S]2+cluster, SAM, and an [2Fe-2S]2+cluster.
The [4Fe-4S]2+cluster is used as a catalytic cofactor, directly coordinating to SAM. Orbital overlap between SAM and a unique Fe atom on the [4Fe-4S]2+cluster has been observed. The predicted role of the [4Fe-4S]2+cofactor is to transfer an electron onto SAM through |
https://en.wikipedia.org/wiki/Butyrate%E2%80%94acetoacetate%20CoA-transferase | In enzymology, a butyrate-acetoacetate CoA-transferase () is an enzyme that catalyzes the chemical reaction
butanoyl-CoA + acetoacetate butanoate + acetoacetyl-CoA
Thus, the two substrates of this enzyme are butanoyl-CoA and acetoacetate, whereas its two products are butanoate and acetoacetyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is butanoyl-CoA:acetoacetate CoA-transferase. Other names in common use include butyryl coenzyme A-acetoacetate coenzyme A-transferase, and butyryl-CoA-acetoacetate CoA-transferase.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Choline%20sulfotransferase | In enzymology, a choline sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + choline adenosine 3',5'-bisphosphate + choline sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and choline, whereas its two products are adenosine 3',5'-bisphosphate and choline sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:choline sulfotransferase. This enzyme is also called choline sulphokinase. This enzyme participates in sulfur metabolism.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondroitin%204-sulfotransferase | In enzymology, a chondroitin 4-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenosine-5'-phosphosulfate + chondroitin adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and chondroitin, whereas its two products are adenosine 3',5'-bisphosphate and chondroitin 4'-sulfate.
This enzyme belongs to the family of transferases, to be specific, the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:chondroitin 4'-sulfotransferase. This enzyme is also called chondroitin sulfotransferase. This enzyme participates in 3 metabolic pathways: chondroitin sulfate biosynthesis, sulfur metabolism, and the biosynthesis of glycan structures.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondroitin%206-sulfotransferase | In enzymology, a chondroitin 6-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + chondroitin adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and chondroitin, whereas its two products are adenosine 3',5'-bisphosphate and Chondroitin 6-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:chondroitin 6'-sulfotransferase. Other names in common use include chondroitin 6-O-sulfotransferase, 3'-phosphoadenosine 5'-phosphosulfate (PAPS):chondroitin sulfate, sulfotransferase, and terminal 6-sulfotransferase. This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cinnamoyl-CoA%3Aphenyllactate%20CoA-transferase | In enzymology, a cinnamoyl-CoA:phenyllactate CoA-transferase () is an enzyme that catalyzes the chemical reaction
(E)-cinnamoyl-CoA + (R)-phenyllactate (E)-cinnamate + (R)-phenyllactyl-CoA
Thus, the two substrates of this enzyme are (E)-cinnamoyl-CoA and (R)-phenyllactate, whereas its two products are (E)-cinnamate and (R)-phenyllactyl-CoA.
This enzyme belongs to the CoA-transferase family. The systematic name of this enzyme class is (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase. This enzyme is also called FldA.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Citramalate%20CoA-transferase | In enzymology, a citramalate CoA-transferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + citramalate acetate + (3S)-citramalyl-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and citramalate, whereas its two products are acetate and (3S)-citramalyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:citramalate CoA-transferase. This enzyme participates in c5-branched dibasic acid metabolism.
References
EC 2.8.3
Enzymes of unknown structure |
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