An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.
A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
A polypeptide antibiotic mixture obtained from Bacillus brevis. It consists of a mixture of three tyrocidines (60%) and several gramicidins (20%) and is very toxic to blood, liver, kidneys, meninges, and the olfactory apparatus. It is used topically.
A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.
Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.
Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.
Compounds containing the -SH radical.
Guidelines and objectives pertaining to food supply and nutrition including recommendations for healthy diet.
The amounts of various substances in food needed by an organism to sustain healthy life.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
The amounts of various substances in the diet recommended by governmental guidelines as needed to sustain healthy life.
Any food that has been supplemented with essential nutrients either in quantities that are greater than those present normally, or which are not present in the food normally. Fortified food includes also food to which various nutrients have been added to compensate for those removed by refinement or processing. (From Segen, Dictionary of Modern Medicine, 1992)

Analysis of 4-phosphopantetheinylation of polyhydroxybutyrate synthase from Ralstonia eutropha: generation of beta-alanine auxotrophic Tn5 mutants and cloning of the panD gene region. (1/116)

The postulated posttranslational modification of the polyhydroxybutyrate (PHA) synthase from Ralstonia eutropha by 4-phosphopantetheine was investigated. Four beta-alanine auxotrophic Tn5-induced mutants of R. eutropha HF39 were isolated, and two insertions were mapped in an open reading frame with strong similarity to the panD gene from Escherichia coli, encoding L-aspartate-1-decarboxylase (EC 4.1.1.15), whereas two other insertions were mapped in an open reading frame (ORF) with strong similarity to the NAD(P)+ transhydrogenase (EC 1.6.1.1) alpha 1 subunit, encoded by the pntAA gene from Escherichia coli. The panD gene was cloned by complementation of the panD mutant of R. eutropha Q20. DNA sequencing of the panD gene region (3,312 bp) revealed an ORF of 365 bp, encoding a protein with 63 and 67% amino acid sequence similarity to PanD from E. coli and Bacillus subtilis, respectively. Subcloning of only this ORF into vectors pBBR1MCS-3 and pBluescript KS- led to complementation of the panD mutants of R. eutropha and E. coli SJ16, respectively. panD-encoded L-aspartate-1-decarboxylase was further confirmed by an enzymatic assay. Upstream of panD, an ORF with strong similarity to pntAA from E. coli, encoding NAD(P)+ transhydrogenase subunit alpha 1 was found; downstream of panD, two ORFs with strong similarity to pntAB and pntB, encoding subunits alpha 2 and beta of the NAD(P)+ transhydrogenase, respectively, were identified. Thus, a hitherto undetermined organization of pan and pnt genes was found in R. eutropha. Labeling experiments using one of the R. eutropha panD mutants and [2-14C]beta-alanine provided no evidence that R. eutropha PHA synthase is covalently modified by posttranslational attachment of 4-phosphopantetheine, nor did the E. coli panD mutant exhibit detectable labeling of functional PHA synthase from R. eutropha.  (+info)

Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. (2/116)

In nonribosomal biosynthesis of peptide antibiotics by multimodular synthetases, amino acid monomers are activated by the adenylation domains of the synthetase and loaded onto the adjacent carrier protein domains as thioesters, then the formation of peptide bonds and translocation of the growing chain are effected by the synthetase's condensation domains. Whether the condensation domains have any editing function has been unknown. Synthesis of aminoacyl-coenzyme A (CoA) molecules and direct enzymatic transfer of aminoacyl-phosphopantetheine to the carrier domains allow the adenylation domain editing function to be bypassed. This method was used to demonstrate that the first condensation domain of tyrocidine synthetase shows low selectivity at the donor residue (D-phenylalanine) and higher selectivity at the acceptor residue (L-proline) in the formation of the chain-initiating D-Phe-L-Pro dipeptidyl-enzyme intermediate.  (+info)

Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model. (3/116)

The objective of this study was to test a new model for the homodimeric animal FAS which implies that the condensation reaction can be catalyzed by the amino-terminal beta-ketoacyl synthase domain in cooperation with the penultimate carboxyl-terminal acyl carrier protein domain of either subunit. Treatment of animal fatty acid synthase dimers with dibromopropanone generates three new molecular species with decreased electrophoretic mobilities; none of these species are formed by fatty acid synthase mutant dimers lacking either the active-site cysteine of the beta-ketoacyl synthase domain (C161A) or the phosphopantetheine thiol of the acyl carrier protein domain (S2151A). A double affinity-labeling strategy was used to isolate dimers that carried one or both mutations on one or both subunits; the heterodimers were treated with dibromopropanone and analyzed by a combination of sodium dodecyl sulfate/polyacrylamide gel electrophoresis, Western blotting, gel filtration, and matrix-assisted laser desorption mass spectrometry. Thus the two slowest moving of these species, which accounted for 45 and 15% of the total, were identified as doubly and singly cross-linked dimers, respectively, whereas the fastest moving species, which accounted for 35% of the total, was identified as originating from internally cross-linked subunits. These results show that the two polypeptides of the fatty acid synthase are oriented such that head-to-tail contacts are formed both between and within subunits, and provide the first structural evidence in support of the new model.  (+info)

Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli. (4/116)

Holo-(acyl carrier protein) synthase (AcpS) post-translationally modifies apoacyl carrier protein (apoACP) via transfer of 4'-phosphopantetheine from coenzyme A (CoA) to the conserved serine 36 gamma-OH of apoACP. The resulting holo-acyl carrier protein (holo-ACP) is then active as the central coenzyme of fatty acid biosynthesis. The acpS gene has previously been identified and shown to be essential for Escherichia coli growth. Earlier mutagenic studies isolated the E. coli MP4 strain, whose elevated growth requirement for CoA was ascribed to a deficiency in holoACP synthesis. Sequencing of the acpS gene from the E. coli MP4 strain (denoted acpS1) showed that the AcpS1 protein contains a G4D mutation. AcpS1 exhibited a approximately 5-fold reduction in its catalytic efficiency when compared with wild type AcpS, accounting for the E. coli MP4 strain phenotype. It is shown that a conditional acpS mutant accumulates apoACP in vivo under nonpermissive conditions in a manner similar to the E. coli MP4 strain. In addition, it is demonstrated that the gene product, YhhU, of a previously identified E. coli open reading frame can completely suppress the acpS conditional, lethal phenotype upon overexpression of the protein, suggesting that YhhU may be involved in an alternative pathway for phosphopantetheinyl transfer and holoACP synthesis in E. coli.  (+info)

Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis. (5/116)

The lantibiotic-synthesizing flavoprotein EpiD catalyzes the oxidative decarboxylation of peptidylcysteines to peptidyl-aminoenethiols. The sequence motif responsible for flavin coenzyme binding and enzyme activity is conserved in different proteins from all kingdoms of life. Dfp proteins of eubacteria and archaebacteria and salt tolerance proteins of yeasts and plants belong to this new family of flavoproteins. The enzymatic function of all these proteins was not known, but our experiments suggested that they catalyze a similar reaction like EpiD and/or may have similar substrates and are homododecameric flavoproteins. We demonstrate that the N-terminal domain of the Escherichia coli Dfp protein catalyzes the decarboxylation of (R)-4'-phospho-N-pantothenoylcysteine to 4'-phosphopantetheine. This reaction is essential for coenzyme A biosynthesis.  (+info)

Identification of an NADH-linked disulfide reductase from Bacillus megaterium specific for disulfides containing pantethine 4',4''-diphosphate moieties. (6/116)

Bacillus megaterium contains an NADH-linked disulfide reductase that is specific for disulfides containing pantethine 4',4''-diphosphate moieties. This reductase is at its highest level in cells late in sporulation and in dormant spores, and could be involved in the formation and cleavage of coenzyme A-protein disulfides which take place late in sporulation and early in spore germination, respectively.  (+info)

Purification, priming, and catalytic acylation of carrier protein domains in the polyketide synthase and nonribosomal peptidyl synthetase modules of the HMWP1 subunit of yersiniabactin synthetase. (7/116)

The 207-kDa polyketide synthase (PKS) module (residues 1-1895) and the 143-kDa nonribosomal peptidyl synthetase (NRPS) module (1896-3163) of the 350-kDa HMWP1 subunit of yersiniabactin synthetase have been expressed in and purified from Escherichia coli in soluble forms to characterize the acyl carrier protein (ACP) domain of the PKS module and the homologous peptidyl carrier protein (PCP(3)) domain of the NRPS module. The apo-ACP and PCP domains could be selectively posttranslationally primed by the E. coli ACPS and EntD phosphopantetheinyl transferases (PPTases), respectively, whereas the Bacillus subtilis PPTase Sfp primed both carrier protein domains in vitro or during in vivo coexpression. The holo-NRPS module but not the holo-PKS module was then selectively aminoacylated with cysteine by the adenylation domain embedded in the HMWP2 subunit of yersiniabactin synthetase, acting in trans. When the acyltransferase (AT) domain of HMWP1 was analyzed for its ability to malonylate the holo carrier protein domains, in cis acylation was first detected. Then, in trans malonylation of the excised holo-ACP or holo-PCP(3)-TE fragments by HMWP1 showed both were malonylated with a 3:1 catalytic efficiency ratio, showing a promiscuity to the AT domain.  (+info)

Arabidopsis thaliana flavoprotein AtHAL3a catalyzes the decarboxylation of 4'-Phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in coenzyme A biosynthesis. (8/116)

The Arabidopsis thaliana flavoprotein AtHAL3a is related to plant growth and salt and osmotic tolerance. AtHAL3a shows sequence homology to the bacterial flavoproteins EpiD and Dfp. EpiD, Dfp, and AtHAL3a are members of the homo-oligomeric flavin-containing Cys decarboxylase (HFCD) protein family. We demonstrate that AtHAL3a catalyzes the decarboxylation of (R)-4'-phospho-N-pantothenoylcysteine to 4'-phosphopantetheine. This key step in coenzyme A biosynthesis is catalyzed in bacteria by the Dfp proteins. Exchange of His-90 of AtHAL3a for Asn led to complete inactivation of the enzyme. Dfp and AtHAL3a are characterized by a shortened substrate binding clamp compared with EpiD. Exchange of the cysteine residue of the conserved ACGD motif of this binding clamp resulted in loss of (R)-4'-phospho-N-pantothenoylcysteine decarboxylase activity. Based on the crystal structures of EpiD H67N with bound substrate peptide and of AtHAL3a, we present a model for the binding of (R)-4'-phospho-N-pantothenoylcysteine to AtHAL3a.  (+info)

Pantetheine is not a medical term per se, but it is a biochemical compound with relevance to medicine. Pantetheine is the alcohol form of pantothenic acid (vitamin B5), and it plays a crucial role in the metabolism of proteins, carbohydrates, and fats. It is a component of coenzyme A, which is involved in numerous biochemical reactions within the body.

Coenzyme A, containing pantetheine, participates in oxidation-reduction reactions, energy production, and the synthesis of various compounds, such as fatty acids, cholesterol, steroid hormones, and neurotransmitters. Therefore, pantetheine is essential for maintaining proper cellular function and overall health.

While there isn't a specific medical condition associated with pantetheine deficiency, ensuring adequate intake of vitamin B5 (through diet or supplementation) is vital for optimal health and well-being.

Pantothenic Acid, also known as Vitamin B5, is a water-soluble vitamin that plays a vital role in the metabolism of proteins, carbohydrates, and fats. It is essential for the synthesis of coenzyme A (CoA), which is involved in various biochemical reactions in the body, including energy production, fatty acid synthesis, and cholesterol metabolism.

Pantothenic Acid is widely distributed in foods, including meat, poultry, fish, whole grains, legumes, and vegetables. Deficiency of this vitamin is rare but can lead to symptoms such as fatigue, irritability, sleep disturbances, muscle cramps, and gastrointestinal problems.

In addition to its role in metabolism, Pantothenic Acid also has potential benefits for wound healing, reducing inflammation, and supporting the immune system.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

Tyrothricin is not typically considered a medical term, but it is a chemical compound with some medical applications. Medically, tyrothricin is often referred to as a polypeptide antibiotic, which is derived from the gram-positive bacteria Bacillus brevis. It is a complex mixture of several chemically related polypeptides, including tyrocidine and gramicidin. Tyrothricin has broad-spectrum antimicrobial activity against many gram-positive and gram-negative bacteria, as well as some fungi and viruses. However, its clinical use is limited due to its potential toxicity and the availability of safer and more effective antibiotics.

Cysteamine is a medication and a naturally occurring aminothiol compound, which is composed of the amino acid cysteine and a sulfhydryl group. It has various uses in medicine, including as a treatment for cystinosis, a rare genetic disorder that causes an accumulation of cystine crystals in various organs and tissues. Cysteamine works by reacting with cystine to form a compound that can be more easily eliminated from the body. It is available in oral and topical forms and may also be used for other indications, such as treating lung diseases and radiation-induced damage.

Acetyl Coenzyme A, often abbreviated as Acetyl-CoA, is a key molecule in metabolism, particularly in the breakdown and oxidation of carbohydrates, fats, and proteins to produce energy. It is a coenzyme that plays a central role in the cellular process of transforming the energy stored in the chemical bonds of nutrients into a form that the cell can use.

Acetyl-CoA consists of an acetyl group (two carbon atoms) linked to coenzyme A, a complex organic molecule. This linkage is facilitated by an enzyme called acetyltransferase. Once formed, Acetyl-CoA can enter various metabolic pathways. In the citric acid cycle (also known as the Krebs cycle), Acetyl-CoA is further oxidized to release energy in the form of ATP, NADH, and FADH2, which are used in other cellular processes. Additionally, Acetyl-CoA is involved in the biosynthesis of fatty acids, cholesterol, and certain amino acids.

In summary, Acetyl Coenzyme A is a vital molecule in metabolism that connects various biochemical pathways for energy production and biosynthesis.

Fatty acid synthases (FAS) are a group of enzymes that are responsible for the synthesis of fatty acids in the body. They catalyze a series of reactions that convert acetyl-CoA and malonyl-CoA into longer chain fatty acids, which are then used for various purposes such as energy storage or membrane formation.

The human genome encodes two types of FAS: type I and type II. Type I FAS is a large multifunctional enzyme complex found in the cytoplasm of cells, while type II FAS consists of individual enzymes located in the mitochondria. Both types of FAS play important roles in lipid metabolism, but their regulation and expression differ depending on the tissue and physiological conditions.

Inhibition of FAS has been explored as a potential therapeutic strategy for various diseases, including cancer, obesity, and metabolic disorders. However, more research is needed to fully understand the complex mechanisms regulating FAS activity and its role in human health and disease.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

Nutrition policy refers to a set of guidelines, regulations, or laws established by governmental or organizational bodies to promote healthy eating habits and reduce the risk of diet-related chronic diseases. These policies aim to create an environment that supports and encourages individuals to make healthier food choices. Nutrition policies can cover various aspects such as food labeling, nutrition education, food safety, agricultural practices, and access to affordable and nutritious foods. They may also address issues related to marketing and advertising of unhealthy food products, particularly to children. The ultimate goal of nutrition policy is to improve public health by creating a food environment that supports optimal nutrition and well-being.

Nutritional requirements refer to the necessary amount of nutrients, including macronutrients (carbohydrates, proteins, and fats) and micronutrients (vitamins and minerals), that an individual requires to maintain good health, support normal growth and development, and promote optimal bodily functions. These requirements vary based on factors such as age, sex, body size, pregnancy status, and physical activity level. Meeting one's nutritional requirements typically involves consuming a balanced and varied diet, with additional consideration given to any specific dietary restrictions or medical conditions that may influence nutrient needs.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Recommended Dietary Allowances (RDAs) are the average daily levels of nutrients that are sufficient to meet the nutrient requirements of nearly all (97-98%) healthy individuals in a specific life stage and gender group. They are considered as the gold standard for establishing nutrient intake recommendations and are used as a benchmark for planning and assessing the nutrient intakes of individuals and populations. The RDAs are established by the Food and Nutrition Board of the National Academies of Sciences, Engineering, and Medicine in the United States. They represent the minimum daily amounts of various nutrients that are necessary to prevent deficiencies and maintain good health.

"Fortified food" is a term used in the context of nutrition and dietary guidelines. It refers to a food product that has had nutrients added to it during manufacturing to enhance its nutritional value. These added nutrients can include vitamins, minerals, proteins, or other beneficial components. The goal of fortifying foods is often to address specific nutrient deficiencies in populations or to improve the overall nutritional quality of a food product. Examples of fortified foods include certain breakfast cereals that have added vitamins and minerals, as well as plant-based milk alternatives that are fortified with calcium and vitamin D to mimic the nutritional profile of cow's milk. It is important to note that while fortified foods can be a valuable source of essential nutrients, they should not replace whole, unprocessed foods in a balanced diet.

... is an intermediate in the production of coenzyme A by the body. MB Hoagland, GD Novelli (1954). "Biosynthesis of ... Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). The dimer of this compound, pantethine is more ... coenzyme A from phosphopantetheine and of pantetheine from pantothenate". Journal of Biological Chemistry. 207 (2): 767-773. ...
In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction (R)-pantetheine + H2O ... The systematic name of this enzyme class is (R)-pantetheine amidohydrolase. Other names in common use include pantetheinase, ... pantetheine and H2O, whereas its two products are (R)-pantothenate and 2-aminoethanethiol. This enzyme belongs to the family of ...
In enzymology, a pantetheine kinase (EC 2.7.1.34) is an enzyme that catalyzes the chemical reaction ATP + pantetheine ⇌ {\ ... The systematic name of this enzyme class is ATP:pantetheine 4'-phosphotransferase. This enzyme is also called pantetheine ... the two substrates of this enzyme are ATP and pantetheine, whereas its two products are ADP and pantetheine 4'-phosphate. This ...
HOAGLAND MB, NOVELLI GD (1954). "Biosynthesis of coenzyme A from phospho-pantetheine and of pantetheine from pantothenate". J. ... pantetheine-4'-phosphate adenylyltransferase. Other names in common use include dephospho-CoA pyrophosphorylase, pantetheine ... In enzymology, a pantetheine-phosphate adenylyltransferase (EC 2.7.7.3) is an enzyme that catalyzes the chemical reaction ATP ... purification of pantetheine phosphate adenylyltransferase". Biochem. Biophys. Res. Commun. 192 (3): 1155-61. doi:10.1006/bbrc. ...
Pantetheinase, an intestinal enzyme, then hydrolyzes pantetheine into free pantothenic acid. Free pantothenic acid is absorbed ... The 4'-phosphopantetheine is then dephosphorylated into pantetheine. ...
The systematic name of this enzyme class is N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase (pantetheine-forming). Other names in ... Brown GM (June 1957). "Pantothenylcysteine, a precursor of pantetheine in Lactobacillus helveticus". The Journal of Biological ... pantetheine + CO2 This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon ...
Schweizer E, Kniep B, Castorph H, Holzner U (1973). "Pantetheine-free mutants of the yeast fatty-acid-synthetase complex". Eur ...
... is two molecules of pantetheine linked by a disulfide bridge. Pantetheine is an intermediate in the production of ... Pantethine (bis-pantethine or co-enzyme pantethine) is a dimeric form of pantetheine, which is produced from pantothenic acid ( ... In the second theory, pantethine is converted to two pantetheine molecules which are in turn metabolized to form two ...
The systematic name is holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. Other names in common use include ACP ... hydrolyase, ACP phosphodiesterase, AcpH, and [acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. This enzyme participates ...
"Biosynthesis of coenzyme A from phospho-pantetheine and of pantetheine from pantothenate". J. Biol. Chem. 207 (2): 767-73. PMID ... pantetheine-4'-phosphate adenylyltransferase, EC 2.7.7.3 and ATP:dephospho-CoA-3'-phosphotransferase EC 2.7.1.24)". Methods ...
The encoded protein contains an AMP-binding domain, PP-binding (phosphopantetheine, or pantetheine 4'phosphate-binding) domain ...
Pantethine (a precursor of pantetheine) has been studied and shown to be effective in a mouse and in a fruit fly model of the ... and pantetheine (OMIM). Mutant PANK2 gene coded proteins are often caused by null or missense mutations most notably a 7bp ...
These thioesters are made by conjugating the fatty acid with the free SH group of the pantetheine moiety of either coenzyme A ( ...
The intermediate pantetheine is broken down into cysteamine and pantothenic acid. It is the biosynthetic precursor to the ...
The CoA thioester derivatives bind in a characteristic hooked shape and a conserved tunnel binds the pantetheine group of CoA, ...
... pantetheine MeSH D02.886.489.725 - s-nitrosothiols MeSH D02.886.489.725.500 - s-nitroso-n-acetylpenicillamine MeSH D02.886. ...
... pantetheine kinase EC 2.7.1.35: pyridoxal kinase EC 2.7.1.36: mevalonate kinase EC 2.7.1.37: now divided into EC 2.7.11.1, EC ... pantetheine-phosphate adenylyltransferase EC 2.7.7.4: sulfate adenylyltransferase EC 2.7.7.5: sulfate adenylyltransferase (ADP ...
To become functional, the 4'-phospho-pantetheine sidechain of acyl-CoA molecules has to be attached to the PCP-domain by 4'PP ... phospho-pantetheine (required in a module) C: Condensation forming the amide bond (required in a module) Cy: Cyclization into ...
... pantetheine hydrolase EC 3.5.1.93: glutaryl-7-aminocephalosporanic-acid acylase EC 3.5.1.94: γ-glutamyl-γ-aminobutyrate ...
... by an intramolecular hydrogen bond between N7 of the adenine ring and a hydroxyl group on the pantetheine tail. In addition, a ...
Pantetheine is an intermediate in the production of coenzyme A by the body. MB Hoagland, GD Novelli (1954). "Biosynthesis of ... Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). The dimer of this compound, pantethine is more ... coenzyme A from phosphopantetheine and of pantetheine from pantothenate". Journal of Biological Chemistry. 207 (2): 767-773. ...
Vanin-1 (Pantetheinase, Pantetheine hydrolase, Tiff66, Vascular non-inflammatory molecule 1). 0 result found ... You are here: Home Products by Molecule of Interest Vanin-1 (Pantetheinase, Pantetheine hydrolase, Tiff66, Vascular non- ...
"Pantetheine" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Pantetheine" by people in this website by year, and whether " ... Below are the most recent publications written about "Pantetheine" by people in Profiles. ...
Pantetheine. C11H22N2O4S. ESI +. 2.5712. 279.1378. - ... pantetheine, l-cysteine, pantothenic acid, serotonin, l- ... pantetheine, l-cysteine, pantothenic acid, 4-(2-Aminophenyl)-2,4-dioxobutanoic acid, 3-indoleacetic acid, l-histidine, ...
Pantetheinase, an intestinal enzyme, then hydrolyzes pantetheine into free pantothenic acid.[29] Free pantothenic acid is ... The 4-phosphopantetheine is then dephosphorylated into pantetheine. ...
Conformational changes at the active site of pantetheine hydrolase during denaturation by guanidine hydrochloride. Pitari, G., ... The results indicate that the active site of pantetheine hydrolase is labile and unfolds under conditions in which no global ... Conformational changes at the active site of pantetheine hydrolase during denaturation by guanidine hydrochloride.. ... Conformational changes at the active site of pantetheine hydrolase (EC3.5.1.-) during guanidine hydrochloride (GndHCl) ...
Wu, J. and Zheng, Y. G. (2010) Synthesis of H4 pantetheine adducts for histone acetyltransferase inhibition. Heterocycl Commun ...
Pantetheine. To figure out where it went wrong, Sibon followed the route that that vitamin B5 makes while turning into coenzyme ... However, pantetheine, a similar molecule that doesnt appear in the route from vitamin B5 to coenzyme A, is easier to make. ... He was on sabbatical in the Netherlands in 2015 and he told me that bacteria were really good at living of off pantetheine. ... They use the molecule as a control test: if everything is working as it should, using pantetheine will not result in the ...
... a derivative of pantetheine, an essential part of the acetylation coenzyme CoA, administered P.O., in normalizing the blood ...
Aqua, glycerin, ammonium polyacrydimethyltauramide, benzyl alcohol, calcium pantetheine sulfonate, cetyl alcohol, citric acid, ...
PANK4 hydrolyzes PPANT to pantetheine (Bos taurus) * H2O [cytosol] * Vitamin B6 activation to pyridoxal phosphate (Bos taurus) ...
Journal Article] Structural Characterization of Complex of Adenylation Domain and Carrier Protein by Using Pantetheine Cross- ...
keywords = "Drosophila, PKAN, acetyl-CoA, coenzyme A, maternal contribution, metabolism, microbiome, pantetheine, pantothenate ...
Henna is a natural dye obtained by processing the leaves of the Lawsonia shrub. This natural dye, unlike chemical dyes, does not harm the hair, moreover, it is an effective remedy. Hair does not fade in the sun at all and does not deteriorate from sea water. It should be noted that henna also has a healing effect on the hair follicle, so the hair begins to grow faster. Indian henna has an exceptional ability to paint over gray hair perfectly. When applied to gray hair, lighter henna tones, such as light chestnut or burgundy, produce an interesting coloring effect. After dyeing, as the hair grows, it is enough to tint the growing roots, and refresh the color along the entire length every six ...
64. PANTETHEINE [ՊԱՆՏԵՏԵԻՆ] 15. PAKISTAN [ՊԱԿԻՍՏԱՆ] 65. PANTOTHENIC ACID [ՊԱՆՏՈԹԵՆԱԹԹՈՒ] 16. PALATAL EXPANSION TECHNIQUE [ՔԻՄՔ ...
Pantetheine Sulfonate. *PEG-7 Glyceryl Cocoate. *PEG-12 Dimethicone. *Polyquaternium-10. *Citric Acid ...
CALCIUM PANTETHEINE SULFONATE • ACETYL TRIFLUOROMETHYLPHENYL VALYLGLYCINE • HYDROXYPROPYL TETRAHYDROPYRANTRIOL • PISUM SATIVUM ...
calcium pantetheine sulfonate. *glyceryl stearate. *prunus amygdalus dulcis (sweet almond) oil. *ammonium ...
ec 2.7.7.3: Pantetheine-phosphate adenylyltransferase. pdb deposition date 2010-01-04. ...
Calcium Pantetheine Sulfonate • Menthol • Paeonia Albiflora Root Extract • Pentaerythrityl Tetra-di-t-butyl ...
CALCIUM PANTETHEINE SULFONATE • MENTHOL • PAEONIA ALBIFLORA ROOT EXTRACT • PENTAERYTHRITYL TETRA-DI-T-BUTYL ...
Calcium Pantetheine Sulfonate • Magnesium Gluconate • Pentaerythrityl Tetra-di-t-butyl Hydroxyhydrocinnamate • Sodium Hydroxide ... Calcium Pantetheine Sulfonate • Magnesium Gluconate • Pentaerythrityl Tetra-di-t-butyl Hydroxyhydrocinnamate • Sodium Hydroxide ...
pantetheine-phosphate adenylyltransferase (NCBI). 143, 204. GSU1260. GSU1260. ABC transporter, permease protein (NCBI). 144, ...
ID: GO:0008441 Type: http://bio2vec.net/ontology/gene_function Label: 3\(2\),5\-bisphosphate nucleotidase activity Synonyms: 3\(2\), 5\-bisphosphate nucleotidase activity Alternative IDs: als API: GO SPARQL: GO ...
... researchers managed to preserve the FAS phospho-pantetheine transferase domain, known to otherwise denature during ...
Pantethine is the disulfide dimer of pantetheine. The 4-phosphate derivative of pantetheine is a step in the formation of ...
Some of the alkaloids include pantetheine and mitragynine. During a kratom high, you will experience a peak period that lasts ...
Pantetheinase, an intestinal enzyme, then hydrolyzes pantetheine into free pantothenic acid. Free pantothenic acid is absorbed ... The 4-phosphopantetheine is then dephosphorylated into pantetheine. ...
Pantetheine is the most active form of vitamin B5, pantothenic acid. Pantethine is involved in hundreds of processes within the ...
  • Cyclohexasiloxane - Hydrolyzed Soy Protein - Isohexadecane - Jasminum Officinale Extract / Jasmine Flower Extract - Mel / Honey - Calcium Pantetheine Sulfonate - Cetearyl Ethylhexanoate - Caffeine - Cholesterol - Ammonium Polyacryldimethyltauramide / Ammonium Polyacryloyldimethyl Taurate - Disodium Edta - Isopropyl Myristate - Hydrogenated Polyisobutene - Hydroxypalmitoyl Sphinganine - Caprylyl Glycol - Biosaccharide Gum-1 - Pentylene Glycol - Phenoxyethanol - Linalool - Geraniol - Eugenol - Coumarin - Limonene - Citral - Citronellol - Benzyl Alcohol - Parfum / Fragrance. (brands.co.nz)
  • Recent investigations have confirmed the effectiveness and the excellent tolerability of pantethine, a derivative of pantetheine, an essential part of the acetylation coenzyme CoA, administered P.O., in normalizing the blood lipid concentrations of patients with hyperlipidemias. (wellnessresources.com)
  • The 4'-phosphate derivative of pantetheine is a step in the formation of coenzyme A from pantothenic acid (vitamin B5). (healthure.com)
  • Pantetheine is an intermediate in the production of coenzyme A by the body. (wikipedia.org)
  • However, pantetheine, a similar molecule that doesn't appear in the route from vitamin B5 to coenzyme A, is easier to make. (ukrant.nl)
  • They use the molecule as a control test: if everything is working as it should, using pantetheine will not result in the creation of coenzyme A. (ukrant.nl)
  • But to Sibon's surprise, the control test was positive: against all expectations, the fruit flies were using the pantetheine to make coenzyme A. (ukrant.nl)
  • It worked: the flies without gut bacteria were no longer able to transform pantetheine into coenzyme A, thus confirming the link between those bacteria and the production of coenzyme A. (ukrant.nl)
  • Pantetheine-phosphate adenylyltransferase. (edu.pl)
  • Pantethine is the disulfide dimer of pantetheine. (healthure.com)
  • Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). (wikipedia.org)
  • Pantetheine is the most active form of vitamin B5, pantothenic acid. (aordistribution.co.uk)
  • Objective: Vanin1 (VNN1) is a pantetheinase that can catalyze the hydrolysis of pantetheine to produce pantothenic acid and cysteamine. (koreascience.kr)
  • Each 1/2 teaspoon supplies high energy, end-chain vitamin B forms (the form ready to use by the cell) including vitamin B6 as pyridoxal, pyridoxine, pyridoxamine, vitamin B5 as pantetheine (and more), folic acid as 5-MTHF and 5-FTHF and much more. (newhopehealth.com)
  • Some of the alkaloids include pantetheine and mitragynine. (fbspost.com)
  • Red Vein Maeng Da Kratom The alkaloids in Red Vein Maeng Da are quite unique and include high levels of Pantetheine and 7-Hydroxy Mitragynine. (littleamsterdamheadshop.com)
  • If it does, we might develop pantetheine into an affordable treatment for PKAN and similar diseases. (ukrant.nl)
  • This graph shows the total number of publications written about "Pantetheine" by people in this website by year, and whether "Pantetheine" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "Pantetheine" by people in Profiles. (uchicago.edu)
  • A follow-up study will have to prove whether administering pantetheine to people will have the same effect. (ukrant.nl)
  • Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). (wikipedia.org)
  • Pantetheine, the dephosphorylated form of phosphopantetheine, however, is first taken up by intestinal cells and converted to pantothenic acid before being delivered into the bloodstream [ 2 ]. (nih.gov)
  • Pantetheinase ( EC 3.5.1.92 ) (Pantetheine hydrolase) (Vanin), which hydrolyzes specifically one of the carboamide linkages in D-pantetheine, thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. (embl.de)
  • The 4'-phosphate derivative of pantetheine is a step in the formation of coenzyme A from pantothenic acid (vitamin B5). (healthure.com)
  • Vanins are enzymes with pantetheinase activity and are presumed to play a role in the recycling of pantothenic acid (vitamin B5) from pantetheine. (ru.nl)
  • Vanin1 (VNN1) is a pantetheinase that can catalyze the hydrolysis of pantetheine to produce pantothenic acid and cysteamine. (animbiosci.org)
  • VNN1 can catalyze the hydrolysis of pantetheine to produce pantothenic acid (vitamin B 5 ) and cysteamine (a highly effective antioxidant) [ 1 ]. (animbiosci.org)
  • Hydrolysis of pantetheine also liberates cysteamine, a known antioxidant. (ru.nl)
  • This is a regulatory enzyme involved in the production of coenzyme A by acting as a catalyst for the phosphorylation of pantothenate (vitamin B5), N-pantothenyl-cystine, and pantetheine. (medscape.com)
  • Pantethine then reacts with ATP and the enzyme pantetheine kinase to form CoA, which is the end product. (coalitionbrewing.com)
  • We hereby report the design, synthesis, and characterization of a novel pantetheine analogue, RR6, that acts as a selective, reversible, and competitive vanin inhibitor at nanomolar concentration. (ru.nl)
  • Pantethine is the disulfide dimer of pantetheine. (healthure.com)