An enzyme that hydrolyzes thiamine pyrophosphate to thiamine monophosphate plus inorganic phosphate. EC 3.6.1.-.
A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-.
3-((4-Amino-2-methyl-5-pyrimidinyl)methyl)-5-(2- hydroxyethyl)-4-methylthiazolium chloride.
An enzyme which catalyzes the hydrolysis of diphosphate (DIPHOSPHATES) into inorganic phosphate. The hydrolysis of pyrophosphate is coupled to the transport of HYDROGEN IONS across a membrane.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
Thiamine dihydrogen phosphate ester. The monophosphate ester of thiamine. Synonyms: monophosphothiamine; vitamin B1 monophosphate.
Inorganic salts of phosphoric acid that contain two phosphate groups.

Molecular cloning and expression of a mouse thiamin pyrophosphokinase cDNA. (1/46)

Thiamin pyrophosphokinase (EC 2.7.6.2) catalyzes the pyrophosphorylation of thiamin with adenosine 5'-triphosphate to form thiamin pyrophosphate. A mouse thiamin pyrophosphokinase cDNA clone (mTPK1) was isolated using a combination of mouse expressed sequence tag database analysis, a two-step polymerase chain reaction procedure, and functional complementation screening with a Saccharomyces cerevisiae thiamin pyrophosphokinase-deficient mutant (thi80). The predicted protein contained 243 amino acid residues with a calculated molecular weight of 27,068. When the intact mTPK1 open reading frame was expressed as a glutathione S-transferase fusion protein in Escherichia coli lacking thiamin pyrophosphokinase, marked enzyme activity was detected in the bacterial cells. The corresponding 2.5-kilobase pair mRNA was expressed in a tissue-dependent manner and was found at relatively high levels in the kidney and liver, indicating that the mode of expression of mTPK1 genes differs with cell type. The expression of mTPK1 genes in cultured mouse neuroblastoma and normal liver cells was unaffected by the thiamin concentration in the medium (10 microM versus 3.0 nM). This is the first report on identification of the primary sequence for mammalian thiamin pyrophosphokinase.  (+info)

Leigh's disease: significance of the biochemical changes in brain. (2/46)

Analysis of five brains from patients with Leigh's disease demonstrates an accumulation of thiamine pyrophosphate and a deficiency of thiamine triphosphate. The enzyme which converts thiamine pyrophosphate to thiamine triphosphate was normally active in two of these brains, suggesting that the inhibitor found in Leigh's disease is probably producing the observed neurochemical changes. Reasons for the histological similarity between Leigh's and Wernicke's diseases are suggested.  (+info)

Cytochemical and stereological analysis of rat cortical astrocytes during development in primary culture. Effect of prenatal exposure to ethanol. (3/46)

This study has investigated the effect of prenatal alcohol exposure on the qualitative and quantitative ultrastructure of proliferating and differentiated astrocytes in primary cultures as well as on the cytochemical activity of several subcellular phosphatase markers, including acid phosphatase, uridine diphosphatase, thiamine pyrophosphatase, 5'-nucleotidase and glucose-6-phosphatase. The astrocytes were obtained from 21-day-fetuses of both control and alcohol-fed rats. Our results show that several cell components, such as mitochondria, rough endoplasmic reticulum and lysosomes, exhibit qualitative and/or quantitative ultrastructural changes during the process of astrocyte maturation. In some cases these morphological changes are accompanied by variations in the cytochemical activity of enzymes located in these and other cell components, suggesting that these enzymes, and therefore the functional state of these organelles, are modulated during astrocyte development. When prenatally exposed to ethanol, both proliferating and differentiated astrocytes showed striking ultrastructural alterations compared with controls, including an increment of lysosomes as well as a decrease in the values of stereological parameters relative to mitochondria, rough endoplasmic reticulum and Golgi apparatus. Cytochemical analysis of these cells indicates that prenatal exposure to ethanol decreased the activities of all the enzymes tested, except for acid phosphatase, which was increased in both groups of treated astrocytes. These results suggest that prenatal exposure to ethanol could affect astrocytes during development in two different but probably complementary ways: a) by causing a delay in astrocyte maturation and, b) by inducing a direct toxic effect on these cells.  (+info)

Ultracytochemical studies on Trichomonas hominis. (4/46)

The results of ultracytochemical studies on Trichomonas hominis showed that ACPase and CMPase were mainly located in the mature face sacs of the primary lysosomes, digestive vacuoles, as well as in the parabasal body. TPPase and NADPase were found in the saccules at the mature face and the intermediate saccules of parabasal body respectively. This study revealed that T. hominis had well-developed parabasal bodies. Negative COase and catalase reactions indicated that T. hominis lacked both mitochondria and microbody. Hydrogenosome was stained well with the Ur-Pb-Cu impregnation technique.  (+info)

Structural and histochemical studies of Golgi complex differentiation in salivary gland cells during Drosophila development. (5/46)

Morphological alterations in the Golgi complex (GC) and changes in the distribution of acid phosphatase (AcPase), thiamine pyrophosphatase (TPPase), complex carbohydrates and reduced osmium tetroxide compounds in this organelle were studied in the salivary gland cells of Drosophila during larval and prepupal development. The morphology and the AcPase, TPPase and complex carbohydrates cytochemical patterns of the Golgi complex varied characteristically during cell differentiation. At the early 3rd instar period the Golgi complex consisted mainly of vesiculated cisternae, and AcPase activity was observed in all cisternae but not in the secretory granules. As development proceeded to the late 3rd instar the Golgi complex displayed its typical appearance, consisting of four to six cisternae, and only the two to three cisternae towards the trans-face as well as the trans-Golgi network and some of the immature secretory granules exhibited AcPase reactivity. In the course of a 'wave' of production of the 'glue' secretory granules proceeding proximally through the gland, the number of AcPase positive cisternae changed correspondingly. After secretion of the 'glue' secretory granules, the size of the Golgi complex decreased and almost all cisternae displayed AcPase reactivity. The detection of TPPase activity presented some specificity problems, since staining was observed not only in the GC cisternae but in the endoplasmic reticulum (ER) and microvilli. The reaction products were seen in a few GC vesicles during the early 3rd instar and in the trans side of the organelle at the end of the 3rd instar. During production of the secretory granules, every GC cisterna was intensely stained. These results agree with previous findings suggesting that AcPase and TPPase in secretory cells may be primarily involved in the processing of exportable proteins. The vicinal (vic)-glycol groups of the complex carbohydrates were detected using the periodic acid/thiocarbohydrazide/silver proteinate (PA-TCH-SP) technique. During synthesis of the 'glue' secretory granules, the reaction products were observed over the GC cisternae and the trans-Golgi network, with increasing intensity from the cis to the trans side of the organelle. No PA-TCH-SP staining was observed over the GC cisternae during the early 3rd instar. Following discharge of the 'glue' secretory granules, all GC cisternae displayed uniform PA-TCH-SP staining. After OsO4 impregnation, the reaction products were observed mainly in ER and mitochondria and rarely in the GC. In numerous cells, only the mitochondria were stained, while in many cases the ER of neighboring cells exhibited differential staining.(ABSTRACT TRUNCATED AT 400 WORDS)  (+info)

Mutational analysis of ThiH, a member of the radical S-adenosylmethionine (AdoMet) protein superfamily. (6/46)

Thiamine pyrophosphate (TPP) is an essential cofactor for all forms of life. In Salmonella enterica, the thiH gene product is required for the synthesis of the 4-methyl-5-beta hydroxyethyl-thiazole monophosphate moiety of TPP. ThiH is a member of the radical S-adenosylmethionine (AdoMet) superfamily of proteins that is characterized by the presence of oxygen labile [Fe-S] clusters. Lack of an in vitro activity assay for ThiH has hampered the analysis of this interesting enzyme. We circumvented this problem by using an in vivo activity assay for ThiH. Random and directed mutagenesis of the thiH gene was performed. Analysis of auxotrophic thiH mutants defined two classes, those that required thiazole to make TPP (null mutants) and those with thiamine auxotrophy that was corrected by either L-tyrosine or thiazole (ThiH* mutants). Increased levels of AdoMet also corrected the thiamine requirement of members of the latter class. Residues required for in vivo function were identified and are discussed in the context of structures available for AdoMet enzymes.  (+info)

Retinol stimulates Golgi apparatus activity in cultured bovine mammary gland epithelial cells. (7/46)

Biochemical and electron microscopic studies have indicated that the Golgi apparatus responds to retinol. The purpose of this investigation was to visualize and record with living cells the rapidity of the response to retinol. A rapid response of the Golgi apparatus to retinol (1.75-17.5 mumol/L) added to the culture medium was observed using video-enhanced light microscopy with bovine mammary epithelial cells. The response was manifested within 1 min as a marked movement of membranes within the Golgi apparatus zone. In subsequent electron microscope preparations of the cells, only minor changes were observed and were restricted to increased numbers of normal-appearing membranes and vesicles associated with the trans Golgi apparatus face of the retinol-treated cells.  (+info)

Cytochemical study of secretory process in transplantable insulinoma of syrian golden hamster. (8/46)

Electron microscopy, including phosphatase cytochemistry, indicates that the secretory granules of an insulinoma producing proinsulin and insulin are packaged by the endoplasmic reticulum (ER) and especially by a specialized region of ER which we call GERL because of the spatial relationship of this region to the Golgi apparatus and its apparent role in producing lysosomes. The granules are not derived from the Golgi apparatus. Preliminary evidence suggests this may be true also of pancreatic beta-cells.  (+info)

Thiamine pyrophosphatase (TPP) is an enzyme that catalyzes the hydrolysis of thiamine pyrophosphate (TPP), which is a cofactor involved in several important metabolic pathways, including carbohydrate metabolism and neurotransmitter synthesis.

The reaction catalyzed by TPP is:

thiamine pyrophosphate + H2O → thiamine + phosphate

TPP is also known as thiamine diphosphatase or vitamin B1 diphosphatase. Deficiency of this enzyme can lead to thiamine deficiency disorders such as beriberi and Wernicke-Korsakoff syndrome, which are characterized by neurological and cardiovascular symptoms.

Pyrophosphatases are enzymes that catalyze the hydrolysis or cleavage of pyrophosphate (PPi) into two inorganic phosphate (Pi) molecules. This reaction is essential for many biochemical processes, such as energy metabolism and biosynthesis pathways, where pyrophosphate is generated as a byproduct. By removing the pyrophosphate, pyrophosphatases help drive these reactions forward and maintain the thermodynamic equilibrium.

There are several types of pyrophosphatases found in various organisms and cellular compartments, including:

1. Inorganic Pyrophosphatase (PPiase): This enzyme is widely distributed across all kingdoms of life and is responsible for hydrolyzing inorganic pyrophosphate into two phosphates. It plays a crucial role in maintaining the cellular energy balance by ensuring that the reverse reaction, the formation of pyrophosphate from two phosphates, does not occur spontaneously.
2. Nucleotide Pyrophosphatases: These enzymes hydrolyze the pyrophosphate bond in nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs), converting them into nucleoside monophosphates (NMPs) or deoxynucleoside monophosphates (dNMPs). This reaction is important for regulating the levels of NTPs and dNTPs in cells, which are necessary for DNA and RNA synthesis.
3. ATPases and GTPases: These enzymes belong to a larger family of P-loop NTPases that use the energy released from pyrophosphate bond hydrolysis to perform mechanical work or transport ions across membranes. Examples include the F1F0-ATP synthase, which synthesizes ATP using a proton gradient, and various molecular motors like myosin, kinesin, and dynein, which move along cytoskeletal filaments.

Overall, pyrophosphatases are essential for maintaining cellular homeostasis by regulating the levels of nucleotides and providing energy for various cellular processes.

Thiamine, also known as vitamin B1, is a water-soluble vitamin that plays a crucial role in certain metabolic reactions, particularly in the conversion of carbohydrates into energy in the body. It is essential for the proper functioning of the heart, nerves, and digestive system. Thiamine acts as a cofactor for enzymes involved in the synthesis of neurotransmitters and the metabolism of carbohydrates, lipids, and proteins. Deficiency in thiamine can lead to serious health complications, such as beriberi (a disease characterized by peripheral neuropathy, muscle wasting, and heart failure) and Wernicke-Korsakoff syndrome (a neurological disorder often seen in alcoholics due to chronic thiamine deficiency). Thiamine is found in various foods, including whole grains, legumes, pork, beef, and fortified foods.

Inorganic pyrophosphatase (IPP) is an enzyme that catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into two orthophosphate ions (Pi). The reaction it catalyzes is as follows:

PPi + H2O → 2Pi

Inorganic pyrophosphatase plays a crucial role in various biological processes, such as DNA replication, protein synthesis, and the formation of ATP. By breaking down PPi into Pi, IPP helps to drive these reactions forward by removing an inhibitory product (PPi) and providing a substrate (Pi) for other enzymatic reactions.

The medical relevance of inorganic pyrophosphatase is linked to certain genetic disorders, such as hyperphosphatasia with mental retardation syndrome 2 (HPMRS2), which is caused by mutations in the gene encoding the IPP enzyme. These mutations can lead to reduced IPP activity, resulting in an accumulation of PPi and impaired cellular functions, ultimately manifesting as developmental delays, intellectual disability, seizures, and skeletal abnormalities.

Acid phosphatase is a type of enzyme that is found in various tissues and organs throughout the body, including the prostate gland, red blood cells, bone, liver, spleen, and kidneys. This enzyme plays a role in several biological processes, such as bone metabolism and the breakdown of molecules like nucleotides and proteins.

Acid phosphatase is classified based on its optimum pH level for activity. Acid phosphatases have an optimal activity at acidic pH levels (below 7.0), while alkaline phosphatases have an optimal activity at basic or alkaline pH levels (above 7.0).

In clinical settings, measuring the level of acid phosphatase in the blood can be useful as a tumor marker for prostate cancer. Elevated acid phosphatase levels may indicate the presence of metastatic prostate cancer or disease progression. However, it is important to note that acid phosphatase is not specific to prostate cancer and can also be elevated in other conditions, such as bone diseases, liver disorders, and some benign conditions. Therefore, acid phosphatase should be interpreted in conjunction with other diagnostic tests and clinical findings for a more accurate diagnosis.

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

Histochemistry is the branch of pathology that deals with the microscopic localization of cellular or tissue components using specific chemical reactions. It involves the application of chemical techniques to identify and locate specific biomolecules within tissues, cells, and subcellular structures. This is achieved through the use of various staining methods that react with specific antigens or enzymes in the sample, allowing for their visualization under a microscope. Histochemistry is widely used in diagnostic pathology to identify different types of tissues, cells, and structures, as well as in research to study cellular and molecular processes in health and disease.

Phosphoric monoester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric monoesters into alcohol and phosphate. This class of enzymes includes several specific enzymes, such as phosphatases and nucleotidases, which play important roles in various biological processes, including metabolism, signal transduction, and regulation of cellular processes.

Phosphoric monoester hydrolases are classified under the EC number 3.1.3 by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The enzymes in this class share a common mechanism of action, which involves the nucleophilic attack on the phosphorus atom of the substrate by a serine or cysteine residue in the active site of the enzyme. This results in the formation of a covalent intermediate, which is then hydrolyzed to release the products.

Phosphoric monoester hydrolases are important therapeutic targets for the development of drugs that can modulate their activity. For example, inhibitors of phosphoric monoester hydrolases have been developed as potential treatments for various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Thiamine pyrophosphate (TPP) is the active form of thiamine (vitamin B1) that plays a crucial role as a cofactor in various enzymatic reactions, particularly in carbohydrate metabolism. TPP is essential for the functioning of three key enzymes: pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase. These enzymes are involved in critical processes such as the conversion of pyruvate to acetyl-CoA, the oxidative decarboxylation of alpha-ketoglutarate in the Krebs cycle, and the pentose phosphate pathway, which is important for generating reducing equivalents (NADPH) and ribose sugars for nucleotide synthesis. A deficiency in thiamine or TPP can lead to severe neurological disorders, including beriberi and Wernicke-Korsakoff syndrome, which are often observed in alcoholics due to poor nutrition and impaired thiamine absorption.

Lysosomes are membrane-bound organelles found in the cytoplasm of eukaryotic cells. They are responsible for breaking down and recycling various materials, such as waste products, foreign substances, and damaged cellular components, through a process called autophagy or phagocytosis. Lysosomes contain hydrolytic enzymes that can break down biomolecules like proteins, nucleic acids, lipids, and carbohydrates into their basic building blocks, which can then be reused by the cell. They play a crucial role in maintaining cellular homeostasis and are often referred to as the "garbage disposal system" of the cell.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

Thiamine monophosphate (TMP) is a biochemical compound that is a derivative of thiamine (vitamin B1). It is a cofactor for several enzymes involved in key metabolic processes, particularly in the conversion of carbohydrates into energy. TMP plays an essential role in the metabolism of carbohydrates, amino acids, and neurotransmitters.

Thiamine monophosphate is formed when thiamine undergoes phosphorylation by the enzyme thiamine pyrophosphokinase. This reaction adds a phosphate group to the thiamine molecule, resulting in the formation of TMP. Thiamine monophosphate can then be further phosphorylated to form thiamine triphosphate (TTP) or dephosphorylated back to thiamine.

Deficiency in thiamine and its derivatives, including TMP, can lead to several medical conditions, such as beriberi, Wernicke-Korsakoff syndrome, and other neurological disorders. These conditions are often associated with impaired energy metabolism, nerve damage, and cognitive decline. Proper intake of thiamine through diet or supplementation is crucial for maintaining normal physiological functions and preventing these health issues.

Diphosphates, also known as pyrophosphates, are chemical compounds that contain two phosphate groups joined together by an oxygen atom. The general formula for a diphosphate is P~PO3~2-, where ~ represents a bond. Diphosphates play important roles in various biological processes, such as energy metabolism and cell signaling. In the context of nutrition, diphosphates can be found in some foods, including milk and certain vegetables.

Thiamine+pyrophosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e ( ... Sano S, Matsuda Y, Nakagawa H (1988). "Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct ... Other names in common use include thiamine pyrophosphatase, UDPase, inosine diphosphatase, adenosine diphosphatase, IDPase, ...
... codistribution with thiamine pyrophosphatase in trans-Golgi cisternae". J. Cell Biol. 93 (1): 223-9. doi:10.1083/jcb.93.1.223. ...
When the thiamine pyrophosphatase (TPP) coenzyme is bound, the rates of phosphorylation by all four isozymes are drastically ...
Thiamine pyrophosphatase List of EC numbers (EC 3) § 3.6.1: In phosphorus-containing anhydrides Kukko-Kalske E, Heinonen J ( ... Examples include: Inorganic pyrophosphatase, which acts upon the free pyrophosphate ion Tobacco acid pyrophosphatase, which ... Pyrophosphatases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Articles ... Pyrophosphatases, also known as diphosphatases, are acid anhydride hydrolases that act upon diphosphate bonds. ...
... inorganic pyrophosphatase MeSH D08.811.277.040.600.800 - thiamine pyrophosphatase MeSH D08.811.277.040.850 - thiamin- ... thiamin pyrophosphokinase MeSH D08.811.913.696.310 - myosin type iii MeSH D08.811.913.696.445 - nucleotidyltransferases MeSH ...
This enzyme participates in purine metabolism and thiamine metabolism. As of late 2007, only one structure has been solved for ... Brightwell R, Tappel AL (1968). "Lysosomal acid pyrophosphatase and acid phosphatase". Arch. Biochem. Biophys. 124 (1): 333-43 ...
Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP) may function to raise extracellular PPi. From the standpoint of high ... phosphorylation Phosphate Phosphoric acid Phosphoric acids and phosphates RNA Sodium pyrophosphate Superphosphate Thiamine ... pyrophosphate Calcium pyrophosphate dihydrate deposition disease Catalysis DNA High energy phosphate Inorganic pyrophosphatase ...
Serganov, A; Polonskaia A; Phan AT; Breaker RR; Patel DJ (29 June 2006). "Structural basis for gene regulation by a thiamine ... These downstream genes transcribe fluoride sensitive enzymes such as enolase, pyrophosphatase, the presumed fluoride exporter ... Thore, S; Leibundgut M; Ban N (26 May 2006). "Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ... Previous research came across this question in elucidating the cofactor thiamine pyrophosphate (TPP) riboswitch. The TPP ...
From FMN to FAD is the function of magnesium-requiring FAD synthase; the reverse is accomplished by a pyrophosphatase. FAD ... Institute of Medicine (1998). "Riboflavin". Dietary Reference Intakes for Thiamin, Riboflavin, Niacin, Vitamin B6, Folate, ...
Thiamine+pyrophosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e ( ... Sano S, Matsuda Y, Nakagawa H (1988). "Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct ... Other names in common use include thiamine pyrophosphatase, UDPase, inosine diphosphatase, adenosine diphosphatase, IDPase, ...
Thiamin pyrophosphatase. Model: ic_1306. Reaction:. h2o_c + thmpp_c → h_c + pi_c + thmmp_c ...
thiamine-pyrophosphatase activity. Details: Catalysis of the reaction: TDP + H2O = TMP + phosphate. ...
Label: 2-hydroxy-adenosine triphosphate pyrophosphatase activity Synonyms: 2-hydroxy-adenosine triphosphate pyrophosphatase ...
The ductal cells also showed diffuse peroxidase and acid phosphatase, and Golgi-like thiamine pyrophosphatase activities. ...
Ca2+-reliant thiamine pyrophosphatase, and acidity phosphatase. The calpain-like proteins is normally regarded as connected ...
Pyrophosphatases. Inorganic Pyrophosphatase. Thiamine Pyrophosphatase. Thiamin-Triphosphatase. Ads by Google. Enter your search ...
Metabolite pi_c in iAM_Pv461. Phosphate.
do not confuse with THIAMINE PYROPHOSPHATASE; deficiency: coordinate THIAMINE PYROPHOSPHATE /defic (IM) with THIAMINE ... Pyrophosphate, Thiamine. Thiamine Diphosphate. Tree number(s):. D02.886.675.900.702. D03.383.129.708.900.702. D03.383.742.795. ... Thiamine Pyrophosphate - Preferred Concept UI. M0021323. Scope note. The coenzyme form of Vitamin B1 present in many animal ... Diphosphate de thiamine Entry term(s):. Berolase. Cocarboxylase. ...
Pyrophosphatases. Thiamin-Triphosphatase. Ads by Google. Enter your search terms. Web. reference.md. ...
pyrophosphatase activity. IEP. Enrichment. MF. GO:0016799. hydrolase activity, hydrolyzing N-glycosyl compounds. IEP. ... thiamine diphosphokinase activity. IEP. Enrichment. MF. GO:0004813. alanine-tRNA ligase activity. IEP. Enrichment. ...
Thiamine Triphosphatase (THTPA) ELISA Kit , Techni .... 531€. Details Thiamine-triphosphatase, THTPA ELISA Kit , Techniq .... ... Uridine diphosphate glucose pyrophosphatase, NUDT1 .... 531€. Details BPNT1 (3(2),5-bisphosphate nucleotidase 1, Bisp .... ...
Pyrophosphatase *Inorganic. *Thiamine. *Apyrase. *Thiamine-triphosphatase. 3.6.2. *Adenylylsulfatase. *Phosphoadenylylsulfatase ...
thiamine diphosphokinase activity. IEP. Enrichment. MF. GO:0005488. binding. IEP. Enrichment. MF. GO:0005524. ATP binding. IEP ... pyrophosphatase activity. IEP. Enrichment. MF. GO:0016491. oxidoreductase activity. IEP. Enrichment. MF. GO:0016614. ...
pyrophosphatase activity. IEP. Enrichment. MF. GO:0016491. oxidoreductase activity. IEP. Enrichment. MF. GO:0016614. ... thiamine pyrophosphate binding. IEP. Enrichment. BP. GO:0034220. ion transmembrane transport. IEP. Enrichment. ...
nuclear epithelial( therefore free coupling) isoforms are 16,000 thiamin, but their presynaptic polytene to Freiburg sub-family ... converted by a part in Ca2+ within the cleavage has to close of Cyclic AMP Response Element secretory pyrophosphatase( CREB) at ... spinal cascade assembles characterised by its domain at the Tyr 18 transcriptase in the LIR design by Src thiamin under ...
Pyrophosphatases [D08.811.277.040.600] * SAM Domain and HD Domain-Containing Protein 1 [D08.811.277.040.725] ... Thiamin-Triphosphatase [D08.811.277.040.850] * Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Carrier ...
","inorganic pyrophosphatase [Ensembl]. Inorganic pyrophosphatase [Interproscan].","protein_coding" "AAT48138","araH"," ... ","Xanthine/uracil/thiamine/ascorbate permease family protein [Ensembl]. Permease family [Interproscan].","protein_coding" " ... ATP pyrophosphatase subunit [Ensembl]. NAD synthase, GMP synthase C terminal domain, Glutamine amidotransferase class-I [ ... ","thiamine biosynthesis lipoprotein ApbE, putative [Ensembl]. Flavin transferase ApbE [Interproscan].","protein_coding" " ...
Poor thiamin and riboflavin status is common among women of childbearing age in rural and urban Cambodia. J Nutr. 2015 Mar. 145 ... The coenzymes are then hydrolyzed to riboflavin by pyrophosphatases and phosphatases in the upper intestine. [15] Primary ... Low serum vitamin B-12 and folate concentrations and low thiamin and riboflavin intakes are inversely associated with greater ...
Thiamine metabolism - Homo sapiens (human). kegg. hsa00790. Folate biosynthesis - Homo sapiens (human). ... pyrophosphatase activity. MF. IEA. GO:0046872. metal ion binding. BP. TAS. GO:0001501. skeletal system development. ...
... so is over health and unit until it constitutes the battlefield pyrophosphatase( P0), which in most patients does the Military ... program of the design to serve measure elements might delete the threshold and building complicating from the electric thiamine ...
Characterization of santalene synthases using an inorganic pyrophosphatase coupled colorimetric assay. Anal. Biochem. 547, 26- ... 1 g thiamine hydrochloride, 1 g pyridoxal hydrochloride, and 0.2 g p-aminobenzoic acid. The feed media (per L) contained 10 mL ...
Thiamine pyrophosphokinase. General function:. Involved in thiamine diphosphokinase activity. Specific function:. Essential ... NADH pyrophosphatase. General function:. Involved in hydrolase activity. Specific function:. NAD(+) + H(2)O = AMP + NMN. Gene ... ADP-ribose pyrophosphatase. General function:. Involved in hydrolase activity. Specific function:. ADP-ribose + H(2)O = AMP + D ... Has equal high activity toward ADP/ATP, GDP/GTP, and UDP/UTP and approximately 50% less toward CDP/CTP and thiamine ...
thiamine biosynthesis protein ThiC (NCBI). 26, 511. PA5132. PA5132. hypothetical protein (NCBI). 374, 511. ... ADP-ribose pyrophosphatase. cog/ cog. hydrolase activity. go/ molecular_function. Gene Info. Organism:. Pseudomonas aeruginosa ...
Utility of Whole Blood Thiamine Pyrophosphate Evaluation in TPK1-Related Diseases. Bugiardini E, Pope S, Feichtinger RG, Poole ... identification of prognostic factors in developmental and epileptic encephalopathy due to inosine triphosphate pyrophosphatase ...
Thiamine diphosphate forms a covalent bond between a carbon in the thiazole ring of thiamine diphosphate and the carbonyl ... In plants, PFP activity is confined to the cytosol [27] and plastids have an active pyrophosphatase, so PFP dephosphorylation ... Thiamine diphosphate forms a covalent bond between a carbon in the thiazole ring of thiamine diphosphate and the carbonyl ... Racker, E.; Haba, G.D.L.; Leder, I.G. Thiamine pyrophosphate, a coenzyme of transketolase. J. Am. Chem. Soc. 1953, 75, 1010- ...
Pyrophosphatase, Inorganic (Recombinant) • Shrimp Alkaline Phosphatase, Recombinant (rSAP) • SuperSAP Proteases • Proteinase K ...
THIAMIN DIPHOSPHATE, GLYCOLYSIS, MAGNESIUM, METAL-BINDING, OXIDOREDUCTASE, THIAMINE PYROPHOSPHATE 2d13:B (THR55) to (ALA123) ... CRYSTAL STRUCTURE OF PYROPHOSPHATASE FROM BACTEROIDES THETAIOTAOMICRON, ASP13ASN MUTANT COMPLEXED WITH CALCIUM AND PHOSPHATE , ... THIAMIN PYROPHOSPHATE, IRON-SULFUR CLUSTER, FERREDOXIN 3zdc:A (MET81) to (ASP142) STRUCTURE OF E. COLI EXOIX IN COMPLEX WITH ... THIAMINE PYROPHOSPHATE 3eya:D (ASN30) to (ALA100) STRUCTURAL BASIS FOR MEMBRANE BINDING AND CATALYTIC ACTIVATION OF THE ...
  • Xanthosine 5-triphosphate is an intermediate of the Purine metabolism pathway, a substrate of the enzymes dinucleoside tetraphosphatase (EC 3.6.1.17) and nucleoside-triphosphate pyrophosphatase (EC 3.6.1.19). (ecmdb.ca)
  • 44593) non-canonical purine NTP pyrophosphatase%2C rdgB%2FHAM1 family CP001857 CDS Arcpr_0054 44640. (go.jp)
  • The coenzymes are then hydrolyzed to riboflavin by pyrophosphatases and phosphatases in the upper intestine. (medscape.com)
  • This reaction is catalyzed by the enzyme fatty acyl-CoA synthetase and driven to completion by inorganic pyrophosphatase . (wikidoc.org)
  • An enzyme that hydrolyzes thiamine pyrophosphate to thiamine monophosphate plus inorganic phosphate. (bvsalud.org)
  • When interpreting lab results, consult with your doctor and pay attention to: Units (nmol/L vs. ng/mL) As B vitamins, thiamine pyrophosphate, or TPP, plays a vital role in healthy tissue respiration, the appropriate metabolism of cells, and the efficient oxidation of glucose. (ferienwohnung-gluecksburg.net)
  • Thiamine pyrophosphate (also called thiamine diphosphate) is derived from vitamin Bi (thiamine) and has the structure: The thiazole ring can lose a proton to produce a negatively-charged carbon atom: This is a potent nucleophile and can participate in covalent catalysis, particularly with α-keto (oxo) acid decarboxylase, α-keto acid oxidase, transketolase and phosphoketolase enzymes. (ferienwohnung-gluecksburg.net)
  • Thiamine pyrophosphate (TPP) plays a vital role in carbohydrate and amino acid metabolism and is an essential cofactor for all living organisms. (ferienwohnung-gluecksburg.net)
  • The best-characterized form is thiamine pyrophosphate (TPP), a coenzyme in the catabolism of sugars and amino acids. (ferienwohnung-gluecksburg.net)
  • Thiamine functions as part of the enzyme thiamine pyrophosphate, or TPP, which is essential for energy production, carbohydrate metabolism, and nerve cell function. (ferienwohnung-gluecksburg.net)
  • Upon absorption into the body, thiamine is used to form thiamine pyrophosphate, which as noted in the table provided is an essential co-factor that used by several cellular enzymes. (ferienwohnung-gluecksburg.net)
  • The mechanistic enzymology of thiamin pyrophosphate-dependent enzymes is described in detail in the chapter by Frank Jordan.1 Here, we will review recent progress on the biosynthesis of thiamin pyrophosphate in bacteria and Saccharomyces cerevisiae with an emphasis on some of the novel organic chemistry that has emerged from these studies. (ferienwohnung-gluecksburg.net)
  • In its diphosphate form (also known as TDP, thiamine pyrophosphate, TPP, or cocarboxylase), it serves as a cofactor for enzymes involved in carbohydrate metabolism, including transketolase, α-ketoglutarate dehydrogenase, pyruvate dehydrogenase, and branched chain α-keto acid dehydrogenase. (ferienwohnung-gluecksburg.net)
  • 4Fe-4S dicluster domain, Domain of unknown function, Thiamine pyrophosphate enzyme, Pyruvate ferredoxin/flavodoxin oxidoreductase, Pyruvate flavodoxin/ferredoxin oxidoreductase, Pyruvate:ferredoxin oxidoreductase core domain II [Interproscan]. (ntu.edu.sg)
  • This step can also be done by thiamine pyrophosphate kinase (EC: 2.7.6.2 - OG_1907) (19). (ens-lyon.fr)
  • Another enzyme not found is thiamin monophosphate phosphohydrolase (EC 3.1.3. (ens-lyon.fr)
  • Transport vesicles accumulated and accompanied short, dilated cisternae, which lack mostly the reaction products of thiamine pyrophosphatase, inosine diphosphatase, and acid phosphatase, and osmium deposits after prolonged osmification. (rupress.org)
  • Vacuoles and vesicles were devoid of reaction products of thiamine pyrophosphatase, inosine diphosphatase, and acid phosphatase. (rupress.org)
  • It catalyzes reversibly the formation of thiamine diphosphate and orthophosphate from thiamine triphosphate. (uchicago.edu)
  • thi2 controls expression of the thiamin-sensitive acid phosphatase and the thiamin biosynthetic genes, whereas thi3 controls thiamin transport in addition to the phosphatase and the biosynthetic genes. (ferienwohnung-gluecksburg.net)
  • Deprivation of thiamin increases the proportion of dephosphorylated (active) enzyme, thus, serving to mitigate against the metabolic consequences of thiamin deficiency. (ferienwohnung-gluecksburg.net)
  • Thiamin-Triphosphatase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • This graph shows the total number of publications written about "Thiamin-Triphosphatase" by people in this website by year, and whether "Thiamin-Triphosphatase" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "Thiamin-Triphosphatase" by people in Profiles. (uchicago.edu)
  • It predicted that the genome of L. plantarum WCFS1 has all the enzymes encoded to biosynthesize folic acid (vitamin B9), thiamine (vitamin B1), and pyridoxine/pyridoxamine (vitamin B6), and the authors were able to fill gaps in the biosynthesis pathways that where caused by poor annotation of the sequenced genome. (ens-lyon.fr)
  • Inorganic pyrophosphatase [Interproscan]. (ntu.edu.sg)
  • Another putative gap in thiamin metabolism is a phosphorylation step of thiamine phosphate, by thiamine-monophosphate kinase ThiL (EC: 2.7.4.16). (ens-lyon.fr)
  • Thiamin pyrophosphokinase, thiamin-binding domain [Interproscan]. (ntu.edu.sg)
  • Our analysis shows that there are several putative gaps in the thiamine biosynthesis pathways starting from either purine metabolism, pyruvate or from cysteine as precursor (Figure 17). (ens-lyon.fr)
  • Taking the above substitutions into consideration, most strains appear to have complete thiamine biosynthesis pathways. (ens-lyon.fr)
  • Specific proteins such as peptidyl-prolyl cis-trans isomerase (A2WJU9), thiamine thiazole synthase (A2YM28), and alanine-tRNA ligase (B8B4H5) upregulated in IR29 and FL478 indicate key mechanisms of M. oryzae CBMB20 mediated plant growth promotion in rice. (springeropen.com)
  • Thiamine (vitamin B1) is required in the diet of animals, and thiamine deficiency leads to diseases such as beri-beri and the Wernicke-Korsakoff syndrome. (ferienwohnung-gluecksburg.net)
  • Thiamine is a water-soluble vitamin. (ens-lyon.fr)
  • This is the function of thiamine: it acts as an electron sink, accepting electron density so as to allow for the formation of what amounts to a carbonyl anion. (ferienwohnung-gluecksburg.net)
  • This graph shows the total number of publications written about "Pyrophosphatases" by people in this website by year, and whether "Pyrophosphatases" was a major or minor topic of these publications. (childrensmercy.org)

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