Phthalic Anhydrides
Maleic Anhydrides
Acid Anhydride Hydrolases
Succinic Anhydrides
Acetic Anhydrides
Aconitic Acid
Hydrolases
Respiration Disorders
Occupational Exposure
A novel interaction mechanism accounting for different acylphosphatase effects on cardiac and fast twitch skeletal muscle sarcoplasmic reticulum calcium pumps. (1/700)
In cardiac and skeletal muscle Ca2+ translocation from cytoplasm into sarcoplasmic reticulum (SR) is accomplished by different Ca2+-ATPases whose functioning involves the formation and decomposition of an acylphosphorylated phosphoenzyme intermediate (EP). In this study we found that acylphosphatase, an enzyme well represented in muscular tissues and which actively hydrolyzes EP, had different effects on heart (SERCA2a) and fast twitch skeletal muscle SR Ca2+-ATPase (SERCA1). With physiological acylphosphatase concentrations SERCA2a exhibited a parallel increase in the rates of both ATP hydrolysis and Ca2+ transport; in contrast, SERCA1 appeared to be uncoupled since the stimulation of ATP hydrolysis matched an inhibition of Ca2+ pump. These different effects probably depend on phospholamban, which is associated with SERCA2a but not SERCA1. Consistent with this view, the present study suggests that acylphosphatase-induced stimulation of SERCA2a, in addition to an enhanced EP hydrolysis, may be due to a displacement of phospholamban, thus to a removal of its inhibitory effect. (+info)Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication. (2/700)
The highly conserved non-structural protein 2C of picornaviruses is involved in viral genome replication and encapsidation and in the rearrangement of intracellular structures. 2C binds RNA, has nucleoside triphosphatase activity, and shares three motifs with superfamily III helicases. Motifs "A" and "B" are involved in nucleotide triphosphate (NTP) binding and hydrolysis, whereas a function for motif "C" has not yet been demonstrated. Poliovirus RNA replication is inhibited by millimolar concentrations of guanidine hydrochloride (GdnHCl). Resistance and dependence to GdnHCl map to 2C. To characterize the nucleoside triphosphatase activity of 2C, we purified poliovirus recombinant 2C fused to glutathione S-transferase (GST-2C) from Escherichia coli. GST-2C hydrolyzed ATP with a Km of 0.7 mM. Other NTPs, including GTP, competed with ATP for binding to 2C but were poor substrates for hydrolysis. Mutation of conserved residues in motif A and B abolished ATPase activity, as did mutation of the conserved asparagine residue in motif C, an observation indicating the involvement of this motif in ATP hydrolysis. GdnHCl at millimolar concentrations inhibited ATP hydrolysis. Mutations in 2C that confer poliovirus resistant to or dependent on GdnHCl increased the tolerance to GdnHCl up to 100-fold. (+info)The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids. (3/700)
NS3 protein of dengue virus type 2 has a serine protease domain within the N-terminal 180 residues. NS2B is required for NS3 to form an active protease involved in processing of the viral polyprotein precursor. The region carboxy terminal to the protease domain has conserved motifs present in several viral RNA-stimulated nucleoside triphosphatase (NTPase)/RNA helicases. To define the functional domains of protease and NTPase/RNA helicase activities of NS3, full-length and amino-terminal deletion mutants of NS3 were expressed in Escherichia coli and purified. Deletion of 160 N-terminal residues of NS3 (as in NS3del.2) had no detrimental effect on the basal and RNA-stimulated NTPase as well as RNA helicase activities. However, mutagenesis of the conserved P-loop motif of the RNA helicase domain (K199E) resulted in loss of ATPase activity. The RNA-stimulated NTPase activity was significantly affected by deletion of 20 amino acid residues from the N terminus or by substitutions of the cluster of basic residues, 184RKRK-->QNGN, of NS3del.2, although both mutant proteins retained the conserved RNA helicase motifs. Furthermore, the minimal NS3 protease domain, required for cleavage of the 2B-3 site, was precisely defined to be 167 residues, using the in vitro processing of NS2B-NS3 precursors. Our results reveal that the functional domains required for serine protease and RNA-stimulated NTPase activities map within the region between amino acid residues 160 and 180 of NS3 protein and that a novel motif, the cluster of basic residues 184RKRK, plays an important role for the RNA-stimulated NTPase activity. (+info)The Saccharomyces cerevisiae YOR163w gene encodes a diadenosine 5', 5"'-P1,P6-hexaphosphate (Ap6A) hydrolase member of the MutT motif (Nudix hydrolase) family. (4/700)
The YOR163w open reading frame on chromosome XV of the Saccharomyces cerevisiae genome encodes a member of the MutT motif (nudix hydrolase) family of enzymes of Mr 21,443. By cloning and expressing this gene in Escherichia coli and S. cerevisiae, we have shown the product to be a (di)adenosine polyphosphate hydrolase with a previously undescribed substrate specificity. Diadenosine 5',5"'-P1, P6-hexaphosphate is the preferred substrate, and hydrolysis in H218O shows that ADP and adenosine 5'-tetraphosphate are produced by attack at Pbeta and AMP and adenosine 5'-pentaphosphate are produced by attack at Palpha with a Km of 56 microM and kcat of 0.4 s-1. Diadenosine 5',5"'-P1,P5-pentaphosphate, adenosine 5'-pentaphosphate, and adenosine 5'-tetraphosphate are also substrates, but not diadenosine 5',5"'-P1,P4-tetraphosphate or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols. The enzyme, which was shown to be expressed in log phase yeast cells by immunoblotting, displays optimal activity at pH 6.9, 50 degrees C, and 4-10 mM Mg2+ (or 200 microM Mn2+). It has an absolute requirement for a reducing agent, such as dithiothreitol (1 mM), and is inhibited by Ca2+ with an IC50 of 3.3 mM and F- (noncompetitively) with a Ki of 80 microM. Its function may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation. (+info)Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein. (5/700)
The non-structural protein 3 (NS3) of hepatitis C virus (HCV) possesses three activities which are likely to be essential for virus replication; a serine protease located in the N terminus and helicase and NTPase activities located in the C terminus. Sequence analysis of the helicase/NTPase domain has identified motifs indicative of the DEAD-box family of helicases. Here we present the characterization of the helicase and NTPase activities of full-length NS3, expressed as a His-tagged fusion protein in E. coli, and make comparisons with published data of NS3 helicase domain alone. The helicase and NTPase activities of full-length NS3 have been demonstrated and we have characterized the effects of amino acid substitutions on conserved motifs of NS3 helicase. Helicase and NTPase activities were dependent on Mg2+ and ATP and inhibited by monovalent cations. NS3 was able to hydrolyse all four NTPs and dNTPs to drive DNA duplex unwinding but with differing abilities. NTPase activity was stimulated by all polynucleotides tested, with poly(U) having the greatest effect. Mutational analysis of conserved motifs of NS3 helicase showed all conserved residues to be required for optimal activity. These results are in accord with a recently proposed model for NS3 helicase activity. (+info)The FHIT gene is expressed in pancreatic ductular cells and is altered in pancreatic cancers. (6/700)
We examined 2 normal pancreata, 21 primary pancreatic ductal cancers, and 19 pancreatic cancer cell lines for Fhit expression and FHIT gene status. The normal pancreas expressed Fhit protein in the cytoplasm of ductular cells, whereas interlobular and larger ducts, acini, and insulae of Langerhans were negative. Fhit protein was detected by immunoblot assay in 11 pancreatic cancer cell lines; of the 8 cell lines lacking Fhit protein, 7 lacked FHIT mRNA and 1 showed an abnormally sized transcript. DNA from five of these eight cell lines showed homozygous loss of FHIT exon 5. In 8 of the 21 primary cancers, Fhit expression was detected by immunohistochemistry. Reverse transcription-PCR analysis of 6 of the 13 cases lacking Fhit showed normal-sized FHIT product in 3 cases and a mixture of normal and abnormal products in the other 3. Sequencing showed that abnormal bands were missing variable numbers of exons. Loss of microsatellite DNA markers internal to the FHIT gene was observed in 10 of 13 primary cancers lacking Fhit protein (homozygous in two cases) and in only 1 of the 8 cancers expressing Fhit protein. In nine primary cancers, four expressing and five lacking Fhit protein, it was possible to obtain pure cancer DNA by microdissection. Three of the five microdissected cases lacking Fhit protein exhibited homozygous deletion of FHIT exon 5. In conclusion, the lack of Fhit protein in pancreatic cancers correlated with absence or alteration of FHIT mRNA and was often associated with FHIT gene anomalies. (+info)Loss of heterozygosity at 3p14.2 in clear cell renal cell carcinoma is an early event and is highly localized to the FHIT gene locus. (7/700)
The VHL tumor suppressor gene (TSG) at 3p25-26 is strongly implicated in the pathogenesis of clear cell renal cell carcinoma (cRCC). In addition, 3p14.2 and 3p21 are suspected of harboring additional TSGs in cRCC, with FHIT being a candidate TSG at 3p14.2. We examined 87 microdissected, histologically well-defined cRCCs classified according to tumor-node-metastasis (TNM) stage (stage 1, 23 cases; stage 2, 14 cases; stage 3, 24 cases; stage 4, 26 cases) and Fuhrman grade (grade 1, 24 cases; grade 2, 19 cases; grade 3, 19 cases; grade 4, 8 cases; sarcomatoid cRCC, 17 cases) for loss of heterozygosity (LOH) at 3p14.2 and 3p25-26 using a series of precisely mapped microsatellite probes. We found that LOH at 3p14.2 exceeded LOH at 3p25-26 in frequency (69% versus 48.3%; P < 0.03) and was highly localized to markers within the FHIT gene locus (D3S1300 and D3S4260), with the majority of chromosomal breakpoints also mapping to this region. In addition, 3p14.2 LOH (P < 0.03), but not 3p25-26 LOH (P = nonsignificant), was associated with lower tumor grades (grades 1-3). These findings suggest that 3p14.2 genomic deletions may be among the earliest events in cRCC pathogenesis, preceding genomic deletions at the VHL locus. FHIT, or an as yet undiscovered TSG mapping to the D3S4103-D3S4260 interval, could be the molecular target of the 3p14.2 deletions. (+info)Designing conditions for in vitro formation of amyloid protofilaments and fibrils. (8/700)
We have been able to convert a small alpha/beta protein, acylphosphatase, from its soluble and native form into insoluble amyloid fibrils of the type observed in a range of pathological conditions. This was achieved by allowing slow growth in a solution containing moderate concentrations of trifluoroethanol. When analyzed with electron microscopy, the protein aggregate present in the sample after long incubation times consisted of extended, unbranched filaments of 30-50 A in width that assemble subsequently into higher order structures. This fibrillar material possesses extensive beta-sheet structure as revealed by far-UV CD and IR spectroscopy. Furthermore, the fibrils exhibit Congo red birefringence, increased fluorescence with thioflavine T and cause a red-shift of the Congo red absorption spectrum. All of these characteristics are typical of amyloid fibrils. The results indicate that formation of amyloid occurs when the native fold of a protein is destabilized under conditions in which noncovalent interactions, and in particular hydrogen bonding, within the polypeptide chain remain favorable. We suggest that amyloid formation is not restricted to a small number of protein sequences but is a property common to many, if not all, natural polypeptide chains under appropriate conditions. (+info)Anhydrides are chemical compounds that form when a single molecule of water is removed from an acid, resulting in the formation of a new compound. The term "anhydride" comes from the Greek words "an," meaning without, and "hydor," meaning water.
In organic chemistry, anhydrides are commonly formed by the removal of water from a carboxylic acid. For example, when acetic acid (CH3COOH) loses a molecule of water, it forms acetic anhydride (CH3CO)2O. Acetic anhydride is a reactive compound that can be used to introduce an acetyl group (-COCH3) into other organic compounds.
Inorganic anhydrides are also important in chemistry and include compounds such as sulfur trioxide (SO3), which is an anhydride of sulfuric acid (H2SO4). Sulfur trioxide can react with water to form sulfuric acid, making it a key intermediate in the production of this important industrial chemical.
It's worth noting that some anhydrides can be hazardous and may require special handling and safety precautions.
I'm sorry for any confusion, but "Phthalic Anhydrides" is not a medical term. It is a chemical compound with the formula C6H4(CO)2O. Phthalic anhydride is a white crystalline powder used in the industrial synthesis of plasticizers, resins, and dyes.
If you have any questions about medical terminology or concepts, please don't hesitate to ask!
I believe there may be some confusion in your question. Maleic anhydride is not a medical term, but rather a chemical compound with the formula C2H2O3. It is a white crystalline solid that is used in industrial applications such as the production of polymers and resins.
If you are asking about a medical condition related to exposure or sensitivity to maleic anhydride, I would recommend consulting a medical professional for accurate information. However, in general, inhalation or skin contact with maleic anhydride can cause irritation and respiratory symptoms, and prolonged exposure may lead to more serious health effects. People with sensitivities or allergies to the compound may experience more severe reactions.
Acid anhydride hydrolases are a class of enzymes that catalyze the hydrolysis (breakdown) of acid anhydrides, which are chemical compounds formed by the reaction between two carboxylic acids. This reaction results in the formation of a molecule of water and the release of a new carboxylic acid.
Acid anhydride hydrolases play important roles in various biological processes, including the metabolism of lipids, carbohydrates, and amino acids. They are also involved in the regulation of intracellular pH and the detoxification of xenobiotics (foreign substances).
Examples of acid anhydride hydrolases include esterases, lipases, and phosphatases. These enzymes have different substrate specificities and catalytic mechanisms, but they all share the ability to hydrolyze acid anhydrides.
The term "acid anhydride hydrolase" is often used interchangeably with "esterase," although not all esterases are capable of hydrolyzing acid anhydrides.
I'm sorry for any confusion, but "Succinic Anhydrides" is not a recognized medical term. Succinic anhydride is a chemical compound with the formula (CH2)2(CO)2O. It is used in organic synthesis as a dehydrating agent and acylating agent. If you're asking about a medical application or effect of succinic anhydride or its derivatives, I would need more specific information to provide an accurate and helpful response.
Acetic anhydride is a chemical compound with the formula (CH3CO)2O. It is a colorless liquid that is used as a reagent in organic synthesis, particularly in the production of cellulose acetate and other acetate esters. Acetic anhydride is also an important intermediate in the synthesis of certain pharmaceuticals and dyes.
In medical terminology, acetic anhydride is not typically used as a diagnostic or therapeutic agent. However, it can be used in laboratory settings to synthesize compounds that may have medical applications. For example, acetic anhydride has been used to produce certain antiviral drugs and antibiotics.
It is important to note that acetic anhydride can be harmful or fatal if swallowed, inhaled, or absorbed through the skin. It can cause burns and eye damage, and may be harmful to the respiratory system if inhaled. Therefore, it should be handled with care and used only in well-ventilated areas with appropriate personal protective equipment.
Aconitic acid is a type of organic acid that is found naturally in some plants, including Aconitum napellus (monkshood or wolf's bane). It is a white crystalline powder with a sour taste and is soluble in water. In the human body, aconitic acid is produced as a byproduct of energy metabolism and can be found in small amounts in various tissues.
Aconitic acid has three carboxylic acid groups, making it a triprotic acid, which means that it can donate three protons (hydrogen ions) in solution. It is a strong acid and is often used as a laboratory reagent for various chemical reactions. In the food industry, aconitic acid may be used as a food additive or preservative.
It's important to note that some species of Aconitum plants contain highly toxic compounds called aconitines, which can cause serious harm or even death if ingested. Therefore, these plants should not be consumed or handled without proper knowledge and precautions.
Hydrolases are a class of enzymes that help facilitate the breakdown of various types of chemical bonds through a process called hydrolysis, which involves the addition of water. These enzymes catalyze the cleavage of bonds in substrates by adding a molecule of water, leading to the formation of two or more smaller molecules.
Hydrolases play a crucial role in many biological processes, including digestion, metabolism, and detoxification. They can act on a wide range of substrates, such as proteins, lipids, carbohydrates, and nucleic acids, breaking them down into smaller units that can be more easily absorbed or utilized by the body.
Examples of hydrolases include:
1. Proteases: enzymes that break down proteins into smaller peptides or amino acids.
2. Lipases: enzymes that hydrolyze lipids, such as triglycerides, into fatty acids and glycerol.
3. Amylases: enzymes that break down complex carbohydrates, like starches, into simpler sugars, such as glucose.
4. Nucleases: enzymes that cleave nucleic acids, such as DNA or RNA, into smaller nucleotides or oligonucleotides.
5. Phosphatases: enzymes that remove phosphate groups from various substrates, including proteins and lipids.
6. Esterases: enzymes that hydrolyze ester bonds in a variety of substrates, such as those found in some drugs or neurotransmitters.
Hydrolases are essential for maintaining proper cellular function and homeostasis, and their dysregulation can contribute to various diseases and disorders.
Respiratory disorders are a group of conditions that affect the respiratory system, including the nose, throat (pharynx), windpipe (trachea), bronchi, lungs, and diaphragm. These disorders can make it difficult for a person to breathe normally and may cause symptoms such as coughing, wheezing, shortness of breath, and chest pain.
There are many different types of respiratory disorders, including:
1. Asthma: A chronic inflammatory disease that causes the airways to become narrow and swollen, leading to difficulty breathing.
2. Chronic obstructive pulmonary disease (COPD): A group of lung diseases, including emphysema and chronic bronchitis, that make it hard to breathe.
3. Pneumonia: An infection of the lungs that can cause coughing, chest pain, and difficulty breathing.
4. Lung cancer: A type of cancer that forms in the tissues of the lungs and can cause symptoms such as coughing, chest pain, and shortness of breath.
5. Tuberculosis (TB): A bacterial infection that mainly affects the lungs but can also affect other parts of the body.
6. Sleep apnea: A disorder that causes a person to stop breathing for short periods during sleep.
7. Interstitial lung disease: A group of disorders that cause scarring of the lung tissue, leading to difficulty breathing.
8. Pulmonary fibrosis: A type of interstitial lung disease that causes scarring of the lung tissue and makes it hard to breathe.
9. Pleural effusion: An abnormal accumulation of fluid in the space between the lungs and chest wall.
10. Lung transplantation: A surgical procedure to replace a diseased or failing lung with a healthy one from a donor.
Respiratory disorders can be caused by a variety of factors, including genetics, exposure to environmental pollutants, smoking, and infections. Treatment for respiratory disorders may include medications, oxygen therapy, breathing exercises, and lifestyle changes. In some cases, surgery may be necessary to treat the disorder.
Citraconic anhydride is a chemical compound that is used in the synthesis of various pharmaceuticals and industrial products. It is an anhydride of citraconic acid, which is a unsaturated dicarboxylic acid. Citraconic anhydride is an important reagent in organic chemistry due to its ability to act as a acylating agent, meaning it can transfer an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom: -CO-) to other molecules.
In the medical field, citraconic anhydride is not used directly as a therapeutic agent. However, it may be used in the production of certain drugs or drug delivery systems. For example, it has been used in the synthesis of biodegradable polymers for drug delivery, and in the modification of proteins and peptides for therapeutic purposes.
It is important to note that citraconic anhydride itself is not a medication, but rather a chemical reagent used in the production of certain pharmaceutical compounds. As such, it does not have a specific medical definition, but rather a chemical one.
Occupational exposure refers to the contact of an individual with potentially harmful chemical, physical, or biological agents as a result of their job or occupation. This can include exposure to hazardous substances such as chemicals, heavy metals, or dusts; physical agents such as noise, radiation, or ergonomic stressors; and biological agents such as viruses, bacteria, or fungi.
Occupational exposure can occur through various routes, including inhalation, skin contact, ingestion, or injection. Prolonged or repeated exposure to these hazards can increase the risk of developing acute or chronic health conditions, such as respiratory diseases, skin disorders, neurological damage, or cancer.
Employers have a legal and ethical responsibility to minimize occupational exposures through the implementation of appropriate control measures, including engineering controls, administrative controls, personal protective equipment, and training programs. Regular monitoring and surveillance of workers' health can also help identify and prevent potential health hazards in the workplace.
Occupational diseases are health conditions or illnesses that occur as a result of exposure to hazards in the workplace. These hazards can include physical, chemical, and biological agents, as well as ergonomic factors and work-related psychosocial stressors. Examples of occupational diseases include respiratory illnesses caused by inhaling dust or fumes, hearing loss due to excessive noise exposure, and musculoskeletal disorders caused by repetitive movements or poor ergonomics. The development of an occupational disease is typically related to the nature of the work being performed and the conditions in which it is carried out. It's important to note that these diseases can be prevented or minimized through proper risk assessment, implementation of control measures, and adherence to safety regulations.
Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.
Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.
These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.
Acid anhydride hydrolases
A genome-wide association study identifies CDHR3 as a susceptibility locus for early childhood asthma with severe exacerbations
SCOPe 2.08: Structural Classification of Proteins - extended
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DeCS
GO:0016817hydrolase activity, acting on acid anhydrides - Slorth
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PDB 1NGD | Chain STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE...
