Sulfatases
Arylsulfatases
Cerebroside-Sulfatase
Chondro-4-Sulfatase
Sphingolipidoses
Sulfotransferases
Lysosomal Storage Diseases
Steryl-Sulfatase
Multiple Sulfatase Deficiency Disease
Chondroitinsulfatases
Alanine
Glycine
N-Acetylgalactosamine-4-Sulfatase
Protein Processing, Post-Translational
Molecular Sequence Data
Heparitin Sulfate
Klebsiella pneumoniae
Amino Acid Sequence
Serine
Encyclopedias as Topic
Glycosaminoglycans
Enzymatic and immunological characterization of the Mycobacterium fortuitum complex. (1/501)
The arylsulfatase isozymes of Mycobacterium fortuitum, M. peregrinum, M. chelonei subsp. chelonei, and M. chelonei subsp. abscessus were examined to determine the isozymal and immunological relationship among the members of the M. fortuitum complex. Cell extracts were subjected to electrophoresis on agarose and polyacrylamide gel, and arylsulfatase activity was localized using beta-naphthyl sulfate as substrate. Unique zymograms were produced for M. fortuitum, M. peregrinum, and M. chelonei which were characteristic for each species. The immunological relationship among the sulfatases was assayed by using immunodiffusion and immunoelectrophoresis followed by sulfatase staining for the enzyme. One of the isozymes of M. fortuitum and M. peregrinum cross-reacted, showing immunological identity. Antisera to sulfatases of M. fortuitum and M. peregrinum did not react with sulfatases of M. chelonei. The characterization of sulfatase isozymes in extracts of organisms in the M. fortuitum complex suggests the division of the M. fortuitum complex into two species, M. fortuitum and M. chelonei, with subspecies designations. (+info)A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. (2/501)
Sequence analysis of the probable archaeal phosphoglycerate mutase resulted in the identification of a superfamily of metalloenzymes with similar metal-binding sites and predicted conserved structural fold. This superfamily unites alkaline phosphatase, N-acetylgalactosamine-4-sulfatase, and cerebroside sulfatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulfatases. In addition to the metal-binding motifs, all these enzymes contain a set of conserved amino acid residues that are likely to be required for the enzymatic activity. Mutational changes in the vicinity of these residues in several sulfatases cause mucopolysaccharidosis (Hunter, Maroteaux-Lamy, Morquio, and Sanfilippo syndromes) and metachromatic leucodystrophy. (+info)Sequence analysis of heparan sulphate and heparin oligosaccharides. (3/501)
The biological activity of heparan sulphate (HS) and heparin largely depends on internal oligosaccharide sequences that provide specific binding sites for an extensive range of proteins. Identification of such structures is crucial for the complete understanding of glycosaminoglycan (GAG)-protein interactions. We describe here a simple method of sequence analysis relying on the specific tagging of the sugar reducing end by 3H radiolabelling, the combination of chemical scission and specific enzymic digestion to generate intermediate fragments, and the analysis of the generated products by strong-anion-exchange HPLC. We present full sequence data on microgram quantities of four unknown oligosaccharides (three HS-derived hexasaccharides and one heparin-derived octasaccharide) which illustrate the utility and relative simplicity of the technique. The results clearly show that it is also possible to read sequences of inhomogeneous preparations. Application of this technique to biologically active oligosaccharides should accelerate progress in the understanding of HS and heparin structure-function relationships and provide new insights into the primary structure of these polysaccharides. (+info)The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. (4/501)
The catalytic residue of eukaryotic and prokaryotic sulfatases is a alpha-formylglycine. In the sulfatase of Klebsiella pneumoniae the formylglycine is generated by posttranslational oxidation of serine 72. We cloned the atsBA operon of K. pneumoniae and found that the sulfatase was expressed in inactive form in Escherichia coli transformed with the structural gene (atsA). Coexpression of the atsB gene, however, led to production of high sulfatase activity, indicating that the atsB gene product plays a posttranslational role that is essential for the sulfatase to gain its catalytic activity. This was verified after purification of the sulfatase from the periplasm of the cells. Peptide analysis of the protein expressed in the presence of AtsB revealed that half of the polypeptides carried the formylglycine at position 72, while the remaining polypeptides carried the encoded serine. The inactive sulfatase expressed in the absence of AtsB carried exclusively serine 72, demonstrating that the atsB gene is required for formylglycine modification. This gene encodes a 395-amino acid residue iron sulfur protein that has a cytosolic localization and is supposed to directly or indirectly catalyze the oxidation of the serine to formylglycine. (+info)A novel mucin-sulphatase activity found in Burkholderia cepacia and Pseudomonas aeruginosa. (5/501)
Lung infections due to Burkholderia cepacia and Pseudomonas aeruginosa in patients with cystic fibrosis (CF) are common, are associated with respiratory morbidity and are a cause of mortality. Respiratory mucin in CF patients is highly sulphated, which increases its resistance to bacterial degradation. Desulphation increases the susceptibility of mucin to degradation by bacterial glycosidases and proteinases, and subsequent deglycosylation may facilitate bacterial colonisation by increasing available substrates and binding sites. This study determined whether clinical and environmental strains of B. cepacia and P. aeruginosa had the ability to desulphate mucin. Mucin-sulphatase activity was tested by incubating bacterial cell suspensions with 35S-sulphated mucins purified from LS174T and HT29-MTX human colon carcinoma cell lines. These mucins were also used to test for differences in substrate specificities. Mucin-sulphatase activity was detected in all nine B. cepacia strains and in four of six P. aeruginosa strains. There was strain variability in the level of mucin-sulphatase activity. Aryl-sulphatase activities of Pseudomonas isolates (determined with methylumbelliferyl sulphate) were c. 20-fold higher than those of B. cepacia strains, and were independent of mucin-sulphatase activity. This is the first report to demonstrate desulphation of mucin by B. cepacia and P. aeruginosa. It is concluded that B. cepacia and P. aeruginosa produce one or more cell-bound glycosulphatase(s), in addition to aryl-sulphatase activity. Mucin-sulphatase activity of B. cepacia and P. aeruginosa may contribute to their association with airway infections in patients with cystic fibrosis. (+info)Ontogeny of estrogen sulfatase activity in ovine fetal hypothalamus, hippocampus, and brain stem. (6/501)
Ovine parturition is initiated by increases in fetal hypothalamus-pituitary-adrenal (HPA) axis activity, which in turn increase placental estrogen biosynthesis and ultimately increase uterine contractility. In addition to the action in the uterus, estrogens augment fetal ACTH secretion. In late gestation, estrone sulfate is more abundant in fetal plasma than is unconjugated estrone. We studied hypothalamus, hippocampus, and brain stem tissue from fetal, neonatal, and adult sheep to test the hypothesis that the ovine brain contains estrogen sulfatase activity. We found that the activity in the hippocampus was significantly increased in late-gestation fetuses compared with both younger and older animals. No significant change in either hypothalamus or brain stem was revealed; however, the activity in all brain areas was high. Immunohistochemistry revealed the presence of estrogen sulfatase in the paraventricular nucleus of the hypothalamus, the nucleus of the solitary tract, and the rostral ventrolateral medulla. We conclude that ovine fetal hypothalamus, hippocampus, and brain stem contain estrogen sulfatase activity and that the activity in the hippocampus is developmentally regulated. (+info)Screening for novel pancreatic genes expressed during embryogenesis. (7/501)
We have combined suppressive subtractive hybridization with in situ hybridization to identify genes expressed at early stages of pancreas development. By using polymerase chain reaction amplification and subtractive hybridization, this protocol for screening can be applied when the amount of RNA is limited. Seven genes expressed in or adjacent to the pancreas anlage were isolated, three of which show similarity to known genes. The expression pattern and sequence information indicate that some of the genes could govern pancreas development. (+info)Iduronate sulfatase analysis of hair roots for identification of Hunter syndrome heterozygotes. (8/501)
Iduronate sulfatase, the enzyme deficient in Hunter syndrome, can be readily measured in individual hair roots. Samples from Hunter syndrome hemizygotes had activities at or near the limits of detection. Samples from two mothers of Hunter syndrome patients, one an obligate heterozygote, had lower average iduronate sulfatase activity than the normal mean, and a significant number of hair roots had activity in the pathognomic range. A third mother showed a normal distribution of enzyme activity, and no hair roots were in the range of those from an affected individual. These results are similar to studies on the distribution of other X-linked enzymes in individual hair root samples from heterozygotes. This suggests that hair root iduronate sulfatase assessment is useful in the detection of Hunter syndrome carrier status, but further refinement of the test system is necessary. (+info)Sulfatases are a group of enzymes that play a crucial role in the metabolism of sulfated steroids, glycosaminoglycans (GAGs), and other sulfated molecules. These enzymes catalyze the hydrolysis of sulfate groups from these substrates, converting them into their respective unsulfated forms.
The human genome encodes for several different sulfatases, each with specificity towards particular types of sulfated substrates. For instance, some sulfatases are responsible for removing sulfate groups from steroid hormones and neurotransmitters, while others target GAGs like heparan sulfate, dermatan sulfate, and keratan sulfate.
Defects in sulfatase enzymes can lead to various genetic disorders, such as multiple sulfatase deficiency (MSD), X-linked ichthyosis, and mucopolysaccharidosis (MPS) type IIIC (Sanfilippo syndrome type C). These conditions are characterized by the accumulation of sulfated molecules in different tissues, resulting in progressive damage to multiple organs and systems.
Arylsulfatases are a group of enzymes that play a role in the breakdown and recycling of complex molecules in the body. Specifically, they catalyze the hydrolysis of sulfate ester bonds in certain types of large sugar molecules called glycosaminoglycans (GAGs).
There are several different types of arylsulfatases, each of which targets a specific type of sulfate ester bond. For example, arylsulfatase A is responsible for breaking down sulfate esters in a GAG called cerebroside sulfate, while arylsulfatase B targets a different GAG called dermatan sulfate.
Deficiencies in certain arylsulfatases can lead to genetic disorders. For example, a deficiency in arylsulfatase A can cause metachromatic leukodystrophy, a progressive neurological disorder that affects the nervous system and causes a range of symptoms including muscle weakness, developmental delays, and cognitive decline. Similarly, a deficiency in arylsulfatase B can lead to Maroteaux-Lamy syndrome, a rare genetic disorder that affects the skeleton, eyes, ears, heart, and other organs.
Cerebroside-sulfatase is an enzyme that plays a crucial role in the breakdown and recycling of lipids within the body, particularly in the brain. Its primary function is to break down a type of lipid called cerebroside sulfate, which is a major component of the myelin sheath that surrounds and insulates nerve fibers in the brain and nervous system.
Cerebroside-sulfatase deficiency can lead to a group of genetic disorders known as the mucopolysaccharidoses (MPS), specifically MPS IIIB or Sanfilippo syndrome B. In this condition, the lack of cerebroside-sulfatase activity leads to an accumulation of cerebroside sulfate in the lysosomes of cells, resulting in progressive neurological deterioration and developmental delays.
Chondro-4-sulfatase is an enzyme that belongs to the family of hydrolases, specifically those acting on ester bonds in sulfuric acid esters. It is responsible for catalyzing the hydrolysis of the 4-sulfate ester group from N-acetylgalactosamine 4-sulfate residues found in chondroitin 4-sulfate, a type of glycosaminoglycan (GAG) that is abundant in connective tissues such as cartilage.
Chondroitin 4-sulfate plays important roles in the structure and function of the extracellular matrix, including regulating cell adhesion, migration, and differentiation. The action of chondro-4-sulfatase helps to control the balance between sulfated and non-sulfated GAG chains, which is critical for maintaining normal tissue homeostasis.
Defects in chondro-4-sulfatase activity can lead to a rare genetic disorder called chondrodysplasia punctata type 1B (CDPX1B), also known as multiple sulfatase deficiency (MSD). This condition is characterized by skeletal abnormalities, developmental delay, and other neurological symptoms.
Sphingolipidoses are a group of inherited metabolic disorders characterized by the accumulation of sphingolipids in various tissues and organs due to deficiencies in enzymes involved in sphingolipid metabolism. Sphingolipids are a type of lipid molecule that play important roles in cell membranes, signal transduction, and cell recognition.
Examples of sphingolipidoses include Gaucher's disease, Tay-Sachs disease, Niemann-Pick disease, Fabry disease, and Krabbe disease, among others. These disorders can affect various organs and systems in the body, including the brain, liver, spleen, bones, and nervous system, leading to a range of symptoms such as developmental delay, seizures, movement disorders, enlarged organs, and skin abnormalities.
Treatment for sphingolipidoses typically involves managing symptoms and addressing complications, although some forms of these disorders may be amenable to enzyme replacement therapy or stem cell transplantation.
Sulfotransferases (STs) are a group of enzymes that play a crucial role in the process of sulfoconjugation, which is the transfer of a sulfo group (-SO3H) from a donor molecule to an acceptor molecule. These enzymes are widely distributed in nature and are found in various organisms, including humans.
In humans, STs are involved in the metabolism and detoxification of numerous xenobiotics, such as drugs, food additives, and environmental pollutants, as well as endogenous compounds, such as hormones, neurotransmitters, and lipids. The sulfoconjugation reaction catalyzed by STs can increase the water solubility of these compounds, facilitating their excretion from the body.
STs can be classified into several families based on their sequence similarity and cofactor specificity. The largest family of STs is the cytosolic sulfotransferases, which use 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a cofactor to transfer the sulfo group to various acceptor molecules, including phenols, alcohols, amines, and steroids.
Abnormalities in ST activity have been implicated in several diseases, such as cancer, cardiovascular disease, and neurological disorders. Therefore, understanding the function and regulation of STs is essential for developing new therapeutic strategies to treat these conditions.
Lysosomal storage diseases (LSDs) are a group of rare inherited metabolic disorders caused by defects in lysosomal function. Lysosomes are membrane-bound organelles within cells that contain enzymes responsible for breaking down and recycling various biomolecules, such as proteins, lipids, and carbohydrates. In LSDs, the absence or deficiency of specific lysosomal enzymes leads to the accumulation of undigested substrates within the lysosomes, resulting in cellular dysfunction and organ damage.
These disorders can affect various organs and systems in the body, including the brain, nervous system, bones, skin, and visceral organs. Symptoms may include developmental delays, neurological impairment, motor dysfunction, bone abnormalities, coarse facial features, hepatosplenomegaly (enlarged liver and spleen), and recurrent infections.
Examples of LSDs include Gaucher disease, Tay-Sachs disease, Niemann-Pick disease, Fabry disease, Pompe disease, and mucopolysaccharidoses (MPS). Treatment options for LSDs may include enzyme replacement therapy, substrate reduction therapy, or bone marrow transplantation. Early diagnosis and intervention can help improve the prognosis and quality of life for affected individuals.
Stearyl-sulfatase is a type of enzyme that is responsible for breaking down certain types of fatty substances called lipids in the body. Specifically, it helps to break down a substance called stearyl sulfate, which is a type of sulfated lipid.
Stearyl-sulfatase is found in various tissues throughout the body, including the brain, skin, and kidneys. Mutations in the gene that provides instructions for making this enzyme can lead to a condition called X-linked ichthyosis, which is characterized by dry, scaly skin. This is because the body is unable to properly break down stearyl sulfate and other related lipids, leading to their accumulation in the skin.
In medical terminology, steruly-sulfatase may also be referred to as arylsulfatase C or Arylsulfatase-C.
Multiple sulfatase deficiency (MSD) is a rare inherited metabolic disorder that affects multiple organ systems in the body. It is caused by mutations in the SUMF1 gene, which provides instructions for making an enzyme called formylglycine-generating enzyme (FGE). FGE is essential for the function of several sulfatase enzymes, which are responsible for removing sulfate groups from certain sugar molecules attached to proteins and lipids.
In MSD, the activity of all or most of these sulfatase enzymes is reduced or absent, leading to the accumulation of sulfated molecules in various tissues and organs. This can result in a wide range of symptoms that typically appear in infancy or early childhood, including developmental delay, intellectual disability, coarse facial features, skeletal abnormalities, vision and hearing loss, and problems with mobility and coordination.
MSD is an autosomal recessive disorder, which means that an individual must inherit two copies of the mutated gene (one from each parent) in order to develop the disease. The incidence of MSD is estimated to be less than 1 in 1 million people worldwide. Currently, there is no cure for MSD and treatment is focused on managing symptoms and improving quality of life.
Chondroitin sulfatases are a group of enzymes that break down chondroitin sulfate, which is a type of glycosaminoglycan (GAG) found in connective tissues such as cartilage, bone, and skin. Glycosaminoglycans are long, complex chains of sugars that help provide structure, hydration, and elasticity to these tissues.
Chondroitin sulfate is composed of alternating units of glucuronic acid and N-acetylgalactosamine, with various sulfate groups attached at different positions along the chain. Chondroitin sulfatases cleave specific bonds within this structure to help regulate the turnover and remodeling of GAGs in tissues.
There are several types of chondroitin sulfatases (designated as chondroitin sulfatase A, B, C, D, etc.), each with distinct substrate specificities and cellular localizations. Defects in these enzymes can lead to various genetic disorders, such as skeletal dysplasias and neurodegenerative diseases, due to the accumulation of unprocessed or partially degraded chondroitin sulfate in tissues.
Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.
Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.
In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.
Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.
Sulfuric acid esters, also known as sulfate esters, are chemical compounds formed when sulfuric acid reacts with alcohols or phenols. These esters consist of a organic group linked to a sulfate group (SO4). They are widely used in industry, for example, as detergents, emulsifiers, and solvents. In the body, they can be found as part of various biomolecules, such as glycosaminoglycans and steroid sulfates. However, excessive exposure to sulfuric acid esters can cause irritation and damage to tissues.
N-Acetylgalactosamine-4-Sulfatase is an enzyme that is responsible for breaking down complex carbohydrates in the body. Its specific function is to remove a sulfate group from a particular type of sugar molecule called N-acetylgalactosamine-4-sulfate, which is found on certain proteoglycans (large, complex sugars attached to proteins) in the body.
This enzyme plays an important role in the normal functioning of cells and tissues, particularly in the development and maintenance of bones, cartilage, and other connective tissues. Deficiencies in this enzyme can lead to a rare genetic disorder called Morquio A syndrome (also known as MPS IVA), which is characterized by skeletal abnormalities, short stature, and other health problems.
Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.
Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.
Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.
In the context of medicine and biology, sulfates are ions or compounds that contain the sulfate group (SO4−2). Sulfate is a polyatomic anion with the structure of a sphere. It consists of a central sulfur atom surrounded by four oxygen atoms in a tetrahedral arrangement.
Sulfates can be found in various biological molecules, such as glycosaminoglycans and proteoglycans, which are important components of connective tissue and the extracellular matrix. Sulfate groups play a crucial role in these molecules by providing negative charges that help maintain the structural integrity and hydration of tissues.
In addition to their biological roles, sulfates can also be found in various medications and pharmaceutical compounds. For example, some laxatives contain sulfate salts, such as magnesium sulfate (Epsom salt) or sodium sulfate, which work by increasing the water content in the intestines and promoting bowel movements.
It is important to note that exposure to high levels of sulfates can be harmful to human health, particularly in the form of sulfur dioxide (SO2), a common air pollutant produced by burning fossil fuels. Prolonged exposure to SO2 can cause respiratory problems and exacerbate existing lung conditions.
Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.
The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:
1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.
Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Heparin sulfate is not exactly referred to as "heparitin sulfate" in medical terminology. The correct term is heparan sulfate, which is a type of glycosaminoglycan (GAG), a long unbranched chain of repeating disaccharide units composed of a hexuronic acid and a hexosamine.
Heparan sulfate is found on the cell surface and in the extracellular matrix, where it plays crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and control of blood coagulation. It is also an important component of the proteoglycans, which are complex molecules that help to maintain the structural integrity and function of tissues and organs.
Like heparin, heparan sulfate has a high negative charge due to the presence of sulfate groups, which allows it to bind to and interact with various proteins and growth factors. However, heparan sulfate has a more diverse structure than heparin, with variations in the pattern of sulfation along the chain, which leads to specificity in its interactions with different proteins.
Defects in heparan sulfate biosynthesis or function have been implicated in various human diseases, including certain forms of cancer, developmental disorders, and infectious diseases.
"Klebsiella pneumoniae" is a medical term that refers to a type of bacteria belonging to the family Enterobacteriaceae. It's a gram-negative, encapsulated, non-motile, rod-shaped bacterium that can be found in various environments, including soil, water, and the gastrointestinal tracts of humans and animals.
"Klebsiella pneumoniae" is an opportunistic pathogen that can cause a range of infections, particularly in individuals with weakened immune systems or underlying medical conditions. It's a common cause of healthcare-associated infections, such as pneumonia, urinary tract infections, bloodstream infections, and wound infections.
The bacterium is known for its ability to produce a polysaccharide capsule that makes it resistant to phagocytosis by white blood cells, allowing it to evade the host's immune system. Additionally, "Klebsiella pneumoniae" has developed resistance to many antibiotics, making infections caused by this bacterium difficult to treat and a growing public health concern.
Aldehydes are a class of organic compounds characterized by the presence of a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bonded oxygen atom, also known as a formyl or aldehyde group. The general chemical structure of an aldehyde is R-CHO, where R represents a hydrocarbon chain.
Aldehydes are important in biochemistry and medicine as they are involved in various metabolic processes and are found in many biological molecules. For example, glucose is converted to pyruvate through a series of reactions that involve aldehyde intermediates. Additionally, some aldehydes have been identified as toxicants or environmental pollutants, such as formaldehyde, which is a known carcinogen and respiratory irritant.
Formaldehyde is also commonly used in medical and laboratory settings for its disinfectant properties and as a fixative for tissue samples. However, exposure to high levels of formaldehyde can be harmful to human health, causing symptoms such as coughing, wheezing, and irritation of the eyes, nose, and throat. Therefore, appropriate safety measures must be taken when handling aldehydes in medical and laboratory settings.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.
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.
Glycosaminoglycans (GAGs) are long, unbranched polysaccharides composed of repeating disaccharide units. They are a major component of the extracellular matrix and connective tissues in the body. GAGs are negatively charged due to the presence of sulfate and carboxyl groups, which allows them to attract positively charged ions and water molecules, contributing to their ability to retain moisture and maintain tissue hydration and elasticity.
GAGs can be categorized into four main groups: heparin/heparan sulfate, chondroitin sulfate/dermatan sulfate, keratan sulfate, and hyaluronic acid. These different types of GAGs have varying structures and functions in the body, including roles in cell signaling, inflammation, and protection against enzymatic degradation.
Heparin is a highly sulfated form of heparan sulfate that is found in mast cells and has anticoagulant properties. Chondroitin sulfate and dermatan sulfate are commonly found in cartilage and contribute to its resiliency and ability to withstand compressive forces. Keratan sulfate is found in corneas, cartilage, and bone, where it plays a role in maintaining the structure and function of these tissues. Hyaluronic acid is a large, nonsulfated GAG that is widely distributed throughout the body, including in synovial fluid, where it provides lubrication and shock absorption for joints.
I'm sorry for any confusion, but "sulfonic acids" are not a medical term. They are a type of compound in chemistry, specifically strong organic acids that contain the functional group -SO3H. Sulfonic acids are widely used in industry and research, including the production of detergents, dyes, and pharmaceuticals.
If you have any questions related to medical terminology or concepts, please don't hesitate to ask!
Sulfatase
Monomethyl-sulfatase
Cerebroside-sulfatase
Steroid sulfatase
Choline-sulfatase
Chondro-6-sulfatase
Glucuronate-2-sulfatase
Multiple sulfatase deficiency
Chondro-4-sulfatase
Disulfoglucosamine-6-sulfatase
Iduronate-2-sulfatase
Galactosamine-6 sulfatase
N-acetylgalactosamine-6-sulfatase
N-acetylgalactosamine-4-sulfatase
N-sulfoglucosamine-3-sulfatase
N-acetylglucosamine-6-sulfatase
D-lactate-2-sulfatase
Formylglycine-generating enzyme
SULF1
List of OMIM disorder codes
SULF2
Arylsulfatase B
Helix pomatia
Planctomycetota
2-Methoxyestradiol disulfamate
Estrone sulfate
Estrone phosphate
Steroidogenesis inhibitor
SUMF1
Danazol
Sulfatase - Wikipedia
Multiple sulfatase deficiency: MedlinePlus Genetics
Identification and evolution of glucosinolate sulfatases in a specialist flea beetle | Scientific Reports
Orphanet: Multiple sulfatase deficiency
Human Sulfatase Modifying Factor 2/ SUMF2 Antibody, R D Systems 25μg; | Fisher Scientific
Steroid Sulfatase Inhibitor Reduces Proliferation of Ishikawa Endometrial Cancer Cells in Co-Culture Systems
Galns (galactosamine (N-acetyl)-6-sulfatase) - Rat Genome Database
N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody (NBP1-00190): Novus Biologicals
LOINC Group LG9700-8 Cerebroside sulfatase activator|Imp|Pt|Fibroblasts
Iduronate 2 Sulfatase (Alpha L Iduronate Sulfate Sulfatase or Idursulfase or IDS or EC 3.1.6.13) Development by Therapy Areas...
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The effect of the steroid sulfatase inhibitor (p-O-sulfamoyl)-tetradecanoyl tyramine (DU-14) on learning and memory in rats...
The Study of Oral Steroid Sulphatase Inhibitor BN83495 Versus Megestrol Acetate (MA) in Women With Advanced or Recurrent...
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Anti-Iduronate 2 sulfatase (3B4) - 200 ul | Appalachia Community Cancer Network ACCN
Inhibition of steroid sulfatase activity by tricyclic coumarin sulphamates. - Department of Pharmacology
Phenq vs clenbuterol, stéroïde sulfatase Phenq vs clenbutero | JJ CHEMITECH Group | JJ CHEMITECH
SciELO - Brazil - Expression Pattern of Sulf1 and Sulf2 in Chicken Tissues and Characterization of Their Expression During...
ARSG arylsulfatase G [Homo sapiens (human)] - Gene - NCBI
MP29-11: Targeting DHEA-S transport and steroid sulfatase for more efficient androgen deprivation therapy | AUA University
Multiple mutations are responsible for the high frequency of metachromatic leukodystrophy in a small geographic area
Organic anion-transporting polypeptide B (OATP-B) and its functional comparison with three other OATPs of human liver
Mucopolysaccharidoses Types I-VII: Practice Essentials, Pathophysiology, Epidemiology
Enzyme15
- The FGE enzyme modifies other enzymes called sulfatases, which aid in breaking down substances that contain chemical groups known as sulfates. (medlineplus.gov)
- The activity of multiple sulfatases is impaired because the FGE enzyme modifies all known sulfatase enzymes. (medlineplus.gov)
- Research indicates that mutations that lead to reduced FGE enzyme function are associated with the less severe cases of the condition, whereas mutations that lead to the production of an unstable FGE enzyme tend to be associated with the more severe cases of multiple sulfatase deficiency. (medlineplus.gov)
- Enzyme activity assays with crude beetle protein extracts revealed that glucosinolate sulfatase (GSS) activity is associated with the gut membrane and has narrow substrate specificity towards the benzenic glucosinolate sinalbin. (nature.com)
- Iduronate 2 Sulfatase (Alpha L Iduronate Sulfate Sulfatase or Idursulfase or IDS or EC 3.1.6.13) - Iduronate 2-sulfatase (IDS) is a sulfatase enzyme associated with Hunter syndrome. (bharatbook.com)
- La stéroïde sulfatase est une enzyme régulant la conversion de stéroïdes sulfatés inactifs en stéroïdes actifs et en stéroïdes oestrogéniques (Purohit et al. (jjchemitech.com)
- Stéroïde sulfatase, Déficit en protéine s - Acheter des stéroïdes anabolisants légaux Stéroïde sulfatase Steroid sulfatase from the microsomal fraction of rat liver exhibits properties which are suggestive of an allosteric type of enzyme. (jjchemitech.com)
- La stéroïde sulfatase de la fraction microsomale de foie de rat se comporte comme un enzyme allostérique. (jjchemitech.com)
- The protein encoded by this gene belongs to the sulfatase enzyme family. (nih.gov)
- 12q14 (Sanfilippo syndrome): The diagnosis requires a specific lysosomal enzyme assay for glucosamine ( N -acetyl)-6-sulfatase (GNS) activity. (medscape.com)
- We report a mechanistic role for the heparan sulfate editing enzyme sulfatase 2 (SULF2) in CCA pathogenesis. (elsevierpure.com)
- N,N-Dialkylated derivatives of the steroid sulphatase inhibitor, oestrone 3-O-sulphamate (EMATE) are weak reversible inhibitors of the enzyme. (ox.ac.uk)
- MPS II is caused by a lack of the enzyme iduronate sulfatase. (mountsinai.org)
- The medicine called idursulfase (Elaprase), which replaces the enzyme iduronate sulfatase may be recommended. (mountsinai.org)
- In 1976, the enzyme deficiency in Morquio syndrome type IVA (galactosamine-6-sulfatase deficiency [ie, N -acetyl-galactosamine-6-sulfate sulfatase deficiency]) was identified. (medscape.com)
Iduronate5
- Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. (bharatbook.com)
- Iduronate 2 Sulfatase (Alpha L Iduronate Sulfate Sulfatase or Idursulfase or IDS or EC 3.1.6.13) pipeline Target constitutes close to 13 molecules. (bharatbook.com)
- The latest report Iduronate 2 Sulfatase - Drugs In Development, 2022, outlays comprehensive information on the Iduronate 2 Sulfatase (Alpha L Iduronate Sulfate Sulfatase or Idursulfase or IDS or EC 3.1.6.13) targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type. (bharatbook.com)
- It also reviews key players involved in Iduronate 2 Sulfatase (Alpha L Iduronate Sulfate Sulfatase or Idursulfase or IDS or EC 3.1.6.13) targeted therapeutics development with respective active and dormant or discontinued projects. (bharatbook.com)
- Mouse monoclonal to Iduronate 2 sulfatase - Store at -20°C or lower. (accnweb.com)
Steroid sulfatase inhibitor4
- Next we examined the effects of steroid sulfatase inhibitor and aromatase inhibitor in monoculture of endometrial cancer cell line (Ishikawa) and in a co-culture system involving an Ishikawa cells and stromal cells. (scirp.org)
- The effect of the steroid sulfatase inhibitor (p-O-sulfamoyl)-tetradecanoyl tyramine (DU-14) on learning and memory in rats with selective lesion of septal-hippocampal cholinergic tract. (atsbio.com)
- Babalola PA, Fitz NF, Gibbs RB, Flaherty PT, Li PK, Johnson DA (2012) The effect of the steroid sulfatase inhibitor (p-O-sulfamoyl)-tetradecanoyl tyramine (DU-14) on learning and memory in rats with selective lesion of septal-hippocampal cholinergic tract. (atsbio.com)
- Working with both DHEAS and the steroid sulfatase inhibitor DU-14, the authors examined cholinergic function by infusing 0.2 μg of 192-IgG-SAP (Cat. (atsbio.com)
Inhibitor1
- 4) the steroid sulfatase (STS)inhibitor STX64 completely inhibited production of DHT from DHEA-S. (auanet.org)
SULF22
- SULF1 and SULF2 are two endo-sulfatases that can cleave specific 6-O-sulfate groups within the heparan chains. (scielo.br)
- Upon increasing culture times in chicken´s primary skeletal muscle satellite cells, SULF1 and SULF2 expression in 1-week-old chickens was significantly higher than in 2-week-old chickens, suggesting that sulfatases play a key role in satellite cell development. (scielo.br)
Inhibition3
- The significant growth inhibition by the steroid sulfatase and aromatase inhibitors were also observed in the co-culture system. (scirp.org)
- The results indicate that memory associated with contextual fear is facilitated by steroid sulfatase inhibition, but acquisition of spatial memory is impaired by these same lesions. (atsbio.com)
- Inhibition of steroid sulfatase activity by tricyclic coumarin sulphamates. (ox.ac.uk)
Sulfate esters1
- Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfate esters. (wikipedia.org)
Cleave2
- Lysosomal sulfatases cleave a range of sulfated carbohydrates including sulfated glycosaminoglycans and glycolipids. (wikipedia.org)
- Sulfatases cleave sulfate groups from such molecules and constitute a biologically and industrially important group of enzymes. (sb-roscoff.fr)
Aryl sulfatase2
- Human sulfatase 1 (hSulf-1) has aryl sulfatase activity. (oncotarget.com)
- The human sulfatase 1 (hSulf-1) gene encodes an aryl sulfatase. (oncotarget.com)
Deficiency14
- Multiple sulfatase deficiency is a condition that mainly affects the brain, skin, and skeleton. (medlineplus.gov)
- Because the signs and symptoms of multiple sulfatase deficiency vary widely, researchers have split the condition into three types: neonatal, late-infantile, and juvenile. (medlineplus.gov)
- Many of the signs and symptoms of neonatal multiple sulfatase deficiency worsen over time. (medlineplus.gov)
- The late-infantile type is the most common form of multiple sulfatase deficiency. (medlineplus.gov)
- The juvenile type is the rarest form of multiple sulfatase deficiency. (medlineplus.gov)
- Ichthyosis is also common in the juvenile type of multiple sulfatase deficiency. (medlineplus.gov)
- Life expectancy is shortened in individuals with all types of multiple sulfatase deficiency. (medlineplus.gov)
- Multiple sulfatase deficiency is estimated to occur in 1 per million individuals worldwide. (medlineplus.gov)
- Multiple sulfatase deficiency is caused by mutations in the SUMF1 gene. (medlineplus.gov)
- The death of cells in particular tissues, specifically the brain, skeleton, and skin, cause many of the signs and symptoms of multiple sulfatase deficiency. (medlineplus.gov)
- Multiple sulfatase deficiency (MSD) is a very rare and fatal lysosomal storage disease characterized by a clinical phenotype that combines the features of different sulfatase deficiencies (whether lysosomal or not) that can have neonatal (most severe), infantile (most common) and juvenile (rare) presentations with manifestations including hypotonia, coarse facial features, mild deafness, skeletal anomalies, ichthyosis, hepatomegaly, developmental delay, progressive neurologic deterioration and hydrocephalus. (orpha.net)
- X-linked ichthyosis (steroid sulfatase deficiency) is associated with increased risk of attention deficit hyperactivity disorder, autism and social communication deficits. (aber.ac.uk)
- Background: X-linked ichthyosis (XLI) (steroid sulfatase deficiency) is caused by deletions or point mutations of the steroid sulfatase (STS) gene on chromosome Xp22.32. (aber.ac.uk)
- Of the two, the most common is XLRI, which has an estimated incidence of 1:3,000 and is caused by a deficiency of steroid sulfatase, resulting in cholesterol sulfate accumulation in the stratum corneum, retained corneodesmosomes, and reduced corneocyte desquamation, Bunick said. (medscape.com)
Esters1
- We consider dialkyl esters of 5-aminosulfonylisophthanoate-based compounds in our efforts to determine factors involved in determining the overall inhibitory activity against estrone sulfatase (ES). (ingentaconnect.com)
Protein3
- Western Blot: N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody [NBP1-00190] - (0.01ug/ml) staining of Human Bone Marrow lysate (35ug protein in RIPA buffer). (novusbio.com)
- Target Protein: SSDD/Steroid sulfatase. (jjchemitech.com)
- This protein displays arylsulfatase activity at acidic pH, as is typical of lysosomal sulfatases, and has been shown to localize in the lysosomes. (nih.gov)
Arylsulfatase2
- Predicted to enable N-acetylgalactosamine-6-sulfatase activity and arylsulfatase activity. (mcw.edu)
- Arylsulfatase G, a novel lysosomal sulfatase.Frese M.A., Schulz S., Dierks T.J. Biol. (joplink.net)
Estrone sulfate1
- Proliferation of the cancer cells was significantly increased through the steroid sulfatase pathway, which metabolizes androgens, estrone sulfate, and estradiol sulfate as its substrates. (scirp.org)
Inhibitors3
- We also assessed the biological effects of inhibitors of steroid sulfatase and aromatase in the co-culture system compared with usual monocultures. (scirp.org)
- However, its proliferation was significantly decreased by the treatment of steroid sulfatase or aromatase inhibitors. (scirp.org)
- Summary: Steroid sulfatase inhibitors such as dehydroepiandrosterone (DHEAS) have memory-enhancing effects. (atsbio.com)
Structurally related1
- SulfAtlas describes the family and sub-families of structurally-related sulfatases. (sb-roscoff.fr)
Gene encodes1
- This gene encodes N-acetylgalactosamine-6-sulfatase which is a lysosomal exohydrolase required for the degradation of the glycosaminoglycans, keratan sulfate, and chondroitin 6-sulfate. (novusbio.com)
SUMF11
- Sulfatase modifying factor (SUMF1) is a key modifier in connective tissue remodelling, and we have shown previously that several SNPs in SUMF1 are associated with COPD. (lu.se)
Annotation1
- In the context of the explosion of genomic data, the functional annotation of sulfatases is thus particularly prone to flaws and misinterpretations. (sb-roscoff.fr)
Mutations1
- Genetic defects in sulfatase activity can arise through mutations in individual sulfatases and result in certain lysosomal storage disorders with a spectrum of phenotypes ranging from defects in physical and intellectual development. (wikipedia.org)
Lysosome2
- Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. (wikipedia.org)
- Many sulfatases are localized in the lysosome, an acidic digestive organelle found within the cell. (wikipedia.org)
Activity3
- In a phylogenetic analysis of coleopteran and lepidopteran arylsulfatases, the P. chrysocephala GSSs formed a cluster within a coleopteran-specific sulfatase clade distant from the previously identified GSSs of the diamondback moth, Plutella xylostella , suggesting an independent evolution of GSS activity in ermine moths and flea beetles. (nature.com)
- According to a quantitative analysis of 4-methylsulfinylbutyl glucosinolate metabolism in P. chrysocephala , about 8% of the total ingested glucosinolates were detoxified by desulfation, indicating small but significant glucosinolate sulfatase (GSS) activity towards 4-methylsulfinylbutyl glucosinolates in adult beetles 15 . (nature.com)
- Experimental evidences for the activity of new sulfatases will be regularly updated. (sb-roscoff.fr)
Synthesis1
- Two principal pathways have been implicated in the final steps of estrogen synthesis: the steroid sulfatase (STS) and aromatase pathways. (scirp.org)
Classification2
- A classification system allowing for a better prediction of substrate specificity and for setting the limit of functional annotations was therefore urgently needed for sulfatases. (sb-roscoff.fr)
- Matching the Diversity of Sulfated Biomolecules: Creation of a Classification Database for Sulfatases Reflecting Their Substrate Specificity. (sb-roscoff.fr)
Factor2
- Sulfatase Modifying Factor 2/SUMF2 Polyclonal specifically detects Sulfatase Modifying Factor 2/SUMF2 in Human samples. (fishersci.com)
- Detects human Sulfatase Modifying Factor 2/SUMF2 in direct ELISAs and Western blots. (fishersci.com)
Wikipedia1
- Dianabol légal, stéroïde sulfatase - Acheter des stéroïdes anabolisants légaux Dianabol légal Dianabol wikipedia, is anavar a steroid, muscler les lombaires en. (jjchemitech.com)
Cell1
- Detection of 2,4-dichlorophenoxyacetic acid herbicide using a FGE-sulfatase based whole-cell Agrobacterium biosensor. (cri.or.th)
Database1
- Welcome to S ulf A tlas , the database of sulfatases! (sb-roscoff.fr)