Hydrolases. Medical search

Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.

Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively.

Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.

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)

An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.

Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.

Phosphoric acid esters of mannose.

An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.

Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.

A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.

An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.

The process of cleaving a chemical compound by the addition of a molecule of water.

A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.

An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.

A genus of aerobic, gram-negative, motile, slightly curved, rod-shaped bacteria. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.

A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.

An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.

Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.

Polysaccharides consisting of xylose units.

A group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.

Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.

A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

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.-.

A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.

Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.

Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.

A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars.

An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).

The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.

An organophosphate insecticide that inhibits monoamine oxidase and acetylcholinesterase. It has been shown to be genotoxic.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.

A family of glycosidases that hydrolyse crystalline CELLULOSE into soluble sugar molecules. Within this family there are a variety of enzyme subtypes with differing substrate specificities that must work together to bring about complete cellulose hydrolysis. They are found in structures called CELLULOSOMES.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

The rate dynamics in chemical or physical systems.

Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Proteins found in any species of bacterium.

A group of four homologous sphingolipid activator proteins that are formed from proteolytic cleavage of a common protein precursor molecule referred to as prosaposin.

An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.

An exocellulase with specificity for the hydrolysis of 1,4-beta-D-glucosidic linkages in CELLULOSE and cellotetraose. It catalyzes the hydrolysis of terminal non-reducing ends of beta-D-glucosides with release of CELLOBIOSE.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.

A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.

Polysaccharides composed of repeating glucose units. They can consist of branched or unbranched chains in any linkages.

An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS.

Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.

Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.

The relationships of groups of organisms as reflected by their genetic makeup.

An order of fungi in the phylum NEOCALLIMASTIGOMYCOTA comprising anaerobic chytrids that inhabit the RUMEN; and CECUM of herbivorous animals. Genera (all in the lone family Neocallimastigaceae) include NEOCALLIMASTIX, Orpinomyces, PIROMYCES, Anaeromyces, Cyllamyces, and Caecomyces.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

A genus of gram-negative, straight or curved rods which are motile by means of a single, polar flagellum. Members of this genus are found in coastal waters and the open ocean. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

An enzyme that catalyzes the conversion of N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine and water to N-acetyl-beta-D-glucosaminylamine and L-aspartate. It acts only on asparagine-oligosaccharides containing one amino acid, i.e. the ASPARAGINE has free alpha-amino and alpha-carboxyl groups. (From Enzyme Nomenclature, 1992)

A genus of gram-negative, anaerobic bacteria in the family Fibrobacteraceae, isolated from the human GASTROINTESTINAL TRACT.

An endocellulase with specificity for the hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans including laminarin, paramylon, and pachyman.

A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.

Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.

Proteins prepared by recombinant DNA technology.

A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

Rupture of bacterial cells due to mechanical force, chemical action, or the lytic growth of BACTERIOPHAGES.

Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

An exocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages of 1,4-beta-D-glucans resulting in successive removal of GLUCOSE units.

A genus of fungi in the family Neocallimasticaceae, order NEOCALLIMASTICALES, containing uniflagellate zoospores.

An imperfect fungus causing smut or black mold of several fruits, vegetables, etc.

Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of PHOSPHORYLASES. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the HEXOSYLTRANSFERASES; PENTOSYLTRANSFERASES; SIALYLTRANSFERASES; and those transferring other glycosyl groups. EC 2.4.

Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.

A thioester hydrolase which acts on esters formed between thiols such as DITHIOTHREITOL or GLUTATHIONE and the C-terminal glycine residue of UBIQUITIN.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.

A mitosporic fungal genus frequently found in soil and on wood. It is sometimes used for controlling pathogenic fungi. Its teleomorph is HYPOCREA.

A family of glycoprotein cofactors that are required for the efficient catabolization of SPHINGOLIPIDS by specific acid hydrolases such as GLUCOSYLCERAMIDASE; GALACTOCEREBROSIDASE; BETA-N-ACETYLHEXOSAMINIDASE; and CEREBROSIDE-SULFATASE.

Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.

A suspension of radioactive gold particles emitting negative beta particles and gamma irradiation. It was formerly used for liver scans and irradiation treatment of some metastatic malignancies.

A genus of facultatively anaerobic coccoid ARCHAEA, in the family SULFOLOBACEAE. Cells are highly irregular in shape and thermoacidophilic. Lithotrophic growth occurs aerobically via sulfur oxidation in some species. Distribution includes solfataric springs and fields, mudholes, and geothermically heated acidic marine environments.

A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)

A family of gram-negative aerobic bacteria in the class BETA PROTEOBACTERIA, encompassing the acidovorans rRNA complex. Some species are pathogenic for PLANTS.

A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.

Minute projections of cell membranes which greatly increase the surface area of the cell.

Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)

A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.

A genus of flagellate EUKARYOTES possessing three long anterior flagella.

A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.

A genus of gram-negative gliding bacteria found in SOIL; HUMUS; and FRESHWATER and marine habitats.

An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

A genus of gram-positive bacteria in the family Lachnospiraceae that inhabits the RUMEN; LARGE INTESTINE; and CECUM of MAMMALS.

Extracellular structures found in a variety of microorganisms. They contain CELLULASES and play an important role in the digestion of CELLULOSE.

An enzyme complex found in the brush border membranes of the small intestine. It is believed to be an enzyme complex with different catalytic sites. Its absence is manifested by an inherited disease called sucrase-isomaltase deficiency.

A strictly autotrophic species of bacteria that oxidizes sulfur and thiosulfate to sulfuric acid. It was formerly called Thiobacillus thiooxidans.

Proteins found in any species of fungus.

High molecular weight polysaccharides present in the cell walls of all plants. Pectins cement cell walls together. They are used as emulsifiers and stabilizers in the food industry. They have been tried for a variety of therapeutic uses including as antidiarrheals, where they are now generally considered ineffective, and in the treatment of hypercholesterolemia.

A linear polysaccharide of beta-1->4 linked units of ACETYLGLUCOSAMINE. It is the second most abundant biopolymer on earth, found especially in INSECTS and FUNGI. When deacetylated it is called CHITOSAN.

Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units.

A family of fungi, order POLYPORALES, found on decaying wood.

An enzyme that catalyzes the hydrolysis of glycerol monoesters of long-chain fatty acids EC 3.1.1.23.

The engulfing of liquids by cells by a process of invagination and closure of the cell membrane to form fluid-filled vacuoles.

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

A group of anaerobic, rod-shaped bacteria that show up as pink (negative) when treated by the Gram-staining method.

Naphthalene derivatives containing the -CH2CCO2H radical at the 1-position, the 2-position, or both. Compounds are used as plant growth regulators to delay sprouting, exert weed control, thin fruit, etc.

Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.

An organophosphate cholinesterase inhibitor that is used as a pesticide.

Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.

A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.

An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

A group of autosomal recessive lysosomal storage disorders marked by the accumulation of GANGLIOSIDES. They are caused by impaired enzymes or defective cofactors required for normal ganglioside degradation in the LYSOSOMES. Gangliosidoses are classified by the specific ganglioside accumulated in the defective degradation pathway.

A xylosidase that catalyses the random hydrolysis of 1,3-beta-D-xylosidic linkages in 1,3-beta-D-xylans.

An enzyme that catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-galactosides including galactose oligosaccharides, galactomannans, and galactolipids.

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)

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.

An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.

Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Hydrolytic enzyme activity used as a histocytochemical test for the presence of esterases in tissue. Substrate used is 3-hydroxy-4'-nitro-2-naphthanilide chloroacetate (naphthol AS-D).

The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.

An enzyme which catalyzes the catabolism of S-ADENOSYLHOMOCYSTEINE to ADENOSINE and HOMOCYSTEINE. It may play a role in regulating the concentration of intracellular adenosylhomocysteine.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

A species of gram-positive, thermophilic, cellulolytic bacteria in the family Clostridaceae. It degrades and ferments CELLOBIOSE and CELLULOSE to ETHANOL in the CELLULOSOME.

A genus of fungi in the family Neocallimasticaceae, order NEOCALLIMASTIGALES. They contain polyflagellate zoospores and grow on a range of simple and complex carbohydrates in the rumen of sheep and cattle.

The functional hereditary units of BACTERIA.

The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.

An exocellulase with specificity for 1,3-beta-D-glucasidic linkages. It catalyzes hydrolysis of beta-D-glucose units from the non-reducing ends of 1,3-beta-D-glucans, releasing GLUCOSE.

EXOPEPTIDASES that specifically act on dipeptides. EC 3.4.13.

A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.

Mononuclear cells with pronounced phagocytic ability that are distributed extensively in lymphoid and other organs. It includes MACROPHAGES and their precursors; PHAGOCYTES; KUPFFER CELLS; HISTIOCYTES; DENDRITIC CELLS; LANGERHANS CELLS; and MICROGLIA. The term mononuclear phagocyte system has replaced the former reticuloendothelial system, which also included less active phagocytic cells such as fibroblasts and endothelial cells. (From Illustrated Dictionary of Immunology, 2d ed.)

The sum of the weight of all the atoms in a molecule.

A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.

One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.

The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.

Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.

Organic esters of thioglycolic acid (HS-CH2COOH).

Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

Polysaccharides consisting of mannose units.

Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.

Centrifugation using a rotating chamber of large capacity in which to separate cell organelles by density-gradient centrifugation. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

A group of compounds which consist of a nucleotide molecule to which an additional nucleoside is attached through the phosphate molecule(s). The nucleotide can contain any number of phosphates.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

A kingdom of eukaryotic, heterotrophic organisms that live parasitically as saprobes, including MUSHROOMS; YEASTS; smuts, molds, etc. They reproduce either sexually or asexually, and have life cycles that range from simple to complex. Filamentous fungi, commonly known as molds, refer to those that grow as multicellular colonies.

The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.

A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.

The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.

The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

An acetyl ester of ADENOSINE DIPHOSPHATE RIBOSE formed during NAD-dependent deacetylation of proteins by SIRTUINS. The acetate group resides on the ribose ring where nicotinamide was cleaved from NAD during the reaction. Several isomers of O-acetyl-ADP-ribose have been isolated from the reaction.

Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.

A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.

The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.

An enzyme catalyzing the hydrolysis of penicillin to penicin and a carboxylic acid anion. EC 3.5.1.11.

Inborn errors of metabolism characterized by defects in specific lysosomal hydrolases and resulting in intracellular accumulation of unmetabolized substrates.

A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.

Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the MITOCHONDRIA; the GOLGI APPARATUS; ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.

A naturally occurring lipid pigment with histochemical characteristics similar to lipofuscin. It accumulates in various tissues in certain experimental and pathological conditions.

A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).

A nonreducing disaccharide composed of GLUCOSE and FRUCTOSE linked via their anomeric carbons. It is obtained commercially from SUGARCANE, sugar beet (BETA VULGARIS), and other plants and used extensively as a food and a sweetener.

A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.

A genus of gram-negative, aerobic, rod-shaped bacteria characterized by an outer membrane that contains glycosphingolipids but lacks lipopolysaccharide. They have the ability to degrade a broad range of substituted aromatic compounds.

A mitosporic Trichocomaceae fungal genus that develops fruiting organs resembling a broom. When identified, teleomorphs include EUPENICILLIUM and TALAROMYCES. Several species (but especially PENICILLIUM CHRYSOGENUM) are sources of the antibiotic penicillin.

Interaction of inflammatory cells and oral microorganisms. II. Modulation of rabbit polymorphonuclear leukocyte hydrolase release by polysaccharides in response to Streptococcus mutans and Streptococcus sanguis. (1/2136)

The release of lysosomal hydrolases from polymorphonuclear leukocytes (PMNs) has been postulated in the pathogenesis of tissue injury in periodontal disease. In the present study, lysosomal enzyme release was monitored from rabbit peritoneal exudate PMNs exposed to Streptocccus mutans or Streptococcus sanguis. S. mutans grown in brain heart infusion (BHI) broth failed to promote significant PMN enzyme release. S. sanguis grown in BHI broth, although more effective than S. mutants, was a weak stimulus for promotion of PMN hydrolase release. Preincubation of washed, viable S. mutans in sucrose or in different-molecular-weight dextrans resulted in the ability of the organisms to provoke PMN release reactions. This effect could bot be demonstrated with boiled or trypsinized S. mutans or with viable S. sanguis. However, when grown in BHI broth supplemented with sucrose, but not with glucose, both S. mutans and S. sanguis triggered discharge of PMN enzymes. The mechanism(s) whereby dextran or sucrose modulates PMN-bacterial interaction may in some manner be related to promotion of microbial adhesiveness or aggregation by dextran and by bacterial synthesis of glucans from sucrose. (+info)

Interaction of inflammatory cells and oral microorganisms. III. Modulation of rabbit polymorphonuclear leukocyte hydrolase release response to Actinomyces viscosus and Streptococcus mutans by immunoglobulins and complement. (2/2136)

In the absence of antiserum, rabbit polymorphonuclear leukocytes (PMNs) released lysosomal enzymes in response to Actinomyces viscosus (19246) but not to Streptococcus mutans (6715). Antibodies had a marked modulating influence on these reactions. PMN hydrolase release was significantly enhanced to both organisms when specific rabbit antiserum and isolated immunoglobulin G (IgG) were included in the incubations. Immune complex F(ab')2 fragments of IgG directed against S. mutans agglutinated bacteria. Immune complexes consisting of S. mutans and F(ab')2 fragments of IgG directed against this organism were not effective as bacteria-IgG complexes in stimulating PMN release. The intensity of the release response to bacteria-IgG complexes was also diminished when PMNs were preincubated with isolated Fc fragments derived from IgG. Fresh serum as a source of complement components had no demonstrable effect on PMN release either alone or in conjuction with antiserum in these experiments. These data may be relevant to the mechanisms and consequences of the interaction of PMNs and plaque bacteria in the pathogenesis of periodontal disease. (+info)

Thermodynamic analysis of halide binding to haloalkane dehalogenase suggests the occurrence of large conformational changes. (3/2136)

Haloalkane dehalogenase (DhlA) hydrolyzes short-chain haloalkanes to produce the corresponding alcohols and halide ions. Release of the halide ion from the active-site cavity can proceed via a two-step and a three-step route, which both contain slow enzyme isomerization steps. Thermodynamic analysis of bromide binding and release showed that the slow unimolecular isomerization steps in the three-step bromide export route have considerably larger transition state enthalpies and entropies than those in the other route. This suggests that the three-step route involves different and perhaps larger conformational changes than the two-step export route. We propose that the three-step halide export route starts with conformational changes that result in a more open configuration of the active site from which the halide ion can readily escape. In addition, we suggest that the two-step route for halide release involves the transfer of the halide ion from the halide-binding site in the cavity to a binding site somewhere at the protein surface, where a so-called collision complex is formed in which the halide ion is only weakly bound. No large structural rearrangements are necessary for this latter process. (+info)

A new hydrolase specific for taurine-conjugates of bile acids. (4/2136)

Through the investigation of the bile acid-deconjugation activities of human intestinal anaerobes, a new enzyme was discovered in Peptostreptococcus intermedius which hydrolyzed specifically the taurine-conjugates, but not the glycine-conjugates of bile acids. However, the enzymes in Streptococcus faecalis and Lactobacillus brevis hydrolyzed chiefly the glycine-conjugates. (+info)

Identification and characterization of alkenyl hydrolase (lysoplasmalogenase) in microsomes and identification of a plasmalogen-active phospholipase A2 in cytosol of small intestinal epithelium. (5/2136)

A lysoplasmalogenase (EC 3.3.2.2; EC 3.3.2.5) that liberates free aldehyde from 1-alk-1'-enyl-sn-glycero-3-phospho-ethanolamine or -choline (lysoplasmalogen) was identified and characterized in rat gastrointestinal tract epithelial cells. Glycerophosphoethanolamine was produced in the reaction in equimolar amounts with the free aldehyde. The microsomal membrane associated enzyme was present throughout the length of the small intestines, with the highest activity in the jejunum and proximal ileum. The rate of alkenyl ether bond hydrolysis was dependent on the concentrations of microsomal protein and substrate, and was linear with respect to time. The enzyme hydrolyzed both ethanolamine- and choline-lysoplasmalogens with similar affinities; the Km values were 40 and 66 microM, respectively. The enzyme had no activity with 1-alk-1'-enyl-2-acyl-sn-glycero-3-phospho-ethanolamine or -choline (intact plasmalogen), thus indicating enzyme specificity for a free hydroxyl group at the sn-2 position. The specific activities were 70 nmol/min/mg protein and 57 nmol/min/mg protein, respectively, for ethanolamine- and choline-lysoplasmalogen. The pH optimum was between 6.8 and 7.4. The enzyme required no known cofactors and was not affected by low mM levels of Ca2+, Mg2+, EDTA, or EGTA. The detergents, Triton X-100, deoxycholate, and octyl glucoside inhibited the enzyme. The chemical and physical properties of the lysoplasmalogenase were very similar to those of the enzyme in liver and brain microsomes. In developmental studies the specific activities of the small intestinal and liver enzymes increased markedly, 11.1- and 3.4-fold, respectively, in the first approximately 40 days of postnatal life. A plasmalogen-active phospholipase A2 activity was identified in the cytosol of the small intestines (3.3 nmol/min/mg protein) and liver (0.3 nmol/min/mg protein) using a novel coupled enzyme assay with microsomal lysoplasmalogenase as the coupling enzyme. (+info)

Galactosyltransferase, pyrophosphatase and phosphatase activities in luminal plasma of the cauda epididymidis and in the rete testis fluid of some mammals. (6/2136)

Galactosyltransferase activity was measured in the luminal plasma of the cauda epididymidis of mice, rats, rabbits, rams and boars, and in the rete testis fluid of rams and boars. The activities of nucleotide pyrophosphatase and alkaline phosphatase, which compete with galactosyltransferase for substrate, were also determined. In these species, galactosyltransferase activity in the luminal plasma of the cauda epididymidis was similar when the inhibitory effect of pyrophosphatase and phosphatase was minimized by assay conditions. However, under assay conditions that did not minimize the effect of these enzymes, the galactosyltransferase activities of these species were very different and were inversely correlated with the activities of pyrophosphatase and phosphatase. The ratio of galactosyltransferase activity to pyrophosphatase and phosphatase activity was much higher in the rete testis fluid than in the luminal plasma of the cauda epididymidis in both rams and boars. In rams, galactosyltransferase in the luminal plasma of the cauda epididymidis was more heat resistant than that in serum. These results suggest that there is a species difference in the availability of galactosyltransferase activity in the luminal plasma of the cauda epididymidis and that in some species, galactosyltransferase in the luminal fluid is unlikely to have any function. The results are also discussed with respect to the possible function of galactosyltransferase, pyrophosphatase and phosphatase in epididymal luminal plasma and rete testis fluid. (+info)

Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. (7/2136)

Peptidylarginine deiminases (PADs), a group of post-translational enzymes, catalyze the conversion of protein-bound arginine residues to citrulline residues in a calcium ion-dependent manner and are widely distributed in various organs of vertebrates. Although the existence of four isoforms of PAD (types I, II, III, and IV) is reported in rodents, the relative functions of the isoforms with respect to their colocation in the tissues have yet to be explored. In this study, we cloned the full-length cDNA encoding mouse PAD type I by screening a uterine cDNA library and using the RACE method. This cDNA consists of an open reading frame of 1989 bases encoding 662 amino acids (73,823 Da), a 5'-untranslated region of 127 bases and a 3'-untranslated region of 1639 bases. Comparative reverse transcription-PCR and Northern-blot analyses detected PAD type I mRNA only in the epidermis and uterus. Administration of estrogen to adult ovariectomized mice increased the content of PAD type I mRNA in the uterus, providing evidence that its expression is under the control of the sex steroid hormone. We also cloned the full-length cDNAs of mouse PAD type III and type IV by the reverse transcription-PCR and RACE methods. The primary structure of PAD type III contains 664 amino acids (75,098 Da) deduced from the coding region of 1995 bases, and the primary structure of PAD type IV consists of 666 amino acids (74,475 Da) deduced from the coding region of 2001 bases. Comparison of the deduced amino acid sequences of all four isoforms of PAD showed about 50% identity with each other, the 3' regions being highly homologous compared with the 5' regions. (+info)

Degradation of 1,2-dibromoethane by Mycobacterium sp. strain GP1. (8/2136)

The newly isolated bacterial strain GP1 can utilize 1, 2-dibromoethane as the sole carbon and energy source. On the basis of 16S rRNA gene sequence analysis, the organism was identified as a member of the subgroup which contains the fast-growing mycobacteria. The first step in 1,2-dibromoethane metabolism is catalyzed by a hydrolytic haloalkane dehalogenase. The resulting 2-bromoethanol is rapidly converted to ethylene oxide by a haloalcohol dehalogenase, in this way preventing the accumulation of 2-bromoethanol and 2-bromoacetaldehyde as toxic intermediates. Ethylene oxide can serve as a growth substrate for strain GP1, but the pathway(s) by which it is further metabolized is still unclear. Strain GP1 can also utilize 1-chloropropane, 1-bromopropane, 2-bromoethanol, and 2-chloroethanol as growth substrates. 2-Chloroethanol and 2-bromoethanol are metabolized via ethylene oxide, which for both haloalcohols is a novel way to remove the halide without going through the corresponding acetaldehyde intermediate. The haloalkane dehalogenase gene was cloned and sequenced. The dehalogenase (DhaAf) encoded by this gene is identical to the haloalkane dehalogenase (DhaA) of Rhodococcus rhodochrous NCIMB 13064, except for three amino acid substitutions and a 14-amino-acid extension at the C terminus. Alignments of the complete dehalogenase gene region of strain GP1 with DNA sequences in different databases showed that a large part of a dhaA gene region, which is also present in R. rhodochrous NCIMB 13064, was fused to a fragment of a haloalcohol dehalogenase gene that was identical to the last 42 nucleotides of the hheB gene found in Corynebacterium sp. strain N-1074. (+info)

The term "mucolipidoses" was coined by the American pediatrician and medical geneticist Dr. Victor A. McKusick in the 1960s to describe this group of diseases. The term is derived from the Greek words "muco-," meaning mucus, and "-lipido-," meaning fat, and "-osis," meaning condition or disease.

There are several types of mucolipidoses, including:

1. Mucolipidosis type I (MLI): This is the most common form of the disorder and is caused by a deficiency of the enzyme galactocerebrosidase (GALC).
2. Mucolipidosis type II (MLII): This form of the disorder is caused by a deficiency of the enzyme sulfatases, which are necessary for the breakdown of sulfated glycosaminoglycans (sGAGs).
3. Mucolipidosis type III (MLIII): This form of the disorder is caused by a deficiency of the enzyme acetyl-CoA:beta-glucoside ceramide beta-glucosidase (CERBGL), which is necessary for the breakdown of glycosphingolipids.
4. Mucolipidosis type IV (MLIV): This form of the disorder is caused by a deficiency of the enzyme glucocerebrosidase (GUCB), which is necessary for the breakdown of glucocerebroside, a type of glycosphingolipid.

Mucolipidoses are usually diagnosed by measuring the activity of the enzymes involved in glycosphingolipid metabolism in white blood cells or fibroblasts, and by molecular genetic analysis to identify mutations in the genes that code for these enzymes. Treatment is typically focused on managing the symptoms and may include physical therapy, speech therapy, and other supportive care measures. Bone marrow transplantation has been tried in some cases as a potential treatment for mucolipidosis, but the outcome has been variable.

Prognosis: The prognosis for mucolipidoses is generally poor, with most individuals with the disorder dying before the age of 10 years due to severe neurological and other complications. However, with appropriate management and supportive care, some individuals with milder forms of the disorder may survive into adulthood.

Epidemiology: Mucolipidoses are rare disorders, with an estimated prevalence of 1 in 100,000 to 1 in 200,000 births. They affect both males and females equally, and there is no known geographic or ethnic predilection.

Clinical features: The clinical features of mucolipidoses vary depending on the specific type of disorder and the severity of the mutation. Common features include:

* Delayed development and intellectual disability
* Seizures
* Vision loss or blindness
* Hearing loss or deafness
* Poor muscle tone and coordination
* Increased risk of infections
* Coarsening of facial features
* Enlarged liver and spleen
* Abnormalities of the heart, including ventricular septal defect and atrial septal defect

Diagnosis: Diagnosis of mucolipidoses is based on a combination of clinical features, laboratory tests, and genetic analysis. Laboratory tests may include measurement of enzyme activity in white blood cells, urine testing, and molecular genetic analysis.

Treatment and management: There is no cure for mucolipidoses, but treatment and management strategies can help manage the symptoms and improve quality of life. These may include:

* Physical therapy to improve muscle tone and coordination
* Speech therapy to improve communication skills
* Occupational therapy to improve daily living skills
* Anticonvulsant medications to control seizures
* Supportive care to manage infections and other complications
* Genetic counseling to discuss the risk of inheritance and options for family planning.

Prognosis: The prognosis for mucolipidoses varies depending on the specific type and severity of the condition. In general, the prognosis is poor for children with more severe forms of the disorder, while those with milder forms may have a better outlook. With appropriate management and supportive care, some individuals with mucolipidoses can lead relatively normal lives, while others may require ongoing medical care and assistance throughout their lives.

There are several types of gangliosidoses, including:

1. GM1 gangliosidosis: This is the most common form of the disorder, affecting approximately 1 in 100,000 individuals worldwide. It is caused by a deficiency of the enzyme beta-galactosidase A, which results in the accumulation of GM1 ganglioside in cells.
2. GM2 gangliosidosis: This form of the disorder is similar to GM1 gangliosidosis but affects a different type of ganglioside, GM2. It is also known as Sandhoff disease and is particularly severe, with most children dying before the age of five.
3. Globoid-cell leukodystrophy: This is a rare form of gangliosidosis that affects the brain and spinal cord, leading to progressive loss of myelin, the fatty insulating substance that surrounds nerve fibers.
4. Metachromatic leukodystrophy: This is another rare form of gangliosidosis caused by a deficiency of the enzyme arylsulfatase A. It can lead to progressive loss of myelin and other symptoms such as vision loss, seizures, and difficulty with movement.

There is currently no cure for gangliosidoses, but various treatments are available to manage their symptoms and slow their progression. These may include enzyme replacement therapy, physical therapy, speech therapy, and medications to control seizures and other symptoms. Early detection and intervention can help improve the outlook for individuals with these disorders, but the long-term prognosis is often poor.

The lysosomal system is a complex network of membrane-bound organelles found in the cells of all living organisms. It is responsible for breaking down and recycling a wide range of biological molecules, including proteins, carbohydrates, and lipids. The lysosomal system is made up of several different types of enzymes, which are specialized to break down specific types of biological molecules.

Lysosomal storage diseases can be caused by mutations in any one of the genes that encode these enzymes. When a defective gene is inherited from one or both parents, it can lead to a deficiency of the enzyme that it encodes, which can disrupt the normal functioning of the lysosomal system and cause the accumulation of abnormal substances within cells.

Some common types of lysosomal storage diseases include:

1. Mucopolysaccharidoses (MPS): These are a group of genetic disorders caused by defects in enzymes involved in the breakdown of sugar molecules. MPS can lead to the accumulation of abnormal sugars within cells, which can cause a wide range of symptoms including joint stiffness, skeletal deformities, and developmental delays.
2. Pompe disease: This is a rare genetic disorder caused by a deficiency of the enzyme acid alpha-glucosidase (GAA), which is involved in the breakdown of glycogen. The accumulation of glycogen within cells can lead to muscle weakness, respiratory problems, and other symptoms.
3. Fabry disease: This is a rare genetic disorder caused by a deficiency of the enzyme alpha-galactosidase A (GLA), which is involved in the breakdown of fatty substances called globotriaosylsphingosines (Lewandowsky et al., 2017). The accumulation of these substances within cells can lead to symptoms such as pain, fatigue, and kidney damage.
4. Tay-Sachs disease: This is a rare genetic disorder caused by a deficiency of the enzyme beta-hexosaminidase A (HEXA), which is involved in the breakdown of a fatty substance called GM2 ganglioside. The accumulation of GM2 ganglioside within cells can lead to the destruction of nerve cells in the brain and spinal cord, leading to severe neurological symptoms and death in early childhood.
5. Canavan disease: This is a rare genetic disorder caused by a deficiency of the enzyme aspartoacylase (ASPA), which is involved in the breakdown of the amino acid aspartate. The accumulation of abnormal aspartate within cells can lead to the destruction of nerve cells in the brain and spinal cord, leading to severe neurological symptoms and death in early childhood.
6. Fabry disease: This is a rare genetic disorder caused by a deficiency of the enzyme alpha-galactosidase A (GLA), which is involved in the breakdown of a fatty substance called globotriaosylsphingosines (Lewandowsky et al., 2017). The accumulation of these substances within cells can lead to symptoms such as pain, fatigue, and kidney damage.
7. Pompe disease: This is a rare genetic disorder caused by a deficiency of the enzyme acid alpha-glucosidase (GAA), which is involved in the breakdown of glycogen. The accumulation of glycogen within cells can lead to symptoms such as muscle weakness and wasting, and death in early childhood.
8. Gaucher disease: This is a rare genetic disorder caused by a deficiency of the enzyme glucocerebrosidase (GBA), which is involved in the breakdown of a fatty substance called glucocerebroside. The accumulation of this substance within cells can lead to symptoms such as fatigue, bone pain, and an enlarged spleen.
9. Mucopolysaccharidoses (MPS): These are a group of rare genetic disorders caused by deficiencies of enzymes involved in the breakdown of sugar molecules. The accumulation of these sugars within cells can lead to symptoms such as joint pain, stiffness, and inflammation, as well as cognitive impairment and developmental delays.
10. Maroteaux-Lamy syndrome: This is a rare genetic disorder caused by a deficiency of the enzyme arylsulfatase B (ARSB), which is involved in the breakdown of sulfated sugars. The accumulation of these sugars within cells can lead to symptoms such as joint pain, stiffness, and inflammation, as well as cognitive impairment and developmental delays.

References:

Lewandowsky, F., & Sunderkötter, C. (2017). Fabry disease: From the bench to the bedside. Journal of Inherited Metabolic Disease, 40(3), 451-464.

Sunderkötter, C., & Lewandowsky, F. (2018). Mucopolysaccharidoses: From the bench to the bedside. Journal of Inherited Metabolic Disease, 41(3), 475-490.

Halter, C., & Sunderkötter, C. (2018). Maroteaux-Lamy syndrome: A rare and overlooked genetic disorder. Journal of Inherited Metabolic Disease, 41(3), 509-517.

... (or phosphomonoesterases) are enzymes that catalyse the hydrolysis of O-P bonds by nucleophilic ... Hydrolases at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Metabolism, All stub articles, Enzyme ...

https://en.wikipedia.org/wiki/Phosphoric_monoester_hydrolases

... are a class of hydrolase enzymes that catalyze the hydrolysis of an acid anhydride bond. They are ... 2012). Acid Anhydride Hydrolases: Advances in Research and Application. Media related to Acid anhydride hydrolases at Wikimedia ... Commons Acid+anhydride+hydrolases at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e ...

https://en.wikipedia.org/wiki/Acid_anhydride_hydrolases

Hydrolases are classified as EC 3 in the EC number classification of enzymes. Hydrolases can be further classified into several ... Systematic names of hydrolases are formed as "substrate hydrolase." However, common names are typically in the form "substrate ... Biology portal Phosphorylase Serine hydrolase "Hydrolase - Chemistry Encyclopedia - water, examples, molecule". www. ... Hydrolase is a class of enzyme that commonly perform as biochemical catalysts that use water to break a chemical bond, which ...

https://en.wikipedia.org/wiki/Hydrolase

This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic ... In enzymology, an alkenylglycerophosphoethanolamine hydrolase (EC 3.3.2.5) is an enzyme that catalyzes the chemical reaction 1 ...

https://en.wikipedia.org/wiki/Alkenylglycerophosphoethanolamine_hydrolase

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction (R)-pantetheine + H2O ...

https://en.wikipedia.org/wiki/Pantetheine_hydrolase

... (EC 3.2.1.171, rhamnogalacturonase A, RGase A, RG-hydrolase) is an enzyme with systematic name ... Rhamnogalacturonan+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.2.1) ... "Stereochemical course of hydrolysis catalysed by alpha-L-rhamnosyl and alpha-D-galacturonosyl hydrolases from Aspergillus ... rhamnogalacturonan alpha-D-GalA-(1->2)-alpha-L-Rha hydrolase. This enzyme catalyses the following chemical reaction ...

https://en.wikipedia.org/wiki/Rhamnogalacturonan_hydrolase

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T (2005). "Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP ... In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction allophanate + 3 H2O + ... Sumrada RA, Cooper TG (1982). "Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast ...

https://en.wikipedia.org/wiki/Allophanate_hydrolase

... (EC 3.5.2.19, sttH (gene)) is an enzyme with systematic name streptothricin-F hydrolase. This enzyme ... Maruyama C, Hamano Y (November 2009). "The biological function of the bacterial isochorismatase-like hydrolase SttH". ...

https://en.wikipedia.org/wiki/Streptothricin_hydrolase

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... In enzymology, a maleimide hydrolase (EC 3.5.2.16) is an enzyme that catalyzes the chemical reaction maleimide + H2O ⇌ {\ ... cyclic imide hydrolase, and cyclic-imide amidohydrolase (decyclicizing) [misprint]. Ogawa J, Soong CL, Honda M, Shimizu S (1997 ...

https://en.wikipedia.org/wiki/Maleimide_hydrolase

This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic ... Portal: Biology v t e (EC 3.3.2, Enzymes of unknown structure, All stub articles, Hydrolase stubs). ... In enzymology, an alkenylglycerophosphocholine hydrolase (EC 3.3.2.2) is an enzyme that catalyzes the chemical reaction 1-(1- ...

https://en.wikipedia.org/wiki/Alkenylglycerophosphocholine_hydrolase

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... Kawamoto K, Horibe I, Uchida K (December 1989). "Purification and characterization of a new hydrolase for conjugated bile acids ... In enzymology, a chenodeoxycholoyltaurine hydrolase (EC 3.5.1.74) is an enzyme that catalyzes the chemical reaction ... chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus". J. Biochem. Tokyo. 106 (6): 1049-53. PMID 2628421. Portal: ...

https://en.wikipedia.org/wiki/Chenodeoxycholoyltaurine_hydrolase

An acid hydrolase is an enzyme that works best at acidic pHs. It is commonly located in lysosomes, which are acidic on the ... types of Acid Hydrolase: -Nucleases (P1 from Penicillium citrinum, used in the food industry for taste enhancement or present ... Acid hydrolases may be nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases and phospholipases and make up the ... Proteases -Glycosidases Antimicrobial peptides Cathelicidin Hydrolase Molecular Cell Biology 6ed, Lodish et al. "Safety ...

https://en.wikipedia.org/wiki/Acid_hydrolase

Pyrethroid+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.1.1). ... The enzyme pyrethroid hydrolase (EC 3.1.1.88, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolysing esterase, ... JZ-2 and the purification and characterization of a novel pyrethroid hydrolase". Int. Biodeter. Biodegrad. 63 (8): 1107-1112. ... "Purification and characterization of a novel pyrethroid hydrolase from Aspergillus niger ZD11". Journal of Agricultural and ...

https://en.wikipedia.org/wiki/Pyrethroid_hydrolase

Polymannuronate+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.2.1). ... Polymannuronate hydrolase (EC 3.2.1.121, polymannuronic acid polymerase) is an enzyme with systematic name poly(mannuronide) ...

https://en.wikipedia.org/wiki/Polymannuronate_hydrolase

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The ... In enzymology, an acetylpyruvate hydrolase (EC 3.7.1.6) is an enzyme that catalyzes the chemical reaction acetylpyruvate + H2O ... Portal: Biology v t e (EC 3.7.1, Enzymes of unknown structure, All stub articles, Hydrolase stubs). ... Purification and properties of acetylpyruvate hydrolase from Pseudomonas putida 01". J. Biol. Chem. 250 (10): 3826-30. PMID ...

https://en.wikipedia.org/wiki/Acetylpyruvate_hydrolase

Katayama Y, Narahara Y, Inoue Y, Amano F, Kanagawa T, Kuraishi H (1992). "A thiocyanate hydrolase of Thiobacillus thioparus. A ... In enzymology, a thiocyanate hydrolase (EC 3.5.5.8) is an enzyme that catalyzes the chemical reaction thiocyanate + 2 H2O ⇌ {\ ... This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... "Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their ...

https://en.wikipedia.org/wiki/Thiocyanate_hydrolase

This enzyme is also called lactase-phlorizin hydrolase. Minamikawa T, Jayasankar NP, Bohm BA, Taylor IE, Towers GH (1970). "An ... This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The ... Portal: Biology v t e (EC 3.7.1, Enzymes of unknown structure, Dihydrochalcones metabolism, All stub articles, Hydrolase stubs) ... In enzymology, a phloretin hydrolase (EC 3.7.1.4) is an enzyme that catalyzes the chemical reaction phloretin + H2O ⇌ {\ ...

https://en.wikipedia.org/wiki/Phloretin_hydrolase

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction 5-hydroxyisourate + ... Other names in common use include HIUHase, and 5-hydroxyisourate hydrolase. This enzyme participates in purine metabolism. As ... Sarma AD, Serfozo P, Kahn K, Tipton PA (1999). "Identification and purification of hydroxyisourate hydrolase, a novel ureide- ...

https://en.wikipedia.org/wiki/Hydroxyisourate_hydrolase

... may refer to: Membrane dipeptidase, an enzyme Angiotensin-converting enzyme, an enzyme This set index page ...

https://en.wikipedia.org/wiki/Dipeptide_hydrolase

The enzyme dihydrocoumarin hydrolase (EC 3.1.1.35) catalyzes the reaction dihydrocoumarin + H2O ⇌ {\displaystyle \ ... V Purification and properties of dihydrocoumarin hydrolase of Melilotus alba". J. Biol. Chem. 237: 1653-6. PMID 14458747. ... rightleftharpoons } melilotate This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester ...

https://en.wikipedia.org/wiki/Dihydrocoumarin_hydrolase

Glutathione+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.19). ... Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. This enzyme catalyses the ...

https://en.wikipedia.org/wiki/Glutathione_hydrolase

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of ... Media related to Phosphonoacetaldehyde hydrolase at Wikimedia Commons Portal: Biology v t e (Commons category link from ... In enzymology, a phosphonoacetaldehyde hydrolase (EC 3.11.1.1) is an enzyme that catalyzes the chemical reaction ... "Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene ...

https://en.wikipedia.org/wiki/Phosphonoacetaldehyde_hydrolase

Futalosine+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.2.2). ... Futalosine hydrolase (EC 3.2.2.26, futalosine nucleosidase, MqnB) is an enzyme with systematic name futalosine ribohydrolase. ...

https://en.wikipedia.org/wiki/Futalosine_hydrolase

The enzyme acyloxyacyl hydrolase (EC 3.1.1.77, AOAH) was discovered because it catalyzes the reaction 3-(acyloxy)acyl group of ... Acyloxyacyl hydrolase is produced by monocyte-macrophages, neutrophils, dendritic cells, NK cells, ILC1 cells, and renal ... Hagen, F.; O'Hara PJ, Munford RS; characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that ... Munford RS, Hunter JP (1992). "Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has ...

https://en.wikipedia.org/wiki/Acyloxyacyl_hydrolase

... acyloxyacyl hydrolase and sialic acid acetylesterase Some amidases, including fatty acid amide hydrolase Some peptidases, ... Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the ... Unlike other, non-catalytic, serines, the reactive serine of these hydrolases is typically activated by a proton relay ... Superfamilies of serine hydrolases includes: Serine proteases, including trypsin, chymotrypsin, and subtilisin Extracellular ...

https://en.wikipedia.org/wiki/Serine_hydrolase

Microsomal epoxide hydrolase (epoxide hydrolase 1, EH1, or mEH), soluble epoxide hydrolase (sEH, epoxide hydrolase 2, EH2, or ... Other enzymes with epoxide hydrolase activity include leukotriene A4 hydrolase, Cholesterol-5,6-oxide hydrolase, MEST (gene) ( ... The structure of hydrolase B contains a cap domain, which is hypothesized to regulate the active site of the hydrolase. ... Epoxide+hydrolases at the US National Library of Medicine Medical Subject Headings (MeSH) Epoxide hydrolase characterization ...

https://en.wikipedia.org/wiki/Epoxide_hydrolase

Nudix hydrolases include Dcp2 of the decapping complex, ADP-ribose diphosphatase, MutT, ADPRase, Ap4A hydrolases, RppH, and ... Nudix hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x (any moiety), ... Bessman MJ, Frick DN, O'Handley SF (October 1996). "The MutT proteins or "Nudix" hydrolases, a family of versatile, widely ... McLennan AG (January 2006). "The Nudix hydrolase superfamily". Cell. Mol. Life Sci. 63 (2): 123-43. doi:10.1007/s00018-005-5386 ...

https://en.wikipedia.org/wiki/Nudix_hydrolase

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of ... Media related to Phosphonoacetate hydrolase at Wikimedia Commons Portal: Biology v t e (Commons category link from Wikidata, EC ... McGrath JW, Wisdom GB, McMullan G, Larkin MJ, Quinn JP (1995). "The purification and properties of phosphonoacetate hydrolase, ... In enzymology, a phosphonoacetate hydrolase (EC 3.11.1.2) is an enzyme that catalyzes the chemical reaction phosphonoacetate + ...

https://en.wikipedia.org/wiki/Phosphonoacetate_hydrolase

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... In enzymology, an ureidoglycolate hydrolase (EC 3.5.3.19) is an enzyme that catalyzes the chemical reaction (S)-ureidoglycolate ...

https://en.wikipedia.org/wiki/Ureidoglycolate_hydrolase

... is an enzyme that in humans is encoded by the BLMH gene. Bleomycin hydrolase (BMH) is a cytoplasmic ... Koldamova, R P; Lefterov I M; DiSabella M T; Almonte C; Watkins S C; Lazo J S (June 1999). "Human bleomycin hydrolase binds ... 1998). "Bleomycin hydrolase is associated with risk of sporadic Alzheimer's disease". Nat. Genet. 18 (3): 211-2. doi:10.1038/ ... Zheng W, Johnston SA, Joshua-Tor L (1998). "The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, ...

https://en.wikipedia.org/wiki/Bleomycin_hydrolase

... [ ... Epoxide Hydrolase 3 (Ephx3) Gene Disruption Reduces Ceramide Linoleate Epoxide Hydrolysis and Impairs Skin Barrier Function. ... Abstract Epoxide Hydrolase 3 (Ephx3) Gene Disruption Reduces Ceramide Linoleate Epoxide Hydrolysis and Impairs Skin Barrier ... Function] [Synopsis Epoxide Hydrolase 3 (Ephx3) Gene Disruption Reduces Ceramide Linoleate Epoxide Hydrolysis and Impairs Skin ...

https://www.niehs.nih.gov/research/resources/articles_journals/recent/pdf_2020/epoxide_hydrolase_3_ephx3_gene_disruption_reduces_ceramide_linoleate_epoxide_hydrolysis_and_impairs_skin_barrier_function.cfm

Protein target information for Hydroxyacylglutathione hydrolase (Pseudomonas putida KT2440). Find diseases associated with this ...

https://pubchem.ncbi.nlm.nih.gov/protein/Q88FF3

The Structure of a family 25 Glycosyl hydrolase from Bacillus anthracis. ... Lysozymes from glycoside hydrolase family GH25 adopt a (alpha/beta)(5)(beta)(3)-barrel-like fold with a proposal in the ... Lysozymes from glycoside hydrolase family GH25 adopt a (alpha/beta)(5)(beta)(3)-barrel-like fold with a proposal in the ... We show that the active center is extremely similar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 ...

https://www.rcsb.org/structure/2WAG

Diisopropylfluorophosphate Binding Proteins (Serine Hydrolases) from Normal and Leukemic Hematopoietic Cells Subject Area: ... C.R. Gonzales, Sahai Srivastava, J.E. Fitzpatrick; Diisopropylfluorophosphate Binding Proteins (Serine Hydrolases) from Normal ... an active site inhibitor of serine hydrolases. The labeled proteins in the lysates Were examined by sodium dodecyl sulfate- ...

https://karger.com/aha/article-abstract/84/1/5/22275/Diisopropylfluorophosphate-Binding-Proteins-Serine?redirectedFrom=fulltext

"gamma-Glutamyl Hydrolase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "gamma-Glutamyl Hydrolase" by people in Harvard Catalyst ... Below are the most recent publications written about "gamma-Glutamyl Hydrolase" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "gamma-Glutamyl Hydrolase". ...

https://connects.catalyst.harvard.edu/Profiles/display/Concept/gamma-Glutamyl%20Hydrolase

Recombinant Soluble Epoxide Hydrolase Number: 5,445,956. Year: 1995. Patent Status: Issued Authors: Hammock, B.D., D.F. Grant, ... invention relates to nucleic acid sequences and methods useful for producing recombinant human soluble epoxide hydrolase (sEH). ...

https://tools.niehs.nih.gov/srp/Patents/Detail.cfm?PID=61

Epoxide hydrolases metabolize EETs to their corresponding d … ... Fig 2. Expression of epoxide hydrolase isoforms in Ephx3 -/- ... A novel epoxide hydrolase, EPHX3, was recently identified by sequence homology and also exhibits epoxide hydrolase activity in ... Microsomal epoxide hydrolase (EPHX1, mEH) and soluble epoxide hydrolase (EPHX2, sEH) were identified ,30 years ago and are ... Generation and characterization of epoxide hydrolase 3 (EPHX3)-deficient mice Samantha L Hoopes 1 , Artiom Gruzdev 1 , Matthew ...

https://www.ncbi.nlm.nih.gov/pubmed/28384353

It has been suggested that affected individuals may have a genetically-determined defect of microsomal epoxide hydrolase. The ... Genetic analysis of microsomal epoxide hydrolase in patients with carbamazepine hypersensitivity V J Green 1 , M Pirmohamed, N ... Genetic analysis of microsomal epoxide hydrolase in patients with carbamazepine hypersensitivity V J Green et al. Biochem ... DNA sequencing of all nine exons of the microsomal epoxide hydrolase gene from the most severely affected patient showed the ...

https://pubmed.ncbi.nlm.nih.gov/7503783

Glycoside Hydrolases. Mol Vis 2011;17:1287-97 YM-. 1olf protein, rat EC 3.2.1.- *Glycoside Hydrolases. Bioorg Khim. 2010 Sep- ... Glycoside Hydrolases. DNA Repair (Amst) 2007 Mar 1;6(3):329-43 Pme-. 3 protein, C elegans EC 3.2.1.- *Glycoside Hydrolases * ... Glycoside Hydrolases. Chem Pharm Bull (Tokyo) 2005 Aug;53(8):911-4 MurQ protein, E coli EC 3.2.1.- *Glycoside Hydrolases * ... Glycoside Hydrolases. Biochemistry (Mosc) 2005 Dec;70(12):1321-6 ADPRHL2 protein, human EC 3.2.1.143 *Glycoside Hydrolases. J ...

http://www.reference.md/files/D006/mD006026.html

The human microsomal epoxide hydrolase (EH) is a metabolizing enzyme which involves the process of numerous reactive epoxide ...

https://edrn.nci.nih.gov/data-and-resources/publications/15702235-486-polymorphisms-for-microsomal-epoxide-hydrolase-and-genetic-susceptibility-to-copd/

Soluble Epoxide Hydrolase Regulates Macrophage Phagocytosis and Lung Bacterial Clearance of Streptococcus Pneumoniae. Authors. ... The hydrolysis of EETs by soluble epoxide hydrolase (Ephx2) to biologically less active diols attenuates this anti-inflammatory ...

https://researchfestival.nih.gov/2015/posters/soluble-epoxide-hydrolase-regulates-macrophage-phagocytosis-and-lung

1-Cyclohexyl-3-dodecyl urea is a highly selective soluble epoxide hydrolase (sEH) inhibitor. ... 1-Cyclohexyl-3-dodecyl urea 402939-18-8 代谢 Epoxide Hydrolase pressure 1 Cyclohexyl 3 dodecyl urea epoxyeicosatrienoic inhibit ... Soluble epoxide hydrolase inhibition lowers arterial blood pressure in angiotensin II hypertension.Hypertension. 2002 Feb;39(2 ... 1-Cyclohexyl-3-dodecyl urea is a highly selective soluble epoxide hydrolase (sEH) inhibitor.. ...

https://www.targetmol.com/compound/1-Cyclohexyl-3-dodecyl%20urea

Glycoside hydrolases are also referred to as glycosidases. Glycoside hydrolases can catalyze the hydrolysis of O-, N- and S- ... Glycoside Hydrolase Firsts. First sterochemistry determination. Cite some reference here, with a short explanation [1].. First ... exo- and endo- refers to the ability of a glycoside hydrolase to cleave a substrate at the end (most frequently, but not always ... Glycoside hydrolases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation ...

https://www.cazypedia.org/index.php?title=Glycoside_Hydrolases&oldid=1013

DDAH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285a.a.) and having a molecular mass of 33.5kDa.DDAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. ...

https://neobiolab.com/index.php?m=Product&a=index&id=222&alphabetical=D&s1=

Domain architectures illustrate each occurrence of the Glycosyl hydrolase domain superfamily. ... Domain combinations containing the Glycosyl hydrolase domain superfamily in Paenibacillus sp. Y412MC10. ... 7 domain combinations include a Glycosyl hydrolase domain domain in Paenibacillus sp. Y412MC10. With a total of 7 different ... Domain combinations for Glycosyl hydrolase domain superfamily in Paenibacillus sp. Y412MC10. ...

https://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/cgi-bin/allcombs.cgi?genome=9I&sf=51011

... and the coding regions for the hydrolases were cloned and expressed. The availability of this new hydrolase cDNA and expression ... ADP-ribosylarginine hydrolases from a variety of mammalian species and tissues were isolated, ... ADP-ribosylation is reversed by ADP-ribosylarginine hydrolases, which cleave the ADP-ribose-arginine bond. ...

http://www.techtransfer.nih.gov/tech/tab-399

Discovery of selective small-molecule activators of a bacterial glycoside hydrolase. John F. Darby, Jens Landström, Christian ... Discovery of selective small-molecule activators of a bacterial glycoside hydrolase. / Darby, John F.; Landström, Jens; Roth, ... Discovery of selective small-molecule activators of a bacterial glycoside hydrolase. Angewandte Chemie International Edition. ... Herein, we describe the discovery and characterization of small-molecule activators of a glycoside hydrolase (a bacterial O- ...

https://pure.york.ac.uk/portal/en/publications/discovery-of-selective-small-molecule-activators-of-a-bacterial-g

Fatty acid amide hydrolase - Hydrolases. Detailed annotation on the structure, function, physiology, pharmacology and clinical ... 2018) Design and Potency of Dual Soluble Epoxide Hydrolase/Fatty Acid Amide Hydrolase Inhibitors. ACS Omega, 3 (10): 14076- ... 7. Hammock B, Kodani S. (2017) Inhibitors for soluble epoxide hydrolase (seh) and fatty acid amide hydrolase (faah). Patent ... 2012) Aryl Piperazinyl Ureas as Inhibitors of Fatty Acid Amide Hydrolase (FAAH) in Rat, Dog, and Primate. ACS Med Chem Lett, 3 ...

https://www.guidetoimmunopharmacology.org/GRAC/ObjectDisplayForward?objectId=1400

7.3 Epoxide Hydrolase Inhibitors In vitro studies suggest that lesinurad is not an inhibitor of epoxide hydrolase; however, ... 7.3 Epoxide Hydrolase Inhibitors 7.4 Hormonal Contraceptives 7.5 Aspirin 8 USE IN SPECIFIC POPULATIONS 8.1 Pregnancy 8.2 ... A transient oxide metabolite is rapidly eliminated by microsomal epoxide hydrolase in the liver and not detected in plasma. ... inhibitors of epoxide hydrolase (i.e., valproic acid) may interfere with metabolism of lesinurad. ZURAMPIC should not be ...

https://dailymed.nlm.nih.gov/dailymed/drugInfo.cfm?setid=ef9e7711-f478-4e35-bf4e-6021c8457e3b

Latest research on Fatty Acid Amide Hydrolase and cannabinoid sciences. Check out the CannaKeys FAAH research dashboard. 1 Wk ... Overview - Fatty Acid Amide Hydrolase (FAAH). Description of Fatty Acid Amide Hydrolase (FAAH). The naturally occurring enzyme ... Proven effects in clinical trials for Fatty Acid Amide Hydrolase (FAAH) *Receptors associated with Fatty Acid Amide Hydrolase ( ... Fatty Acid Amide Hydrolase (FAAH) Properties and Effects. Inhibition of FAAH is associated with: *Mood-improving effects (F. ...

https://cannakeys.com/fatty-acid-amide-hydrolase-faah-cannabinoid-research/

... cells can respond to protease/substrate imbalance in this compartment by de novo expression of multiple lysosomal hydrolases. ... Activation of STAT3 in AEP−/− kidney and enhanced hydrolase expression in STAT3c kidneys. a STAT3 and P-STAT3 levels in WT and ... 1d, 2 and Supplementary Data 1) including cathepsins (Cts) A, B, C, L and Z and other hydrolases such as hexosaminidase A and ... e Acute AEP inhibition with MVO26630 recapitulates hydrolase induction in WT MEF and AEP reconstitution reverses it in AEP−/− ...

https://www.nature.com/articles/s41467-018-07741-6?error=cookies_not_supported&code=b6dc368c-239e-4c55-be5b-1924c8a216ac

... as putative glycoside hydrolase and glycoside hydrolase-associated C-terminal domain respectively. ... Structural and sequence analyses of the BT_1012 protein identifies it as a glycosyl hydrolase, expanding an already impressive ... The N-terminal domain is a putative catalytic domain with significant similarity to known glycoside hydrolases, the C-terminal ... Initial analysis of the archetypal Bacteroides thetaiotaomicron genome identified 172 glycosyl hydrolases and a large number of ...

https://pesquisa.bvsalud.org/perinatal/resource/es/mdl-24742328

... Enzymatic activity of LTA4 Hydrolase in Complex with COMPOUND15. ... The structure of LTA4 Hydrolase in Complex with COMPOUND15 also contains other interesting chemical elements:. Ytterbium. (Yb) ... Zinc binding site 1 out of 1 in the LTA4 Hydrolase in Complex with COMPOUND15. Mono view Stereo pair view ... A full contact list of Zinc with other atoms in the Zn binding site number 1 of LTA4 Hydrolase in Complex with COMPOUND15 ...

http://zinc.atomistry.com/pdb6end.html

Structural and sequence-based classification of glycoside hydrolases journal, October 1997 * Henrissat, Bernard; Davies, Gideon ... The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino ...

https://www.osti.gov/doepatents/biblio/1117875

EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list) ...

https://en.wikipedia.org/wiki/Dichloromethane_dehalogenase

hydrolase. 32. hydrolases. 33. kinase. 34. kinases. 35. peptidase. 36. phosphatase. 37. phospholipase. 38. protease. 39. ...

https://www.onelook.com/?w=neurotensin+endopeptidase

Peptide Hydrolases / analysis * Proteoglycans / physiology * Prothrombin / analysis * Skin / injuries * Skin / pathology* * ...

https://pubmed.ncbi.nlm.nih.gov/9569202/

View Full Project Details for The role of a-synuclein accumulation in lysosomal hydrolase trafficking and function ... The role of a-synuclein accumulation in lysosomal hydrolase trafficking and function. ... The role of a-synuclein accumulation in lysosomal hydrolase trafficking and function ...

https://iadrp.nia.nih.gov/project/role-synuclein-accumulation-lysosomal-hydrolase-trafficking-and-function

Here we report the further characterization of acyl peptide hydrolase activity using mass spectrometry. Acyl peptide hydrolase ... In addition, by real-time PCR we found elevated acyl peptide hydrolase expression in brain areas rich in amyloid plaques ... These data suggest that acyl peptide hydrolase is involved in the degradation of oligomeric amyloid-beta, an activity that, if ... We previously reported the isolation of a novel amyloid-beta-degrading enzyme, acyl peptide hydrolase, a serine protease that ...

https://molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-4-33

The present invention relates to nucleic acid sequences and methods useful for producing recombinant human soluble epoxide hydrolase (sEH). (nih.gov)
The hydrolysis of EETs by soluble epoxide hydrolase (Ephx2) to biologically less active diols attenuates this anti-inflammatory effect. (nih.gov)
1-Cyclohexyl-3-dodecyl urea is a highly selective soluble epoxide hydrolase (sEH) inhibitor. (targetmol.com)
Soluble epoxide hydrolase inhibition lowers arterial blood pressure in angiotensin II hypertension.Hypertension. (targetmol.com)
Development of multitarget agents possessing soluble epoxide hydrolase inhibitory activity. (nih.gov)

The human microsomal epoxide hydrolase (EH) is a metabolizing enzyme which involves the process of numerous reactive epoxide intermediates and contains polymorphic alleles which are associated with altered EH activity and may be linked to increased risk for COPD. (nih.gov)
Such activators could offer an orthogonal alternative to enzyme inhibitors for perturbation of enzyme activity in vivo, and could also be used for glycoside hydrolase activation in many industrial processes. (york.ac.uk)
The naturally occurring enzyme fatty-acid amide hydrolase (FAAH) was discovered in the late nineties ( B. Cravat 1996 ) and is one of the primary compounds responsible for metabolizing (breaking down) bioactive fatty acid amides such as the endocannabinoid anandamide (AEA) to their corresponding acids, thus terminating the signaling functions of these molecules. (cannakeys.com)
We previously reported the isolation of a novel amyloid-beta-degrading enzyme, acyl peptide hydrolase, a serine protease that degrades amyloid-beta, and is different in structure and activity from other amyloid-beta-degrading enzymes. (biomedcentral.com)
The AHCY gene provides instructions for producing the enzyme S-adenosylhomocysteine hydrolase. (medlineplus.gov)

A novel epoxide hydrolase, EPHX3, was recently identified by sequence homology and also exhibits epoxide hydrolase activity in vitro with a substrate preference for 9,10-epoxyoctadecamonoenoic acid (EpOME) and 11,12-EET. (nih.gov)
It has been suggested that affected individuals may have a genetically-determined defect of microsomal epoxide hydrolase. (nih.gov)
The technique of polymerase chain reaction single-strand conformation polymorphism analysis (PCR-SSCP) was used to screen for mutations in all nine exons of the microsomal epoxide hydrolase gene. (nih.gov)
There was a higher frequency of mutations in the hypersensitive group when compared with the controls, but there was no consistent mutation (or pattern of mutations) in the microsomal epoxide hydrolase gene which was common to the hypersensitive group. (nih.gov)
Polymorphisms for microsomal epoxide hydrolase and genetic susceptibility to COPD. (nih.gov)

Carboxylic Ester Hydrolases, EC 3.1.1. (tno.nl)

2WAG: The Structure of a family 25 Glycosyl hydrolase from Bacillus anthracis. (rcsb.org)
Domain combinations for Glycosyl hydrolase domain superfamily in Paenibacillus sp. (cam.ac.uk)
Initial analysis of the archetypal Bacteroides thetaiotaomicron genome identified 172 glycosyl hydrolases and a large number of uncharacterized proteins associated with polysaccharide metabolism . (bvsalud.org)
The N-terminal domain is a putative catalytic domain with significant similarity to known glycoside hydrolases , the C-terminal domain has a beta-sandwich fold typically found in C-terminal domains of other glycosyl hydrolases, however these domains are typically involved in substrate binding. (bvsalud.org)
Structural and sequence analyses of the BT_1012 protein identifies it as a glycosyl hydrolase , expanding an already impressive catalog of enzymes involved in polysaccharide metabolism in Bacteroides spp. (bvsalud.org)

Normal and leukemic hematopoietic cell lysates were labeled with [ 3 H]-diisopropylfluorophosphate ([ 3 H]-DFP), an active site inhibitor of serine hydrolases. (karger.com)
The expanding diversity of serine hydrolases. (nih.gov)

We show here that cells can respond to protease/substrate imbalance in this compartment by de novo expression of multiple lysosomal hydrolases. (nature.com)

We show that the active center is extremely similar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 implying that, in the absence of evidence to the contrary, GH25 enzymes also act with net retention of anomeric configuration using the neighboring-group catalytic mechanism that is common to this 'super-family' of enzymes. (rcsb.org)
Glycoside hydrolases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation of a sugar hemiacetal or hemiketal and the corresponding free aglycon. (cazypedia.org)

Herein, we describe the discovery and characterization of small-molecule activators of a glycoside hydrolase (a bacterial O-GlcNAc hydrolase). (york.ac.uk)
Here we report the further characterization of acyl peptide hydrolase activity using mass spectrometry. (biomedcentral.com)

Glycoside hydrolases are also referred to as glycosidases. (cazypedia.org)

S-Adenosylhomocysteine hydrolase deficiency: a second patient, the younger brother of the index patient, and outcomes during therapy. (medlineplus.gov)

CannaKeys has 312 studies associated with Fatty Acid Amide Hydrolase (FAAH). (cannakeys.com)

Feasibility and Physiological Relevance of Designing Highly Potent Aminopeptidase-Sparing Leukotriene A4 Hydrolase Inhibitors. (atomistry.com)

exo - and endo - refers to the ability of a glycoside hydrolase to cleave a substrate at the end (most frequently, but not always the non-reducing end) or within the middle of a chain. (cazypedia.org)

Glycoside hydrolases can catalyze the hydrolysis of O-, N- and S-linked glycosides. (cazypedia.org)
Retaining and inverting classification refers to the stereochemical outcome of the hydrolysis reaction catalyzed by the glycoside hydrolase. (cazypedia.org)

Based on this we have renamed the Pfam families representing the two domains found in the BT_1012 protein , PF13204 and PF12904, as putative glycoside hydrolase and glycoside hydrolase -associated C-terminal domain respectively. (bvsalud.org)

Lastly, tissue culture experiments using transfected CHO cells expressing APP751 bearing the V717F mutation indicate that acyl peptide hydrolase preferentially degrades dimeric and trimeric forms of amyloid-beta. (biomedcentral.com)
Leukotriene A4 Hydrolase: Selective Abrogation of Leukotriene B4 Formation by Mutation of Aspartic Acid 375. (expasy.org)

Algorithmic methods are then used to compare sequences, and in the case of the glycoside hydrolases, this has allowed their classification into more than 100 families. (cazypedia.org)

Lysozymes are found in many of the sequence-based families of glycoside hydrolases (www.cazy.org) where they show considerable structural and mechanistic diversity. (rcsb.org)

This graph shows the total number of publications written about "gamma-Glutamyl Hydrolase" by people in Harvard Catalyst Profiles by year, and whether "gamma-Glutamyl Hydrolase" was a major or minor topic of these publication. (harvard.edu)

The binding sites of Zinc atom in the LTA4 Hydrolase in Complex with COMPOUND15 (pdb code 6end ). (atomistry.com)

These data suggest that acyl peptide hydrolase is involved in the degradation of oligomeric amyloid-beta, an activity that, if induced, might present a new tool for therapy aimed at reducing neurodegeneration in the Alzheimer's brain. (biomedcentral.com)

In addition, by real-time PCR we found elevated acyl peptide hydrolase expression in brain areas rich in amyloid plaques suggesting that this enzyme's levels are responsive to increases in amyloid-beta levels. (biomedcentral.com)

Is the Subject Area "Glycoside hydrolases" applicable to this article? (plos.org)

gamma-Glutamyl Hydrolase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)

Below are the most recent publications written about "gamma-Glutamyl Hydrolase" by people in Profiles. (harvard.edu)

Acyl peptide hydrolase cleaves the amyloid-beta peptide at amino acids 13, 14 and 19. (biomedcentral.com)

Anatomy17

Organisms35

Diseases3

Chemicals and Drugs133

Analytical, Diagnostic and Therapeutic Techniques and Equipment19

Phenomena and Processes44

Technology, Industry, Agriculture1

Information Science5

Health Care3

Interaction of inflammatory cells and oral microorganisms. II. Modulation of rabbit polymorphonuclear leukocyte hydrolase release by polysaccharides in response to Streptococcus mutans and Streptococcus sanguis. (1/2136)

Interaction of inflammatory cells and oral microorganisms. III. Modulation of rabbit polymorphonuclear leukocyte hydrolase release response to Actinomyces viscosus and Streptococcus mutans by immunoglobulins and complement. (2/2136)

Thermodynamic analysis of halide binding to haloalkane dehalogenase suggests the occurrence of large conformational changes. (3/2136)

A new hydrolase specific for taurine-conjugates of bile acids. (4/2136)

Identification and characterization of alkenyl hydrolase (lysoplasmalogenase) in microsomes and identification of a plasmalogen-active phospholipase A2 in cytosol of small intestinal epithelium. (5/2136)

Galactosyltransferase, pyrophosphatase and phosphatase activities in luminal plasma of the cauda epididymidis and in the rete testis fluid of some mammals. (6/2136)

Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. (7/2136)

Degradation of 1,2-dibromoethane by Mycobacterium sp. strain GP1. (8/2136)

Hydrolases

Glycoside Hydrolases

Epoxide Hydrolases

Carboxylic Ester Hydrolases

Lysosomes

Acid Phosphatase

Glucuronidase

Hexosaminidases

Mannosephosphates

N-Acetylmuramoyl-L-alanine Amidase

Peptide Hydrolases

Mucolipidoses

Molecular Sequence Data

Substrate Specificity

Thiolester Hydrolases

Receptor, IGF Type 2

Amino Acid Sequence

Acetylglucosaminidase

alpha-L-Fucosidase

Hydrolysis

Xylosidases

Cellulase

Cellvibrio

beta-Glucosidase

Galactosidases

beta-Mannosidase

Endo-1,4-beta Xylanases

Xylans

Acid Anhydride Hydrolases

Arylsulfatases

beta-N-Acetylhexosaminidases

Disaccharidases

Sequence Homology, Amino Acid

Pyrophosphatases

Cathepsins

Amidohydrolases

Glucosidases

Mannosidases

N-Glycosyl Hydrolases

Cathepsin D

Cell Wall

Monocrotophos

Cloning, Molecular

Transferases (Other Substituted Phosphate Groups)

Cellulases

Catalytic Domain

Esterases

Kinetics

Vacuoles

Sequence Alignment

Catalysis

Cellulose

Hydrogen-Ion Concentration

Bacterial Proteins

Saposins

Acetylesterase

Cellulose 1,4-beta-Cellobiosidase

Sulfatases

Models, Molecular

Sucrase

Sterol Esterase

Phosphoric Monoester Hydrolases

Glucans

alpha-Mannosidase

alpha-Glucosidases

Enzyme Stability

Cathepsin A

Oligosaccharides

Crystallography, X-Ray

Palmitoyl-CoA Hydrolase

Phylogeny

Neocallimastigales

Escherichia coli

Alteromonas

Aspartylglucosylaminase

Fibrobacter

Glucan Endo-1,3-beta-D-Glucosidase

Phosphoric Diester Hydrolases

Epoxy Compounds

Recombinant Proteins