Hydrolases
Epoxide Hydrolases
Carboxylic Ester Hydrolases
Lysosomes
Acid Phosphatase
Hexosaminidases
N-Acetylmuramoyl-L-alanine Amidase
Peptide Hydrolases
Mucolipidoses
Molecular Sequence Data
Substrate Specificity
Receptor, IGF Type 2
Amino Acid Sequence
Acetylglucosaminidase
alpha-L-Fucosidase
Xylosidases
Cellulase
Cellvibrio
beta-Glucosidase
Galactosidases
beta-Mannosidase
Endo-1,4-beta Xylanases
Acid Anhydride Hydrolases
Arylsulfatases
beta-N-Acetylhexosaminidases
Sequence Homology, Amino Acid
Pyrophosphatases
Cathepsins
N-Glycosyl Hydrolases
Cathepsin D
Cell Wall
Monocrotophos
Cloning, Molecular
Transferases (Other Substituted Phosphate Groups)
Cellulases
Catalytic Domain
Vacuoles
Sequence Alignment
Catalysis
Cellulose
Hydrogen-Ion Concentration
Saposins
Acetylesterase
Cellulose 1,4-beta-Cellobiosidase
Models, Molecular
Sterol Esterase
Phosphoric Monoester Hydrolases
Glucans
alpha-Mannosidase
alpha-Glucosidases
Enzyme Stability
Cathepsin A
Oligosaccharides
Crystallography, X-Ray
Palmitoyl-CoA Hydrolase
Neocallimastigales
Escherichia coli
Alteromonas
Aspartylglucosylaminase
Fibrobacter
Glucan Endo-1,3-beta-D-Glucosidase
Phosphoric Diester Hydrolases
Epoxy Compounds
Sequence Analysis, DNA
Bacteriolysis
Carboxylesterase
Binding Sites
Glucan 1,4-beta-Glucosidase
Piromyces
Glycosyltransferases
Carboxypeptidases
Ubiquitin Thiolesterase
Base Sequence
Leucyl Aminopeptidase
Endopeptidases
Cathepsin B
Trichoderma
Sphingolipid Activator Proteins
Carbohydrate Metabolism
Gold Colloid, Radioactive
Acidianus
Mannose
Comamonadaceae
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
Subcellular Fractions
Aminopeptidases
beta-Galactosidase
Cytophaga
Lipase
Mutation
Protein Structure, Tertiary
Ruminococcus
Cellulosomes
Sucrase-Isomaltase Complex
Acidithiobacillus thiooxidans
Pectins
Chitin
Cell Fractionation
Protein Conformation
alpha-Amylases
Monoacylglycerol Lipases
Pinocytosis
Models, Chemical
Temperature
Gram-Negative Anaerobic Straight, Curved, and Helical Rods
Naphthaleneacetic Acids
Enzymes
Endocytosis
Multigene Family
Electrophoresis, Polyacrylamide Gel
Cell Compartmentation
Mutagenesis, Site-Directed
Vesicular Transport Proteins
Aspergillus oryzae
Protein Structure, Secondary
Gangliosidoses
Xylan Endo-1,3-beta-Xylosidase
alpha-Galactosidase
Golgi Apparatus
Microscopy, Electron
Alkaline Phosphatase
Endosomes
Protein Processing, Post-Translational
Naphthol AS D Esterase
Biocatalysis
Adenosylhomocysteinase
Liver
Clostridium thermocellum
Neocallimastix
Molecular Structure
Glucan 1,3-beta-Glucosidase
Cathepsin L
Mononuclear Phagocyte System
Conserved Sequence
Bacteria
Carbohydrates
Plants
Protein Binding
Solubility
Structure-Activity Relationship
Chromatography, Ion Exchange
Centrifugation, Zonal
Dinucleoside Phosphates
Saccharomyces cerevisiae
Fungi
Sequence Homology
Bacillus
Carbohydrate Sequence
Proteins
Muramidase
Stereoisomerism
O-Acetyl-ADP-Ribose
Centrifugation, Density Gradient
Organophosphorus Compounds
Clostridium
Biological Transport
Penicillin Amidase
Lysosomal Storage Diseases
Arabidopsis
Organelles
Ceroid
Open Reading Frames
Sucrose
Gene Library
Sphingomonas
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.
Phosphoric monoester hydrolases
Acid anhydride hydrolases
Hydrolase
Alkenylglycerophosphoethanolamine hydrolase
Pantetheine hydrolase
Rhamnogalacturonan hydrolase
Allophanate hydrolase
Streptothricin hydrolase
Maleimide hydrolase
Alkenylglycerophosphocholine hydrolase
Chenodeoxycholoyltaurine hydrolase
Acid hydrolase
Pyrethroid hydrolase
Polymannuronate hydrolase
Acetylpyruvate hydrolase
Thiocyanate hydrolase
Phloretin hydrolase
Hydroxyisourate hydrolase
Dipeptide hydrolase
Dihydrocoumarin hydrolase
Glutathione hydrolase
Phosphonoacetaldehyde hydrolase
Futalosine hydrolase
Acyloxyacyl hydrolase
Serine hydrolase
Epoxide hydrolase
Nudix hydrolase
Phosphonoacetate hydrolase
Ureidoglycolate hydrolase
Bleomycin hydrolase
Epoxide Hydrolase 3 (Ephx3) Gene Disruption Reduces Ceramide Linoleate Epoxide Hydrolysis and Impairs Skin Barrier Function
Hydroxyacylglutathione hydrolase (Pseudomonas putida KT2440) | Protein Target - PubChem
RCSB PDB - 2WAG: The Structure of a family 25 Glycosyl hydrolase from Bacillus anthracis.
Diisopropylfluorophosphate Binding Proteins (Serine Hydrolases) from Normal and Leukemic Hematopoietic Cells | Acta...
gamma-Glutamyl Hydrolase | Harvard Catalyst Profiles | Harvard Catalyst
Patent Detail: Recombinant Soluble Epoxide Hydrolase (Superfund Research Program)
Generation and characterization of epoxide hydrolase 3 (EPHX3)-deficient mice - PubMed
Genetic analysis of microsomal epoxide hydrolase in patients with carbamazepine hypersensitivity - PubMed
Glycoside Hydrolases (definition)
Polymorphisms for microsomal epoxide hydrolase and genetic susceptibility to COPD.
Soluble Epoxide Hydrolase Regulates Macrophage Phagocytosis and Lung Bacterial Clearance of Streptococcus Pneumoniae | NIH...
1-Cyclohexyl-3-dodecyl urea | Epoxide Hydrolase | TargetMol
Glycoside Hydrolases - CAZypedia
Hydrolase
Domain combinations for Glycosyl hydrolase domain superfamily in Paenibacillus sp. Y412MC10
Clones Encoding Mammalian ADP-Ribosylarginine Hydrolases | Technology Transfer
Discovery of selective small-molecule activators of a bacterial glycoside hydrolase<...
Fatty acid amide hydrolase | Hydrolases | IUPHAR Guide to IMMUNOPHARMACOLOGY
These highlights do not include all the information needed to use ZURAMPIC safely and effectively. See full prescribing...
Fatty Acid Amide Hydrolase (FAAH) Cannabinoid Research - Cannakeys
Lysosomal protease deficiency or substrate overload induces an oxidative-stress mediated STAT3-dependent pathway of lysosomal...
Structural genomics analysis of uncharacterized protein families overrepresented in human gut bacteria identifies a novel...
Zinc in PDB 6end: LTA4 Hydrolase in Complex with COMPOUND15
Cellobiohydrolase I enzymes (Patent) | DOE Patents
Dichloromethane dehalogenase - Wikipedia
Definitions of neurotensin endopeptidase - OneLook Dictionary Search
Effects of skin mast cells on bleeding time and coagulation activation at the site of platelet plug formation
The role of a-synuclein accumulation in lysosomal hydrolase trafficking and function | NIH
Acyl peptide hydrolase degrades monomeric and oligomeric amyloid-beta peptide | Molecular Neurodegeneration | Full Text
Soluble epoxide h5
- 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)
Enzyme5
- 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)
Epoxide Hydrolase5
- 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 Hydrolases1
- Carboxylic Ester Hydrolases, EC 3.1.1. (tno.nl)
Glycosyl5
- 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)
Serine2
- 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)
Lysosomal1
- We show here that cells can respond to protease/substrate imbalance in this compartment by de novo expression of multiple lysosomal hydrolases. (nature.com)
Enzymes2
- 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)
Characterization2
- 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)
Glycosidases1
- Glycoside hydrolases are also referred to as glycosidases. (cazypedia.org)
Deficiency1
- S-Adenosylhomocysteine hydrolase deficiency: a second patient, the younger brother of the index patient, and outcomes during therapy. (medlineplus.gov)
Faah1
- CannaKeys has 312 studies associated with Fatty Acid Amide Hydrolase (FAAH). (cannakeys.com)
Inhibitors1
- Feasibility and Physiological Relevance of Designing Highly Potent Aminopeptidase-Sparing Leukotriene A4 Hydrolase Inhibitors. (atomistry.com)
Substrate1
- 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)
Hydrolysis2
- 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)
Protein1
- 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)
Mutation2
- 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)
Classification1
- 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)
Diversity1
- 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)
Publication1
- 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)
Complex1
- The binding sites of Zinc atom in the LTA4 Hydrolase in Complex with COMPOUND15 (pdb code 6end ). (atomistry.com)
Activity1
- 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)
Expression1
- 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)
Article1
- Is the Subject Area "Glycoside hydrolases" applicable to this article? (plos.org)
Library1
- gamma-Glutamyl Hydrolase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
Publications1
- Below are the most recent publications written about "gamma-Glutamyl Hydrolase" by people in Profiles. (harvard.edu)
Beta1
- Acyl peptide hydrolase cleaves the amyloid-beta peptide at amino acids 13, 14 and 19. (biomedcentral.com)