Ammonia: A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.Lyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.Chondroitin Lyases: Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chondroitin sulfate A and C as well as on dermatan sulfate and slowly on hyaluronate. EC 4.2.2.5 acts on chondroitin sulfate A and C.Pectobacterium chrysanthemi: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria that causes vascular wilts on a wide range of plant species. It was formerly named Erwinia chrysanthemi.Chondroitinases and Chondroitin Lyases: Enzymes which catalyze the elimination of glucuronate residues from chondroitin A,B, and C or which catalyze the hydrolysis of sulfate groups of the 2-acetamido-2-deoxy-D-galactose 6-sulfate units of chondroitin sulfate. EC 4.2.2.-.Pectins: 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.Phycobiliproteins: Light harvesting proteins found in phycobilisomes.Chicory: A thick-rooted perennial (Cichorium intybus) native to Europe but widely grown for its young leaves used as salad greens and for its roots, dried and ground-roasted, used to flavor or adulterate coffee. (From Webster, 3d ed)Aldehyde-Lyases: Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.Nitrosomonas: A genus of gram-negative, ellipsoidal or rod-shaped bacteria whose major source of energy and reducing power is from the oxidation of ammonia to nitrite. Its species occur in soils, oceans, lakes, rivers, and sewage disposal systems.Carbon-Oxygen Lyases: Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.Erwinia: A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria whose organisms are associated with plants as pathogens, saprophytes, or as constituents of the epiphytic flora.Heparin Lyase: An enzyme of the isomerase class that catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. (From Enzyme Nomenclature, 1992) EC 4.2.2.7.Carbamoyl-Phosphate Synthase (Ammonia): An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and ammonia. This enzyme is specific for arginine biosynthesis or the urea cycle. Absence or lack of this enzyme may cause CARBAMOYL-PHOSPHATE SYNTHASE I DEFICIENCY DISEASE. EC 6.3.4.16.Oxo-Acid-Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.Polygalacturonase: A cell wall-degrading enzyme found in microorganisms and higher plants. It catalyzes the random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans. EC 3.2.1.15.Hyperammonemia: Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.Molecular Sequence Data: 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.Urea: A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.Glutamate-Ammonia Ligase: An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.Alginates: Salts of alginic acid that are extracted from marine kelp and used to make dental impressions and as absorbent material for surgical dressings.Glutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Hydrogen-Ion Concentration: 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)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Ammonium Chloride: An acidifying agent that has expectorant and diuretic effects. Also used in etching and batteries and as a flux in electroplating.Nitrogen Radioisotopes: Unstable isotopes of nitrogen that decay or disintegrate emitting radiation. N atoms with atomic weights 12, 13, 16, 17, and 18 are radioactive nitrogen isotopes.Hexuronic Acids: Term used to designate tetrahydroxy aldehydic acids obtained by oxidation of hexose sugars, i.e. glucuronic acid, galacturonic acid, etc. Historically, the name hexuronic acid was originally given to ascorbic acid.Isocitrate Lyase: A key enzyme in the glyoxylate cycle. It catalyzes the conversion of isocitrate to succinate and glyoxylate. EC 4.1.3.1.Nitrification: A process facilitated by specialized bacteria involving the oxidation of ammonium to nitrite and nitrate.Rhodophyta: Plants of the division Rhodophyta, commonly known as red algae, in which the red pigment (PHYCOERYTHRIN) predominates. However, if this pigment is destroyed, the algae can appear purple, brown, green, or yellow. Two important substances found in the cell walls of red algae are AGAR and CARRAGEENAN. Some rhodophyta are notable SEAWEED (macroalgae).Phycobilins: Open chain tetrapyrroles that function as light harvesting chromophores in PHYCOBILIPROTEINS.Chondroitin ABC Lyase: An enzyme that catalyzes the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups. (Enzyme Nomenclature, 1992)Sphingomonas: 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.Amino Acid Sequence: 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.Cytochromes c1: The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (From Enzyme Nomenclature, 1992, p545)Bacteroides: A genus of gram-negative, anaerobic, rod-shaped bacteria. Its organisms are normal inhabitants of the oral, respiratory, intestinal, and urogenital cavities of humans, animals, and insects. Some species may be pathogenic.Kinetics: The rate dynamics in chemical or physical systems.Glucuronic Acid: A sugar acid formed by the oxidation of the C-6 carbon of GLUCOSE. In addition to being a key intermediate metabolite of the uronic acid pathway, glucuronic acid also plays a role in the detoxification of certain drugs and toxins by conjugating with them to form GLUCURONIDES.Flavobacterium: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in SOIL and WATER. Its organisms are also found in raw meats, MILK and other FOOD, hospital environments, and human clinical specimens. Some species are pathogenic in humans.Adenylosuccinate Lyase: An enzyme that, in the course of purine ribonucleotide biosynthesis, catalyzes the conversion of 5'-phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole to 5'-phosphoribosyl-4-carboxamide-5-aminoimidazole and the conversion of adenylosuccinic acid to AMP. EC 4.3.2.2.Streptococcus anginosus: A species of gram-positive bacteria in the STREPTOCOCCUS MILLERI GROUP. It is the most frequently seen isolate of that group, has a proclivity for abscess formation, and is most often isolated from the blood, gastrointestinal, and urogenital tract.GlutaminaseCloning, Molecular: 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.Hevea: A plant genus of the family EUPHORBIACEAE, order Euphorbiales, subclass Rosidae. Commercial natural RUBBER is mainly obtained from Hevea brasiliensis but also from some other plants.Bacterial Proteins: Proteins found in any species of bacterium.Hepatic Encephalopathy: A syndrome characterized by central nervous system dysfunction in association with LIVER FAILURE, including portal-systemic shunts. Clinical features include lethargy and CONFUSION (frequently progressing to COMA); ASTERIXIS; NYSTAGMUS, PATHOLOGIC; brisk oculovestibular reflexes; decorticate and decerebrate posturing; MUSCLE SPASTICITY; and bilateral extensor plantar reflexes (see REFLEX, BABINSKI). ELECTROENCEPHALOGRAPHY may demonstrate triphasic waves. (From Adams et al., Principles of Neurology, 6th ed, pp1117-20; Plum & Posner, Diagnosis of Stupor and Coma, 3rd ed, p222-5)Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Manure: Accumulations of solid or liquid animal excreta usually from stables and barnyards with or without litter material. Its chief application is as a fertilizer. (From Webster's 3d ed)Nitrosomonas europaea: The type species of the genus NITROSOMONAS, a gram-negative chemolithotroph that oxidizes ammonia to nitrite. It is found in soil, sewage, freshwater, and on building walls, and especially in polluted areas where air contains high levels of nitrogen compounds.Carbon-Nitrogen Lyases: Enzymes that catalyze the cleavage of a carbon-nitrogen bond by means other than hydrolysis or oxidation. Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3.Glutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.Carbon-Carbon Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond by means other than hydrolysis or oxidation. This subclass contains the DECARBOXYLASES, the ALDEHYDE-LYASES, and the OXO-ACID-LYASES. EC 4.1.Glycosaminoglycans: Heteropolysaccharides which contain an N-acetylated hexosamine in a characteristic repeating disaccharide unit. The repeating structure of each disaccharide involves alternate 1,4- and 1,3-linkages consisting of either N-acetylglucosamine or N-acetylgalactosamine.Proteus vulgaris: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria that occurs in soil, fecal matter, and sewage. It is an opportunistic pathogen and causes cystitis and pyelonephritis.Uronic Acids: Acids derived from monosaccharides by the oxidation of the terminal (-CH2OH) group farthest removed from the carbonyl group to a (-COOH) group. (From Stedmans, 26th ed)Rumen: The first stomach of ruminants. It lies on the left side of the body, occupying the whole of the left side of the abdomen and even stretching across the median plane of the body to the right side. It is capacious, divided into an upper and a lower sac, each of which has a blind sac at its posterior extremity. The rumen is lined by mucous membrane containing no digestive glands, but mucus-secreting glands are present in large numbers. Coarse, partially chewed food is stored and churned in the rumen until the animal finds circumstances convenient for rumination. When this occurs, little balls of food are regurgitated through the esophagus into the mouth, and are subjected to a second more thorough mastication, swallowed, and passed on into other parts of the compound stomach. (From Black's Veterinary Dictionary, 17th ed)Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Chondroitin Sulfates: Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.Disaccharides: Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Escherichia coli: 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.Sulfonium Compounds: Sulfur compounds in which the sulfur atom is attached to three organic radicals and an electronegative element or radical.Phenylalanine Ammonia-Lyase: An enzyme that catalyzes the deamination of PHENYLALANINE to form trans-cinnamate and ammonia.Gills: Paired respiratory organs of fishes and some amphibians that are analogous to lungs. They are richly supplied with blood vessels by which oxygen and carbon dioxide are exchanged directly with the environment.Glycoside HydrolasesDermatan Sulfate: A naturally occurring glycosaminoglycan found mostly in the skin and in connective tissue. It differs from CHONDROITIN SULFATE A (see CHONDROITIN SULFATES) by containing IDURONIC ACID in place of glucuronic acid, its epimer, at carbon atom 5. (from Merck, 12th ed)Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Sequence Alignment: 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.Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.Glutamate Synthase: An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13.DNA-(Apurinic or Apyrimidinic Site) Lyase: A DNA repair enzyme that catalyses the excision of ribose residues at apurinic and apyrimidinic DNA sites that can result from the action of DNA GLYCOSYLASES. The enzyme catalyzes a beta-elimination reaction in which the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. This enzyme was previously listed under EC 3.1.25.2.Quaternary Ammonium Compounds: Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.AcetyleneGlutamates: Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Bacillus: A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.Methionine SulfoximineArchaea: One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.N-Glycosyl Hydrolases: A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars.Urease: An enzyme that catalyzes the conversion of urea and water to carbon dioxide and ammonia. EC 3.5.1.5.Fatty Acids, Volatile: Short-chain fatty acids of up to six carbon atoms in length. They are the major end products of microbial fermentation in the ruminant digestive tract and have also been implicated in the causation of neurological diseases in humans.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Fungi: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Genes, Bacterial: The functional hereditary units of BACTERIA.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Acidosis: A pathologic condition of acid accumulation or depletion of base in the body. The two main types are RESPIRATORY ACIDOSIS and metabolic acidosis, due to metabolic acid build up.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Nitrogen Isotopes: Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Fish Proteins: Proteins obtained from species of fish (FISHES).Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.MethylaminesChromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Carbohydrate Conformation: The characteristic 3-dimensional shape of a carbohydrate.DNA Glycosylases: A family of DNA repair enzymes that recognize damaged nucleotide bases and remove them by hydrolyzing the N-glycosidic bond that attaches them to the sugar backbone of the DNA molecule. The process called BASE EXCISION REPAIR can be completed by a DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE which excises the remaining RIBOSE sugar from the DNA.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Temperature: 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.Urea Cycle Disorders, Inborn: Rare congenital metabolism disorders of the urea cycle. The disorders are due to mutations that result in complete (neonatal onset) or partial (childhood or adult onset) inactivity of an enzyme, involved in the urea cycle. Neonatal onset results in clinical features that include irritability, vomiting, lethargy, seizures, NEONATAL HYPOTONIA; RESPIRATORY ALKALOSIS; HYPERAMMONEMIA; coma, and death. Survivors of the neonatal onset and childhood/adult onset disorders share common risks for ENCEPHALOPATHIES, METABOLIC, INBORN; and RESPIRATORY ALKALOSIS due to HYPERAMMONEMIA.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Intramolecular Lyases: Enzymes of the isomerase class that catalyze reactions in which a group can be regarded as eliminated from one part of a molecule, leaving a double bond, while remaining covalently attached to the molecule. (From Enzyme Nomenclature, 1992) EC 5.5.Air: The mixture of gases present in the earth's atmosphere consisting of oxygen, nitrogen, carbon dioxide, and small amounts of other gases.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Enzyme Stability: 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.AminohydrolasesBacteria: 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.Heparitin Sulfate: A heteropolysaccharide that is similar in structure to HEPARIN. It accumulates in individuals with MUCOPOLYSACCHARIDOSIS.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Animal Feed: Foodstuff used especially for domestic and laboratory animals, or livestock.Chromatography: Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.Oncorhynchus mykiss: A large stout-bodied, sometimes anadromous, TROUT found in still and flowing waters of the Pacific coast from southern California to Alaska. It has a greenish back, a whitish belly, and pink, red, or lavender stripes on the sides, with usually a sprinkling of black dots. It is highly regarded as a sport and food fish. Its former name was Salmo gairdneri. The sea-run rainbow trouts are often called steelheads. Redband trouts refer to interior populations of rainbows.Persea: A plant genus in the LAURACEAE family. The tree, Persea americana Mill., is known for the Avocado fruit, the food of commerce.Ketoglutaric Acids: A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Oligosaccharides: 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 crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme. (1/224)

BACKGROUND: The bifunctional enzyme formiminotransferase-cyclodeaminase (FTCD) contains two active sites at different positions on the protein structure. The enzyme binds a gamma-linked polyglutamylated form of the tetrahydrofolate substrate and channels the product of the transferase reaction from the transferase active site to the cyclodeaminase active site. Structural studies of this bifunctional enzyme and its monofunctional domains will provide insight into the mechanism of substrate channeling and the two catalytic reactions. RESULTS: The crystal structure of the formiminotransferase (FT) domain of FTCD has been determined in the presence of a product analog, folinic acid. The overall structure shows that the FT domain comprises two subdomains that adopt a novel alpha/beta fold. Inspection of the folinic acid binding site reveals an electrostatic tunnel traversing the width of the molecule. The distribution of charged residues in the tunnel provides insight into the possible mode of substrate binding and channeling. The electron density reveals that the non-natural stereoisomer, (6R)-folinic acid, binds to the protein; this observation suggests a mechanism for product release. In addition, a single molecule of glycerol is bound to the enzyme and indicates a putative binding site for formiminoglutamate. CONCLUSIONS: The structure of the FT domain in the presence of folinic acid reveals a possible novel mechanism for substrate channeling. The position of the folinic acid and a bound glycerol molecule near to the sidechain of His82 suggests that this residue may act as the catalytic base required for the formiminotransferase mechanism.  (+info)

Mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Proton nuclear magnetic resonance studies of the binding of adenine nucleosides and substrate to ethanolamine ammonia-lyase. (2/224)

Proton NMR spectroscopy was used to study the binding of adenosine, 5'-deoxyadenosine, adenine, and ethanolamine to the adenosylcobalamin-dependent enzyme ethanolamine ammonia-lyase. Broadening of ligand resonances in the presence of ethanolamine ammonia-lyase indicated that adenosine, 5'-deoxyadenosine, and ethanolamine all formed complexes with the enzyme (KD(mM) = 3.5, 3.0, and 2.5 respectively). The methyl group of enzyme-bound 5'-deoxyadenosine rotated at a rate exceeding 10(7) revolutions/s. Adenine did not appear to bind to the enzyme. Rates of dissociation of nucleosides from the enzyme were fast on the NMR time scale, precluding measurements of rate constants for the binding reaction. The departure of ethanolamine was slow, however, permitting their determination. The values for these rate constants were: k1 = 4.4 times 10(5) M-1 S-1; k-1 = 1.1 times 10(3) S-1. Addition of 1 mol of cyanocobalamin/mol of active sites led to narrowing of the enzyme-broadened ligand resonances. With 5'-deoxyadenosine, linewidths still exceeded those of the free ligand, indicating that binding to enzyme was weakened but not abolished. The KD for this nucleoside in the presence of CNCbl was 8.0 mM. With ethanolamine and adenosine, however, linewidths reverted to values characteristic of the unbound ligand, indicating either that CNCbl greatly lowered the rate of dissociation of the ligand or displaced the ligand from the enzyme. A decision between these two possibilities could not be made from the data at hand, although analogy with the situation obtaining with 5'-deoxyadenosine suggests that adenosine is displaced from the enzyme by CNCbl. 5'-Deoxyadenosine inhibited catalytic activity of the enzyme, competing with adenosylcobalamin (Ki = 2.7 mM). Adenosine had no effect, despite NMR evidence indicating that it formed a complex with free enzyme. These experiments showed that ethanolamine ammonia-lyase possesses binding sites for adenine nucleosides, a class of compounds chemically related to the Cobeta-ligand of the cofactor, as well as for ethanolamine. Binding to the enzyme has now been demonstrated for all three categories of low molecular weight compounds thought to be involved in the reaction; namely, substrate (ethanolamine), corrin, and adenine nucleoside.  (+info)

Interaction between ethanolamine ammonia-lyase and methylcobalamin. Half-site reactivity with an adenosylcobalamin-dependent enzyme. (3/224)

The adenosylcobalamin-dependent enzyme ethanolamine ammonia-lyase contains two active sites per molecule. The effects of methylcobalamin on the properties of this enzyme differ qualitatively depending on whether one or both of these sites is occupied by the cobamide. At 0.5 mol of methylcobalamin/mol of active sites, catalytic activity fell rapidly to approximately 30% of control levels, thereafter remaining constant for an hour. With the partially inhibited enzyme, Km values for ethanolamine and adenosylcobalamin were 5.5 muM and 1.6 muM, respectively, values that do not differ significantly from those of uninhibited enzyme. When the methylcobalamin per active site ratio was increased to 1, the decline in activity became progressive with time, eventually falling to levels much lower than seen at a cobamide per active site ratio of 0.5. Methylcobalamin also promotes the formation of a complex stable to gel filtration between ethanolamine and enzyme. Complex formation increased with increasing methylcobalamin per active site ratios up to a ratio of 0.7/1, at which point 0.5 mol of ethanol/mol of active sites was taken up. Ethanolamine uptake did not increase at higher methylcobalamin to active sites ratios. Methylcobalamin itself was taken up by enzyme, forming a complex containing 0.5 mol of methylcobalamin/mol of active sites that was stable to gel filtration. Measurement by the technique of Hummel and Dreyer ((1962) Biochim. Biophys. Acta 63, 530-532), however, showed one methylcobalamin binding site per active site. The formation of enzyme-ligand complexes stable to gel filtration was not affected by 5'-deoxyadenosine nor did 5'-deoxyadenosine by itself promote the formation of a stable complex between enzyme and ethanolamine. These observations were interpreted as evidence indicating half-site reactivity of ethanolamine ammonia-lyase with methylcobalamin. Comparison with previous results suggested that this half-site reactivity was an epiphenomenon not related to catalysis.  (+info)

The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. The source of the third methyl hydrogen in the 5'-deoxyadenosine generated from the cofactor during catalysis. (4/224)

Ethanolamine ammonia-lyase is an adenosylcobalamin-dependent enzyme which catalyzes the conversion of ethanolamine and propanolamine to ammonia and the corresponding aldehydes. A mechanism has been proposed for this and other adenosylcobalamin-dependent reactions which involves cleavage of the carbon-cobalt bond of the cofactor followed by abstraction of a substrate hydrogen atom by the adenosyl fragment to form 5'-deoxyadenosine. In support of this proposal, a previous study demonstrated that the deamination of propanolamine by ethanolamine ammonia-lyase is accompanied by the reversible cleavage of the carbon-cobalt bond of the cofactor, with the production of 5'-deoxyadenosine (Babior, B.M., Carty, T.J., and Abeles, R.H. (1974) J. Biol. Chem. 249, 1689-1695). The present study is concerned with the origin of the third hydrogen atom on the methyl group of the 5'-deoxyadenosine produced in that reaction. The 5'-deoxyadenosine isolated from an incubation mixture initially containing enzyme, [5',5'-D2]adenosylcobalamin, and [1,1-D2]propanolamine was chemically degraded so that the 4' and 5' carbon atoms were, respectively, converted to the carbonyl and methyl carbons of acetaldehyde. Analysis of the p-nitrophenylhydrazone of the acetaldehyde by gas-liquid chromatography-mass spectroscopy revealed 3 deuterium atoms/molecule, indicating that two of the methyl hydrogens originated from adenosylcobalamin and the third was donated by substrate. This observation provides further support for the participation of 5'-deoxyadenosine in the mechanism of adenosylcobalamin-dependent reactions.  (+info)

Cloning and characterization of the pnb genes, encoding enzymes for 4-nitrobenzoate catabolism in Pseudomonas putida TW3. (5/224)

Pseudomonas putida strain TW3 is able to metabolize 4-nitrotoluene via 4-nitrobenzoate (4NBen) and 3, 4-dihydroxybenzoic acid (protocatechuate [PCA]) to central metabolites. We have cloned, sequenced, and characterized a 6-kbp fragment of TW3 DNA which contains five genes, two of which encode the enzymes involved in the catabolism of 4NBen to PCA. In order, they encode a 4NBen reductase (PnbA) which is responsible for catalyzing the direct reduction of 4NBen to 4-hydroxylaminobenzoate with the oxidation of 2 mol of NADH per mol of 4NBen, a reductase-like enzyme (Orf1) which appears to have no function in the pathway, a regulator protein (PnbR) of the LysR family, a 4-hydroxylaminobenzoate lyase (PnbB) which catalyzes the conversion of 4-hydroxylaminobenzoate to PCA and ammonium, and a second lyase-like enzyme (Orf2) which is closely associated with pnbB but appears to have no function in the pathway. The central pnbR gene is transcribed in the opposite direction to the other four genes. These genes complete the characterization of the whole pathway of 4-nitrotoluene catabolism to the ring cleavage substrate PCA in P. putida strain TW3.  (+info)

A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton. (6/224)

The integration of the vimentin intermediate filament (IF) cytoskeleton and cellular organelles in vivo is an incompletely understood process, and the identities of proteins participating in such events are largely unknown. Here, we show that the Golgi complex interacts with the vimentin IF cytoskeleton, and that the Golgi protein formiminotransferase cyclodeaminase (FTCD) participates in this interaction. We show that the peripherally associated Golgi protein FTCD binds directly to vimentin subunits and to polymerized vimentin filaments in vivo and in vitro. Expression of FTCD in cultured cells results in the formation of extensive FTCD-containing fibers originating from the Golgi region, and is paralleled by a dramatic rearrangements of the vimentin IF cytoskeleton in a coordinate process in which vimentin filaments and FTCD integrate into chimeric fibers. Formation of the FTCD fibers is obligatorily coupled to vimentin assembly and does not occur in vim(-/-) cells. The FTCD-mediated regulation of vimentin IF is not a secondary effect of changes in the microtubule or the actin cytoskeletons, since those cytoskeletal systems appear unaffected by FTCD expression. The assembly of the FTCD/vimentin fibers causes a coordinate change in the structure of the Golgi complex and results in Golgi fragmentation into individual elements that are tethered to the FTCD/vimentin fibers. The observed interaction of Golgi elements with vimentin filaments and the ability of FTCD to specifically interacts with both Golgi membrane and vimentin filaments and promote their association suggest that FTCD might be a candidate protein integrating the Golgi compartment with the IF cytoskeleton.  (+info)

Quantitative measurement of the course of bean callus differentiation. (7/224)

Two strains of callus have been isolated from bean hypocotyl and grown on a defined maintenance medium supplemented with 2 mg/l. 2:4-dichlorophenoxyacetic acid (2:4D) and 2% sucrose. Root initiation was observed in one strain and formation of nodules containing xylem and phloem in both strains after transfer to an induction medium supplemented with 1 mg/l. naphthyleneacetic acid, 0-2 mg/l. kinetin and 3% sucrose, after 3 transfers to maintenance medium. The number of nodules per gramme increased 10-fold between 6 and 12 days after transfer, and thereafter remained constant. Phenylalanine ammonia lyase (PAL) activity rose to a maximum value when the rate of nodule formation was greatest, and decreased after the maximum nodule concentration was reached. The final constant value for PAL activity was above that of callus grown on maintenance medium. Beta I leads to 3 glucan synthetase activity rose to a maximum 15 days after transfer, and then fell gradually to a level above that measured in callus on maintenance medium. Callus was transferred from maintenance medium after 3, 4, 5 and 6 transfers. The concentration of nodules after 21 days on induction medium decreased as the callus was kept in culture. No further differentiation could be induced after 6 transfers. The fall in nodule formation was paralleled by a decrease in PAL and betaI leads to 3 glucan synthetase activities measured 21 days after transfer.  (+info)

Methanococcus jannaschii generates L-proline by cyclization of L-ornithine. (8/224)

Cell extracts of Methanococcus jannaschii have been shown to readily convert L-ornithine to L-proline. This cyclization reaction proceeds with the loss of only the C-2 nitrogen, as has been documented for ornithine cyclodeaminase (EC 4.3.1.12). Since no gene homologous to that coding for ornithine cyclodeaminase is present in the genome of M. jannaschii, these results indicate that proline biosynthesis in M. jannaschii is accomplished by a previously unrecognized enzyme.  (+info)

*Histidine ammonia-lyase

Histidase converts histidine into ammonia and urocanic acid. Histidine ammonia-lyase is a cytosolic enzyme catalyzing the first ... Histidine ammonia-lyase (or histidase, or histidinase) is an enzyme that in humans is encoded by the HAL gene. ... Histidine Ammonia-Lyase at the US National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text ... Schwede, TF; Rétey, J; Schulz, GE (Apr 27, 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide ...

*Threonine ammonia-lyase

... is a tetramer of identical subunits, and is arranged as a dimer of dimers. Each subunit has two domains ... Threonine ammonia-lyase is a member of the Fold Type II family, also known as the tryptophan synthase family. Though threonine ... Threonine ammonia-lyase is not found in humans. Thus, this is one example of why humans cannot synthesize all 20 proteinogenic ... In fact, threonine ammonia-lyase has been shown to exhibit some specificity towards serine and can convert serine into pyruvate ...

*D-serine ammonia-lyase

In enzymology, a D-serine ammonia-lyase (EC 4.3.1.18) is an enzyme that catalyzes the chemical reaction D-serine ⇌ {\ ... and D-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism. It employs one ...

*Tyrosine ammonia-lyase

Tyrosine ammonia lyase (L-tyrosine ammonia-lyase, TAL or Tyrase) is an enzyme in the natural phenols biosynthesis pathway. It ... phenylalanine ammonia-lyase) EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase) Louie, G.V.; Bowman, M.E.; Moffitt, M.C.; Baiga ... "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chem ... Tyrosine ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH) www.hhmi.org Molecular and ...

*Methylaspartate ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a methylaspartate ammonia-lyase (EC 4.3.1.2) is an enzyme that catalyzes the chemical reaction L-threo-3- ... and L-threo-3-methylaspartate ammonia-lyase. This enzyme participates in c5-branched dibasic acid metabolism and nitrogen ... "Insights into Enzyme Evolution Revealed by the Structure of Methylaspartate Ammonia Lyase". Structure. 10 (1): 105-13. doi: ...

*Phenylalanine ammonia-lyase

L-tyrosine ammonia-lyase, phenylalanine ammonium-lyase, PAL, and L-phenylalanine ammonia-lyase. Phenylalanine ammonia lyase is ... phenylalanine ammonia-lyases), EC 4.3.1.25 (tyrosine ammonia-lyases), and EC 4.3.1.26 (phenylalanine/tyrosine ammonia-lyases). ... Phenylalanine ammonia lyase (EC 4.3.1.24) is an enzyme that catalyzes a reaction converting L-phenylalanine to ammonia and ... The enzyme is a member of the ammonia lyase family, which cleaves carbon-nitrogen bonds. Like other lyases, phenylalanine ...

*Dihydroxyphenylalanine ammonia-lyase

... ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ammonia-lyase. This enzyme participates in tyrosine metabolism. MacLeod NJ; ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a dihydroxyphenylalanine ammonia-lyase (EC 4.3.1.11) is an enzyme that catalyzes the chemical reaction 3,4- ... 4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming). Other names in common use include beta-(3,4-dihydroxyphenyl ...

*Ethanolamine ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, an ethanolamine ammonia-lyase (EC 4.3.1.7) is an enzyme that catalyzes the chemical reaction ethanolamine ⇌ {\ ... name of this enzyme class is ethanolamine ammonia-lyase (acetaldehyde-forming). This enzyme is also called ethanolamine ...

*Glucosaminate ammonia-lyase

... aminodeoxygluconate ammonia-lyase, 2-amino-2-deoxy-D-gluconate ammonia-lyase, and D-glucosaminate ammonia-lyase. This enzyme ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a glucosaminate ammonia-lyase (EC 4.3.1.9) is an enzyme that catalyzes the chemical reaction D-glucosaminate ... name of this enzyme class is D-glucosaminate ammonia-lyase (isomerizing 2-dehydro-3-deoxy-D-gluconate-forming). Other names in ...

*Aspartate ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction L-aspartate ⇌ {\ ... and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. As of late ... name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric ...

*Diaminopropionate ammonia-lyase

... beta-diaminopropionate ammonia-lyase, 2,3-diaminopropionate ammonia-lyase, and 2,3-diaminopropanoate ammonia-lyase. It employs ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a diaminopropionate ammonia-lyase (EC 4.3.1.15) is an enzyme that catalyzes the chemical reaction 2,3- ... Nagasawa T, Tanizawa K, Satoda T, Yamada H (1988). "Diaminopropionate ammonia-lyase from Salmonella typhimurium Purification ...

*Serine-sulfate ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a serine-sulfate ammonia-lyase (EC 4.3.1.10) is an enzyme that catalyzes the chemical reaction L-serine O- ... name of this enzyme class is L-serine-O-sulfate ammonia-lyase (pyruvate-forming). This enzyme is also called (L-SOS)lyase. ...

*Phenylalanine/tyrosine ammonia-lyase

Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. (1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity ... "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chem ... Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine(or ... Phenylalanine/tyrosine ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...

*Threo-3-hydroxy-D-aspartate ammonia-lyase

CS1 maint: Multiple names: authors list (link) Threo-3-hydroxy-D-aspartate ammonia-lyase at the US National Library of Medicine ... Threo-3-hydroxy-D-aspartate ammonia-lyase (EC 4.3.1.27, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic ... name threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming). This enzyme catalyses the following chemical reaction ...

*L-serine ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a L-serine ammonia-lyase (EC 4.3.1.17) is an enzyme that catalyzes the chemical reaction L-serine ⇌ {\ ... name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L- ... hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme ...

*Carbamoyl-serine ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a carbamoyl-serine ammonia-lyase (EC 4.3.1.13) is an enzyme that catalyzes the chemical reaction O-carbamoyl-L- ... and O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). It employs one cofactor, pyridoxal phosphate. Copper AJ, Meister A ( ... name of this enzyme class is O-carbamoyl-L-serine ammonia-lyase (decarboxylating pyruvate-forming). Other names in common use ...

*Beta-alanyl-CoA ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a beta-alanyl-CoA ammonia-lyase (EC 4.3.1.6) is an enzyme that catalyzes the chemical reaction beta-alanyl-CoA ... This enzyme is also called beta-alanyl coenzyme A ammonia-lyase. This enzyme participates in beta-alanine metabolism and ... name of this enzyme class is beta-alanyl-CoA ammonia-lyase (acryloyl-CoA-forming). ...

*Threo-3-hydroxyaspartate ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction threo-3 ... and threo-3-hydroxy-L-aspartate ammonia-lyase. N, Yamada H, Shimizu S (1999). "Purification and characterization of a novel ... name of this enzyme class is threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use ...

*3-aminobutyryl-CoA ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... In enzymology, a 3-aminobutyryl-CoA ammonia-lyase (EC 4.3.1.14) is an enzyme that catalyzes the chemical reaction L-3- ... and L-3-aminobutyryl-CoA ammonia-lyase. Jeng I, Barker HA (October 1974). "Purification and properties of l-3-aminobutyryl ... name of this enzyme class is L-3-aminobutyryl-CoA ammonia-lyase (crotonoyl-CoA-forming). Other names in common use include L-3- ...

*Erythro-3-hydroxyaspartate ammonia-lyase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating), and erythro-3-hydroxy-Ls-aspartate ammonia-lyase. It employs one ... In enzymology, an erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) is an enzyme that catalyzes the chemical reaction ... name of this enzyme class is erythro-3-hydroxy-Ls-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use ...

*Eric Conn

Conn researched phenylalanine ammonia-lyase and cyanogenic glycosides. In 1988, he was elected to the National Academy of ...

*Pisatin

Wanner, L.A.; Ware, D.; Somssich, I.E.; Davis, K.R. (1995). "The phenylalanine ammonia-lyase gene family in Arabidopsis ...

*Phenylpropanoid

Role of bifunctional ammonia-lyase in grass cell wall biosynthesis. Nat. Plants. 2: 16050. doi:10.1038/nplants.2016.50. PMID ... Phenylalanine is first converted to cinnamic acid by the action of the enzyme phenylalanine ammonia-lyase (PAL). Some plants, ... In the orchid Phalaenopsis, phenylpropanoid enzymes (shikimate dehydrogenase, phenylalanine ammonia-lyase (PAL) and cinnamyl ... use tyrosine to synthesize p-coumaric acid by the action of the bifunctional enzyme Phenylalanine/tyrosine ammonia-lyase (PTAL ...

*Histidine

The enzyme histidine ammonia-lyase converts histidine into ammonia and urocanic acid. A deficiency in this enzyme is present in ... Overall, these reactions result in the formation of glutamate and ammonia. Glutamate can then be deaminated by glutamate ...

*James Bidlack

Phenylalanine ammonia lyase as a precursory enzyme of legume stem lignification. Can. J. Plant Sci. 75:135-140. Bidlack, J.E., ... Arthropod population, phenylalanine ammonia lyase activity, and fresh weight of sweet basil (Ocimum basilicum) as affected by ... Phenylalanine ammonia lyase and syringaldazine oxidase activities in relation to lignin deposition in legumes. Recent Res. ...

*Ornithine cyclodeaminase

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... and L-ornithine ammonia-lyase (cyclizing). This enzyme participates in arginine and proline biosynthesis. It employs one ... name of this enzyme class is L-ornithine ammonia-lyase (cyclizing; L-proline-forming). Other names in common use include ...
Kwiatkowski, M, Wang, J, Forster, A C. Manuscript in preparation on improved synthesis of unnatural aminoacyl-tRNAs. Gynnå, A H, Gullberg, E, Forster, A C. Generalizable tailoring of inhibition and fitness costs of artificial small RNAs in E. coli. Submitted. AD Edlund, S Jamal, H Elofsson, P Yuen, K Dyrhage, E Marklund, J Liljeruhm, M Nissbeck, A Gynnå, C Ahlström, L Alexis, N Anlind, AA Avalos, A Berglund, M Bergman, M Beyan, V Blomkvist, M Borg, F Boström, K Braesch-Andersen, L Bransell, J Brisvåg, P Cederberg, S Ciftci, T Dalmo, P Danielsson, C Frisk, H Gavali, SMR Gunja, A Gustafsson, S Herman, K Holdar, M Hong, K Ivermark, J Karlsson, K Lundmark, J Lövgren, T Löwe, O Nordesjö, A Nyberg, L Pello-Esso, L Pettersson, A Saffari, N Sandberg, CO Sidibeh, V Sjöstedt, J Spaak, A Srivastava, M Strandgren, L Sun, V Törnblom, E Vu, A Wirtanen, C Wärn, J Ås, C Östlin, G Johansson, A Virtanen, AC Forster, ER Lundin and E Gullberg. Optimizing chromoproteins and tyrosine ammonia-lyase for ...
NIH Rare Diseases : 50 glutamate formiminotransferase deficiency is an inheritedmetabolic disorder that affects physical and mental development. there are two forms of this condition, a mild form and a severe form. people with the mild form have minor delays in physical and mental development and may have mild intellectual disability. they also have unusually high levels of a molecule called formiminoglutamate (figlu) in their urine. individuals with the severe form have profound intellectual disability, delayed development of motor skills (sitting, standing, and walking) and megaloblastic anemia. in addition to figlu in their urine, they have elevated amounts of certain b vitamins (called folates) in their blood. glutamate formiminotransferase deficiency is caused by mutations in the ftcd gene. it is inherited in an autosomal recessive pattern. there are currently no treatments known to prevent or delay the signs and symptoms of glutamate formiminotransferase deficiency. last updated: 8/10/2016 ...
Looking for online definition of ammonia-lyases in the Medical Dictionary? ammonia-lyases explanation free. What is ammonia-lyases? Meaning of ammonia-lyases medical term. What does ammonia-lyases mean?
Shop Histidine ammonia-lyase ELISA Kit, Recombinant Protein and Histidine ammonia-lyase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Ornithine cyclodeaminase (OCD) is an NAD+-dependent deaminase that is found in bacterial species such as Pseudomonas putida. Importantly, it catalyzes the direct conversion of the amino acid L-ornithine to L-proline. Using molecular dynamics (MD) and a hybrid quantum mechanics/molecular mechanics (QM/MM) method in the ONIOM formalism, the catalytic mechanism of OCD has been examined. The rate limiting step is calculated to be the initial step in the overall mechanism: hydride transfer from the L-ornithines Cα-H group to the NAD+ cofactor with concomitant formation of a Cα=NH2+ Schiff base with a barrier of 90.6 kJ mol−1. Importantly, no water is observed within the active site during the MD simulations suitably positioned to hydrolyze the Cα=NH2+ intermediate to form the corresponding carbonyl. Instead, the reaction proceeds via a non-hydrolytic mechanism involving direct nucleophilic attack of the δ-amine at the Cα-position. This is then followed by cleavage and loss of the α-NH2 group to give
1AH5: Determination of the structure of seleno-methionine-labelled hydroxymethylbilane synthase in its active form by multi-wavelength anomalous dispersion.
We previously reported 2 osteoporosis-susceptibility genes--formiminotransferase N-terminal sub-domain containing gene (FONG) and thrombospondin, type 1, domain-containing 7A (THSD7A)--in which we identified two common single-nucleotide polymorphisms
American Phytopathological Society Board & Staff. VIEW ABSTRACT , VIEW ARTICLE The Relationship Between Glycoalkaloids and Disease Resistance in Potatoes. J. A. Frank, J. M. Wilson, and R. E. Webb. Pages 1045-1049. VIEW ABSTRACT , VIEW ARTICLE Levels of Chlorogenic Acid in Tobacco Cultivars, Healthy and Infected with Thielaviopsis basicola. S. K. Gayed, Nestor Rosa. Pages 1049-1053. VIEW ABSTRACT , VIEW ARTICLE On Exclusion as the Mechanism of Ozone Resistance in Virus-Infected Plants. Eileen Brennan. Pages 1054-1055. VIEW ABSTRACT , VIEW ARTICLE Attempts to Use Satellite Data to Detect Vegetative Damage and Alteration Caused by Air and Soil Pollutants. E. L. Fritz, S. P. Pennypacker. Pages 1056-1060. VIEW ABSTRACT , VIEW ARTICLE , VIEW ERRATUM Types of Germination and Differentiation of Vesicles by Basidiospores of Cronartium ribicola. Everett M. Hansen, Robert F. Patton. Pages 1061-1071. VIEW ABSTRACT , VIEW ARTICLE Phenylalanine Ammonia-lyase, Tyrosine Ammonia-lyase, and Lignin in Wheat ...
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Kwiatkowski, M, Wang, J, Forster, A C. Manuscript in preparation on improved synthesis of unnatural aminoacyl-tRNAs. Edlund, A, Jamal, S, Elofsson, H, Yuen, P, Dyrhagen, K, Marklund, E, Liljeruhm, J, Nissbeck, M, Gynnå, A, Ahlström, C, Alexis, L, Anlind, N, Ascue Avalos, G A, Berglund, A, Bergman, M, Beyan, M, Blomkvist, V, Borg, M, Boström, F, Braesch-Andersen, K, Bransell, L, Brisvåg, J, Cederberg, P, Ciftci, S, Dalmo, T, Danielsson, P, Frisk, C, Gavali, H, Gunja, S, Gustafsson, A, Herman, S, Holdar, K, Hong, M, Karlsson, J, Lundmark, K, Löwe, T, Nordsjö, O, Nyberg, A, Pello-Esso, L, Pettersson, L, Saffari, A, Sandberg, N, Sidibeh, C, Sjöstedt, V, Spaak, J, Srivastava, A, Strandgren, M, Sun, L, Törnblom, V, Vu, E, Wirtanen, A, Wärn, C, Ås, J, Östlin, C, Virtanen, A, Forster, A C, Lundin, E, Gullberg, E. Optimizing chromoproteins and tyrosine ammonia-lyase for use in Escherichia coli. Under revision for ACS Synthetic Biology. Liljeruhm, J, Gullberg, E, Forster A C. Synthetic biology: ...
Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J. and Schmidt-Dannert, C. (2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chem. Biol. 13: 1317-1326. PMID 17185227. ...
Human formiminotransferase cyclodeamidase (FTCD) is an approximately 60 kDa, liver specific, bifunctional enzyme, involved in both histidine and folate metabolism. It is identical with the so-called liver cytosol type 1 antigen (LC1), and has been reported to oligomerize in the cytoplasm. DIARECT™ antigens are for further manufacturing or research use only. ...
Porphobilinogen deaminase mutants that cause acute intermittent porphyria have been investigated as recombinant proteins expressed in Escherichia coli, yielding important insight into the mechanism of dipyrromethane cofactor assembly and tetrapyrrole chain polymerization. A mutation that affects a key catalytic residue, D99G, results in an inactive holo-protein that exists as a complex with two substrate molecules covalently bound to the dipyrromethane cofactor arising from the reaction between the apo-protein and pre-uroporphyrinogen. The R149Q mutant is also devoid of catalytic activity but the mutant protein is unable to assemble the dipyrromethane cofactor from pre-uroporphyrinogen and persists as an unstable, heat-labile apo-protein. The mutant, R173Q, has very low activity and, like R149Q, also exhibits largely as an apo-protein. The inability to reconstitute either R149Q or R173Q with exogenous pre-uroporphyrinogen confirms the importance of these two arginine residues for dipyrromethane ...
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SARAH J. AWAN, GIULIANO SILIGARDI, MARTIN J. WARREN, PETER M. SHOOLINGIN-JORDAN; Discovery of a novel mechanism for cofactor assembly by Escherichia coli porphobilinogen deaminase. Biochem Soc Trans 1 February 1997; 25 (1): 79S. doi: https://doi.org/10.1042/bst025079s. Download citation file:. ...
Epithelial and fibroblast cells were obtained from cultures of amniotic fluid cells. Epithelial cells demonstrated high activities of histidase. In contrast, histidase activity was not detected in fibroblasts derived from the same original culture. This observation indicates that cultures of amniotic fluid cells consist of cells with different biochemical properties as well as morphological characteristics. ...
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The nucleotide sequences of two segments of DNA (2250 and 2921 base-pairs) containing the functionally related fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12 were determined. The fumC structural gene comprises 1398 base-pairs (466 codons, excluding the initiation codon), and it encodes a polypeptide of Mr 50353 that resembles the fumarases of Bacillus subtilis 168 (citG-gene product), rat liver and pig heart. The fumC gene starts 140 base-pairs downstream of the structurally-unrelated fumA gene, but there is no evidence that both genes form part of the same operon. The aspA structural gene comprises 1431 base-pairs (477 codons excluding the initiation codon), and it encodes a polypeptide of Mr 52190, similar to that predicted from maxicell studies and for the enzyme from E. coli W. Remarkable homologies were found between the primary structures of the fumarase (fumC and citG) and aspartase (aspA) genes and their products, suggesting close structural and evolutionary ...
The roots will split and form legs if you allow the soil to become too dry. Water and mulch regularly if youre experiencing a dry summer. They should be ready to harvest three or four months after seeding, you can also harvest it any time between late summer and mid-spring the following year. The root can be left in the ground all winter and dug up when you require. (Ref: Wikipedia - see link). Comments Warnings : This type of parsley produces much thicker roots than types cultivated for their leaves. Although seldom used in Britain and the United States, root parsley is very common in central and eastern European cuisine, where it is used in soups and stews. ...
The thesis describes the synthesis of new analogues (53-57) of PBG and their inhibition of and mechanistic studies on the enzyme PBG deaminase from E. coli. The analogues with an additional alkyl group, 53 and 54, were successfully obtained in good yields in 10 steps. The caged compound 97 was also obtained but the final step of hydrogenolysis of the benzyl protecting groups also caused reduction of the nitro group on the 2-nitrobenzyl substituent. Testing of analogues 53 and 54 with the enzyme (PBGD), however, showed no inhibition. A new route for the synthesis of the conformationally restricted analogue 6, 11-ethanoPBG 56 was developed in this work and one stereoisomer of 56 was obtained (the cis-isomer). When this analogue was tested as an inhibitor it also showed no inhibition. This was thought to be due to the stereochemistry of the compound since modelling studies had predicted that the trans-isomer would bind tightly to the enzyme not the cis-isomer. Therefore, the ...
Gene target information for HEM3 - hydroxymethylbilane synthase (Saccharomyces cerevisiae S288C). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
Porphobilinogen Deaminase; Catalyzes The Conversion Of 4-porphobilinogen To Hydroxymethylbilane, The Third Step In Heme Biosynthesis; Localizes To The Cytoplasm And Nucleus; Expression Is Regulated By Hap2p-Hap3p, But Not By Levels Of Heme
Thank you for your interest in spreading the word about Biochemical Society Transactions.. NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.. ...
1AJS: Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate.
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Complete information for HAL gene (Protein Coding), Histidine Ammonia-Lyase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
phenylalanine ammonia-lyase [putative phenylalanine ammonia lyase EncP] ATGACCTTCGTCATAGAGCTCGACATGAACGTCACGCTCGACCAACTTGAGGACGCGGCG CGACAGCGCACGCCCGTGGAGCTGTCCGCACCCGTCCGCTCCCGCGTCCGCGCCTCGCGC GACGTGTTGGTGAAGTTCGTGCAGGACGAACGTGTCATCTACGGGGTCAACACCAGCATG GGGGGCTTCGTCGACCACCTCGTCCCGGTGTCCCAGGCCCGGCAGCTCCAGGAGAACCTG ATCAACGCGGTCGCCACCAACGTGGGGGCGTATCTGGACGACACGACCGCCCGGACCATC ATGCTGTCCCGCATCGTGTCGCTGGCGCGCGGGAACTCCGCGATCACCCCGGCGAATCTG GACAAGCTGGTGGCCGTACTCAACGCCGGGATCGTGCCGTGCATCCCGGAGAAGGGCTCT TTGGGCACCAGCGGTGACCTCGGCCCGCTGGCCGCGATCGCCCTGGTGTGCGCGGGGCAG TGGAAGGCCCGCTACAACGGTCAGATCATGCCCGGGCGGCAGGCCCTGTCCGAGGCCGGC GTCGAGCCGATGGAGCTGAGCTACAAGGATGGCCTGGCCCTGATCAACGGCACGTCAGGC ATGGTCGGCCTGGGCACCATGGTCCTCCAGGCCGCGCGCCGGCTCGTGGACCGCTACCTG CAGGTGTCCGCGTTGTCGGTCGAGGGCCTGGCAGGCATGACGAAACCGTTCGACCCTCGC GTGCACGGCGTCAAGCCGCACCGCGGGCAGCGTCAGGTGGCCTCGCGGTTGTGGGAGGGG CTTGCCGACTCGCACCTGGCGGTCAACGAACTGGACACCGAGCAGACCCTGGCCGGAGAG ATGGGCACGGTCGCCAAGGCCGGTTCGCTGGCGATCGAGGACGCCTACTCCATCCGGTGC ...
ASPA山羊多克隆抗体(ab112530)可与小鼠, 大鼠样本反应并经WB实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
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Photo/image Capillary Thread-moss (Bryum capillare), Family: Bryaceae. Location Buderupholm Bjergskov, Rold Skov, Jylland, Danmark. Photographer: JC Schou, Photoid 54728
Plasmid pDONR223-SCYL2 from Dr. William Hahns lab contains the insert SCYL2 and is published in Nature. 2010 Nov 24. ():. This plasmid is available through Addgene.
PBGD_ : The porphyrias are a group of inherited disorders resulting from enzyme defects in the heme biosynthetic pathway. Acute intermittent porphyria (AIP) is caused by diminished erythrocyte activity of porphobilinogen deaminase (PBGD), also known as uroporphyrinogen I synthase or hydroxymethylbilane synthase. Onset of AIP typically occurs during puberty or later. Individuals may experience acute episodes of neuropathic symptoms. Common symptoms include severe abdominal pain, peripheral neuropathy, and psychiatric symptoms. Crises may be precipitated by a broad range of medications (including barbiturates and sulfa drugs), alcohol, infection, starvation, heavy metals, and hormonal changes. AIP is inherited in an autosomal dominant manner. At-risk family members of patients with a biochemical diagnosis of AIP should undergo appropriate testing. Timely diagnosis is important as acute episodes of AIP can be fatal. Treatment of AIP includes the prevention of symptoms through avoidance of precipitating
TY - JOUR. T1 - Asymptomatic erythrocyte disorder presenting as increased porphobilinogen deaminase and uroporphyrinogen decarboxylase.. AU - Anderson, Karl. AU - Goeger, D. E.. AU - Bessman, J. D.. PY - 1995/11. Y1 - 1995/11. UR - http://www.scopus.com/inward/record.url?scp=0029410609&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0029410609&partnerID=8YFLogxK. M3 - Article. C2 - 7586564. AN - SCOPUS:0029410609. VL - 41. SP - 1670. JO - Clinical Chemistry. JF - Clinical Chemistry. SN - 0009-9147. IS - 11. ER - ...
In enzymology, a dihydroxyphenylalanine ammonia-lyase (EC 4.3.1.11) is an enzyme that catalyzes the chemical reaction 3,4-dihydroxy-L-phenylalanine ⇌ {\displaystyle \rightleftharpoons } trans-caffeate + NH3 Hence, this enzyme has one substrate, 3,4-dihydroxy-L-phenylalanine (L-DOPA), and two products, trans-caffeate and NH3. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 3,4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming). Other names in common use include beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ammonia-lyase. This enzyme participates in tyrosine metabolism. MacLeod NJ; Pridham JB (1963). "Deamination of beta-(3,4-dihydroxyphenyl)-L-alanine by plants". Biochem. J. 88 (1): 45-52. PMC 1203845 . PMID 16749027. Molecular and Cellular Biology ...
Shop Aspartate ammonia-lyase ELISA Kit, Recombinant Protein and Aspartate ammonia-lyase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Khaw, L.E., Bohm, G.A., Metcalfe, S., Staunton, J. and Leadlay, P.F. (1998). „Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase". J. Bacteriol. 180: 809-814. PMID 9473033 ...
Brevibacillus brevis glutamyl-tRNA reductase (hemA) gene, partial cds; HemX(hemX) gene, complete cds; and porphobilinogen deaminase (hemC) gene,partial ...
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Acute intermittent porphyria (AIP) is a condition that can cause sudden, severe attacks of stomach pain that may last for a days to weeks. It is called a porphyria because substances called porphyrins build up in the body and can cause the symptoms. Porphyrins are normally used by the body to help cells use oxygen. In AIP, people may also experience mental changes in attacks of acute intermittent porphyria that can include insomnia or difficulty sleeping, anxiety, depression, hallucinations, confusion, paranoia, and amnesia or memory loss.. To understand more about AIP from someone who has the condition, watch this video from the American Porphyria Foundation.. ...
Another name for Intermittent Porphyria is Acute Intermittent Porphyria. What is acute intermittent porphyria? A person with acute intermittent porphyria ...
We report a case of early onset recurrent preeclampsia in a patient with positive family history of preeclampsia and a newly discovered acute intermittent porphyria. A 28 years old patient was admitted to our Clinic, due to early onset of preeclampsia in her third pregnancy. She had refractory hypertension with tachycardia, facial flush, anxiety and difficulty in breathing. During hospitalization, she reported occurrence of opalescent orange to reddish morning urine, which turned dark after a while. The dipstick test revealed positive urobilinogen in the urine. The same sample of urine was tested for porphobilinogens in the urine (by the use of Ehrlichs reagent) which were found positive and also porphyrins which were found negative; therefore, her medication was switched to a beta blocker. She decided to terminate pregnancy and this was done in the next few days by the use of anesthetics that are approved for acute intermittent porphyria. At her check up one month after delivery, her blood ...
Looking for online definition of aspartate ammonia-lyase in the Medical Dictionary? aspartate ammonia-lyase explanation free. What is aspartate ammonia-lyase? Meaning of aspartate ammonia-lyase medical term. What does aspartate ammonia-lyase mean?
Acute Intermittent porphyria (AIP) is a rare genetic disease which is caused by mutations in the porphobilinogen deaminase (PBGD) gene; one of the enzymes of the heme biosynthesis pathway. Mutations in this gene cause insufficient activity of the protein resulting in partially disruption of heme synthesis. This in turn leads to accumulation of toxic intermediates (ALA and PBG) giving rise to a wide variety of problems including acute, severe abdominal pains, psychiatric and neurological disorders, and muscular weakness. Acute porphyric attacks can be life-threatening and the long-term consequences include irreversible nerve damage, liver cancer and kidney failure. Currently, the only curative therapy is liver transplantation and thus, new curative options are urgently needed. Severe AIP patients are suffering poor quality of life with palliative treatments for the different symptoms including glucose or heme infusions for metabolic replacement and inhibition of toxic metabolic production.. About ...
A genetic survey which was carried out on 11 affected families with acute intermittent porphyria (AIP) confirmed autosomal dominant mode of transmission.
So Alone : A true, personal story from the experience, I Have Acute Intermittent Porphyria. As I lay here wondering how my life went from perfect ( for me) to this! How did I go from an able bodied mom and wife? I worked, cleaned and had dinner on the table when my husband got home. I was th...
Acute intermittent porphyria may present with symptoms and signs such as recurrent intermittent abdominal pain, peripheral neuropathy, hyporeflexia, hallucinations and blurred vision as well as neuropsychiatric signs.
Phenylalanine ammonia lyase (EC 4.3.1.24) is an enzyme that catalyzes a reaction converting L-phenylalanine to ammonia and trans-cinnamic acid. Phenylalanine ammonia lyase (PAL) is the first and committed step in the phenyl propanoid pathway and is therefore involved in the biosynthesis of the polyphenol compounds such as flavonoids, phenylpropanoids, and lignin in plants. Phenylalanine ammonia lyase is found widely in plants, as well as some yeast and fungi, with isoenzymes existing within many different species. It has a molecular mass in the range of 270-330 kDa. The activity of PAL is induced dramatically in response to various stimuli such as tissue wounding, pathogenic attack, light, low temperatures, and hormones. PAL has recently been studied for possible therapeutic benefits in humans afflicted with phenylketonuria. It has also been used in the generation of L-phenylalanine as precursor of the sweetener aspartame. The enzyme is a member of the ammonia lyase family, which cleaves ...
The amino acid histidine, when catalyzed by the enzyme histidase, forms urocanic acid. Disruptions in this pathway, caused by a deficiency of histidase, is the underlying cause of histidinemia. This results in reduced levels of skin and serum urocanic acid, the primary indicator of insufficient histidase activity. In urocanic aciduria, increased urocanic acid in the urine indicates a deficiency of the enzyme urocanase. This enzyme breaks down urocanic acid, forming formininoglutamic acid, and also forms imidazolonepropionic acid from trans-urocanic acid. With normal to only slightly elevated levels of histidine present in the liver during urocanic aciduria, the only true metabolic indicator of the disorder can be found in the urine.[2] ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Posted on September 2, 2013 by Ivan Gary The report firstly introduced L-Phenylalanine basic information included definition classification application industry chain structure industry overview; international market analysis, Global and China domestic market analysis, Macroeconomic environment and economic situation analysis and influence, L-Phenylalanine Industry policy and plan, L-Phenylalanine product specification, manufacturing process, product cost structure etc.. Browse Complete Report with TOC: http://www.qyresearchreports.com/report/global-and-china-l-phenylalanine-industry-2013-market-research-report.htm. Then statistics Global and China key manufacturers L-Phenylalanine capacity production cost price profit production value gross margin etc details information, at the same time, statistics these manufacturers L-Phenylalanine products customers application capacity market position information etc company related information, then collect all these manufacturers data and listed Global ...
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4-(Trifluoromethyl)-L-phenylalanine chemical properties, What are the chemical properties of 4-(Trifluoromethyl)-L-phenylalanine 114926-38-4, What are the physical properties of 4-(Trifluoromethyl)-L-phenylalanine ect.
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Information of L-Phenylalanine. L-Phenylalanine essential amino acid is classified as neutral and nonpolar because of the inert and hydrophobic.
Видеокамера предназначена для преобразования оптического изображения, создаваемого эндоскопом при всех видах эндоскопических исследований и операций, в полный телевизионный сигнал цветного изображения в системе PAL. Камерная головка видеокамеры снабжена объективом с переменным фокусным расстоянием. Видеокамера оснащена встроенным блоком питания, предназначенным для подключения светодиодного осветителя в вариантах его исполнения ...
Acute intermittent porphyria (AIP), the most common acute hepatic porphyria, is an autosomal dominant disorder with low penetrance that results from a partial deficiency of hydroxymethylbilane synthase (HMBS), the third enzyme in the heme biosynthetic pathway. The disease is clinically characterized by acute neurovisceral attacks that are precipitated by several factors including certain drugs, steroid hormones, alcohol and fasting. Early diagnosis and counselling are essential to prevent attacks, being mutation analysis the most reliable method to identify asymptomatic carriers in AIP families. In this study we have investigated the molecular defect in 15 unrelated Spanish AIP patients. Mutation analysis of the HMBS gene revealed a total of fourteen mutations including six novel ones, two of them were on the same allele in one patient. The novel mutations were three missense (R26L, R173G and D178H), two frameshift (c.749_765dup and c.874insC) and one intronic deletion ...
Acute intermittent porphyria is an inborn error of metabolism characterized by the excretion of excess porphyrin precursors (porphobilinogen and usually δ-aminolevulinic acid) in the urine, and by sporadic attacks of neurologic dysfunction. The disease is complex, involving variable patterns of autonomic and peripheral neuropathy as well as central nervous system manifestations. There may be alterations in carbohydrate, lipid, water, and electrolyte metabolism in addition to clinically inapparent endocrine abnormalities. The fundamental defect is thought to be a 50% decrease of uroporphyrinogen I synthetase, the third enzyme of the heme biosynthetic pathway. This is associated with a marked increase of hepatic δ-aminolevulinic acid synthetase, the first and rate controlling enzyme of the pathway. The measurement of uroporphyrinogen I synthetase in erythrocytes now provides an enzyme diagnostic test for the disease. Two therapeutic approaches that may prove to reverse the fundamental disease ...
Another name for Intermittent Porphyria is Acute Intermittent Porphyria. Home care for acute intermittent porphyria includes: * Do not drink alcohol. ...
Paenibacillus macerans glutamyl-tRNA reductase (hemA), siroheme synthase(cysG(B)), porphobilinogen deaminase (hemC), and uroporphyrinogen-IIImethyltransferase/uroporphyrinogen-III synthase (cysG(A)-hemD) genes,complete cds; and 5-aminolevulinic acid dehydratase (hemB) gene, ...
Paenibacillus macerans glutamyl-tRNA reductase (hemA), siroheme synthase(cysG(B)), porphobilinogen deaminase (hemC), and uroporphyrinogen-IIImethyltransferase/uroporphyrinogen-III synthase (cysG(A)-hemD) genes,complete cds; and 5-aminolevulinic acid dehydratase (hemB) gene, ...
SWISS-MODEL Repository entry for A8FKW8 (HEM3_CAMJ8), Porphobilinogen deaminase. Campylobacter jejuni subsp jejuni serotype O:6 (strain 81116 / NCTC11828)
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Labile Hypertension Possible Causes (Differential Diagnoses) include ❗ Labile Hypertension ❗ Acute Intermittent Porphyria ❗ Acute Hepatic Porphyria ❗ Check more at Symptoma.com
Thorazine (chlorpromazine) is used for treating nausea, vomiting, nervousness before surgery, acute intermittent porphyria, and tetanus.
Latitude longitude of Hortense Amsterdam in District of Columbia County, District of Columbia along with maps, comments, photos and links.
Specification sheet links below are a standard copy of the COA less the batch or lot number and manufactures dates. Specification sheet can be dated and should only be considered as a general information. Please contact and request an up to date COA if needed for specific updated information before placing order by filling out the contact form with product name and SKU number. If ordering quantities of twenty five kilos or more contact for availability ...
Chemical manipulations of pyrrolic compounds can often prove to be difficult. This is especially true for dipyrrins. As a result of this, methodology development for the chemical manipulation of pyrrolic compounds is of particular interest. The graduate work presented herein involves three projects dedicated to developing such methodologies. Based on microwave-promoted deprotection of F-BODIPYs previously developed by the Thompson group, an F-BODIPY was probed for use as a protecting group option for the manipulation of the parent dipyrrin. Rather than isolating the expected functional group interconversion product, the F-BODIPY was deprotected and the resulting dipyrrin was reduced to form its corresponding dipyrromethane in moderate yield. A series of reactions using similar conditions and substrates were performed to explore the scope of this reaction. Methodologies for the manipulation of functional groups can also prove useful when trying to improve the stability of a molecule. ...
C Aspa Scorb was formulated as a mineral transporter based on the results of studies by several researchers, principally Hans Neiper, M.D., West Germany.
Phenylalanine is an essential amino acid, which are building blocks for protein that you must get from dietary sources. L-phenylalanine is found in most...
You are viewing an interactive 3D depiction of the molecule 4-[difluoro(phosphono)methyl]-l-phenylalanine (C10H12F2NO5P) from the PQR.
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Structure, properties, spectra, suppliers and links for: L-(-)-Phenylalanine, Phenylalanine, L-Phenylalanine, 63-91-2, C6H5CH2CH(NH2)COOH.
Divalent dipeptides have been introduced as counter ions in aqueous CZE. The dipeptides form ion pairs with amino alcohols in the BGE and facilitate the separation of amino alcohols. High concentrations of dipeptide caused reversed effective mobility for the analytes. The net charge of the dipeptide can be controlled using a buffer or a strong base, and regulates the interaction between the dipeptide and the amino alcohol. A stronger interaction and higher selectivity of amino alcohols was observed when the dipeptides were used as divalent counter ions, than in monovalent or uncharged form. Association constants for ion pairs between divalent dipeptides and amino alcohols can be used to enhance selectivity for amino alcohols in CZE. No chiral separation of amino alcohols was observed when using the dipeptides as ion-pairing chiral selectors in aqueous BGE, but addition of methanol to the BGE promoted enantioselectivity.. ...
acute intermittent porphyria: 95% are erythroid type & 5% non-erythroid; blood test for PBG-deaminase will be low in the former but not necessarily in the 5% (but, in just population screening, the vast majority of instances of low PBG-deaminase are not AIP...so a low level is not diagnostic). A 24-hour urine test [CP07-17] collected in opaque container (protect from sunlight), clean catch & without preservative or chemicals, & keep specimen refrigerated (or ice slush in a cooler) at all times and direct lab that it must be kept refrigerated...test for PBG & delta ALA. Unless pain episode VERY remote, eryhtroid AIP should have an elevated urine PBG. Also use this specimen when 24 hour urine porphyrins are tested ...
Petroselinum sativum Hoffm.. Plants c. 1 m tall. Leaves petiolate, 2-3-pinnate; segments linear to lanceo¬late or oval, 1-3 cm long. Peduncles 3-15 cm long. Involucre of 1-3 linear bracts or lacking. Rays 10-20, subequal, up to 2.5 cm long. Involucel of 5-6 linear bractlets, shorter than the flowering umbellet. Calyx teeth obsolete. Petals green¬ish. Fruit ovoid, 2.5-3 mm long.. Type: Described from Sardinia, Italy. Distribution: A cosmopolitan plant. Parsley is a cultivated plant used for its edible foliage.. ...
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Hortense - No 266. LRV (Light Reflectance Value) - 55. A gentle lilac tone with a soft hint of grey - the aging petal colour, calm and beautiful.
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The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a…
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91417-78-6 - QHOOBIFBRLBIGF-KLSJZZFUSA-N - L-Phenylalanine, N-(1-(cyanomethyl)-2-pyrrolidinylidene)-, hydrate - Similar structures search, synonyms, formulas, resource links, and other chemical information.
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Levels of erythrocyte delta-aminolevulinate dehydratase [ALA-dehydratase; porphobilinogen synthase; 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing), EC 4.2.1.24], UROPORPHYRINOGEN-I synthase [Uro-synthase; porphobilinogen ammonia-lyase (polymerizing), EC 4.3;1.8], AND PROTOPORPHYRIN IX (Proto) were measured by sensitive semimicroassays using 2-5 mul of whole blood obtained from normal and anemic mutant mice. The levels of erythrocyte ALA-dehydratase and Uro-synthase showed marked developmental changes and ALA-dehydratase was influenced by the Lv gene. Mice with overt hemolytic diseases (ja/ja, sph/sph, nb/nb, ha/ha) had 10- to 20-fold increases in ALA-dehydratase, Uro-synthase, and Proto compared with their normal controls. Mice with an iron deficiency (mk/mk) and mice with hypoplastic anemias (W/Wv, Sl/Sld, an/an) had mild to moderate increases in these parameters. Elevated enzyme activities and Proto correlated well with the number of reticulocytes. Because all mice
To assess nickel-induced toxicity in plants, Zea mays seeds were germinated and cultured on nutrient solution with nickel concentrations of 50-200 μM for a period of two weeks. Observed biological makers included biomass, soluble and total protein contents, and the activities of guaiacol peroxidase (GPX), ascorbate peroxidase (APX), catalase (CAT), and phenylalanine ammonia-lyase (PAL) in the leaves and roots of maize. The fresh and dry weight of leaves and roots increased in 50 μM nickel but decreased in 100 and 200 μM. Soluble and total protein contents were significantly increased by increasing nickel concentrations up to 200 μM nickel in both roots and leaves of maize. Significant increases of ascorbate peroxidase (the highest activity at 200 μM nickel), catalase (the highest activity at 50 μM nickel), and phenylalanine ammonia-lyase (the highest activity at 100 μM nickel) were observed in the leaves and roots of Zea mays seedlings at all tested nickel concentrations. Guiacol peroxidase
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Phenylketonuria (PKU) was the first inherited metabolic disease in which dietary treatment was found to prevent the diseases clinical features. Treatment of phenylketonuria remains difficult due to progressive decrease in adherence to diet and the presence of neurocognitive defects despite therapy. This review aims to summarize the current literature on new treatment strategies. Additions to treatment include new, more palatable foods based on glycomacropeptide that contains very limited amount of aromatic amino acids, the administration of large neutral amino acids to prevent phenylalanine entry into the brain or tetrahydropterina cofactor capable of increasing residual activity of phenylalanine hydroxylase. Moreover, human trials have recently been performed with subcutaneous administration of phenylalanine ammonia-lyase, and further efforts are underway to develop an oral therapy containing phenylanine ammonia-lyase. Gene therapy also seems to be a promising approach in the near future.
Hollow fiber enzyme-reactors with immobilized phenylalanine ammonia-lyase (PAL) were developed for the in vivo depletion of phenylalanine (Phe) in circulating blood. A series of experiments was conducted with a large animal model in order to explore its safety for clinical use. The level of red blood cells, white blood cells and platelets did not change during a 2-hr application of the reactors in anesthetized, heparinized dogs and monkeys with experimental hyperphenylalaninemia. No increase in blood urea nitrogen was observed due to generation of ammonia from PAL-catalyzed Phe breakdown. The other metabolic product, trans-cinnamic acid, was reported to be nontoxic. Repeated application of the PAL-reactors to the same animals did not produce untoward physiological or immunological reactions. These data suggest that PAL-reactors may be safe for in vivo use to control excess Phe brought about by fever, infection or pregnancy in phenylketonuric individuals otherwise balanced by a Phe-poor diet. ...
The primer sequences are listed in Supplemental Table 7.. Plasmid construction. The plasmid C2-EGFP-L10a was provided by Nathaniel Heintz (The Rockefeller University, New York, NY, USA). The GFP-L10a coding sequence was amplified by PCR using the primers L10a-R-BsiWI and MfeI-EGFP-F and subcloned into the vector pKT2/Fah-mCa//SB (15) at the EcoRI and BsiWI restriction sites. The vector utilizes the Sleeping Beauty (SB) transposon system to enable integration of transgene sequences into the genome. The Slc7a11 cDNA was purchased (MG225346, OriGene) and amplified by PCR with the primers Slc7a11_clone_F1 and Slc7a11_psmd_bcd-R or Slc7a11-HA_bcd-R to include the HA tag. For the CRISPR/Cas9 studies, the vector pKT2/Fah-SpCas9//SB (34) was used to replace the SpCas9 with the SaCas9 sgRNA scaffold and introduce the subcloning site for further sgRNA subcloning using the oligonucleotides SaCas9Ins-F and -R and the restriction enzymes SapI and EcoRI to generate the vector pKT2/Fah-SaCas9//SB. Next, 10 ...
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PBGU : First-order test for evaluation of a suspected acute porphyria: acute intermittent porphyria, hereditary coproporphyria, and variegate porphyria
Acute Intermittent Porphyria. Abdominal pain is the most common complaint in acute intermittent porphyria. In addition, some of the following symptoms occur with varying frequency: pain in the arms and leg, generalized weakness, vomiting, confusion, constipation, tachycardia, fluctuating blood pressure, urinary retention, psychosis, hallucinations, and seizures. The muscle weakness may progress to respiratory paralysis, necessitating artificial respiration. Porphobilinogen is elevated during the attack but may be consistently high in some patients. Urine may exhibit a purple-red color. Unlike other forms of porphyria, sun sensitivity is not present in this type.. Variegate Porphyria. Variegate porphyria is characterized by abrasions, blisters, and erosions of the skin which are commonly seen during the second and third decade. These lesions tend to heal slowly, often leaving pigmented or slightly depressed scars. The patients experience sensitivity to light and fragility of skin exposed to the ...

Histidine ammonia-lyase - WikipediaHistidine ammonia-lyase - Wikipedia

Histidase converts histidine into ammonia and urocanic acid. Histidine ammonia-lyase is a cytosolic enzyme catalyzing the first ... Histidine ammonia-lyase (or histidase, or histidinase) is an enzyme that in humans is encoded by the HAL gene. ... Histidine Ammonia-Lyase at the US National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text ... Schwede, TF; Rétey, J; Schulz, GE (Apr 27, 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide ...
more infohttps://en.wikipedia.org/wiki/Histidine_ammonia-lyase

Threonine ammonia-lyase - WikipediaThreonine ammonia-lyase - Wikipedia

Threonine ammonia-lyase is a tetramer of identical subunits, and is arranged as a dimer of dimers. Each subunit has two domains ... Threonine ammonia-lyase is a member of the Fold Type II family, also known as the tryptophan synthase family. Though threonine ... Threonine ammonia-lyase is not found in humans. Thus, this is one example of why humans cannot synthesize all 20 proteinogenic ... In fact, threonine ammonia-lyase has been shown to exhibit some specificity towards serine and can convert serine into pyruvate ...
more infohttps://en.wikipedia.org/wiki/Threonine_ammonia-lyase

Aspartate ammonia-lyase (IPR004708) | InterPro | EMBL-EBIAspartate ammonia-lyase (IPR004708) | InterPro | EMBL-EBI

A number of enzymes, belonging to the lyase class, for which fumarate is a substrate have been shown [PMID: 3282546] to share a ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR004708

Ammonia-lyase | Define Ammonia-lyase at Dictionary.comAmmonia-lyase | Define Ammonia-lyase at Dictionary.com

Ammonia-lyase definition at Dictionary.com, a free online dictionary with pronunciation, synonyms and translation. Look it up ... ammonia-lyase in Medicine Expand. ammonia-lyase n. Any of various enzymes that remove ammonia or an amino compound by breaking ...
more infohttp://www.dictionary.com/browse/ammonia-lyase?qsrc=2446

Ammonia-lyases | definition of ammonia-lyases by Medical dictionaryAmmonia-lyases | definition of ammonia-lyases by Medical dictionary

... ammonia-lyases explanation free. What is ammonia-lyases? Meaning of ammonia-lyases medical term. What does ammonia-lyases mean? ... Looking for online definition of ammonia-lyases in the Medical Dictionary? ... Ammonia-lyases , definition of ammonia-lyases by Medical dictionary https://medical-dictionary.thefreedictionary.com/ammonia- ... ammonia-lyases. am·mo·ni·a-ly·as·es. (ă-mōnē-ă-līās-ēz), Enzymes that remove ammonia or an amino compound nonhydrolytically ( ...
more infohttp://medical-dictionary.thefreedictionary.com/ammonia-lyases

ethanolamine ammonia-lyase small subunit [Psychromonas ingrahamii 37] - Protein - NCBIethanolamine ammonia-lyase small subunit [Psychromonas ingrahamii 37] - Protein - NCBI

ethanolamine ammonia-lyase small subunit [Psychromonas ingrahamii 37]. * Record removed. The sequence YP_941742 is 100% ...
more infohttps://www.ncbi.nlm.nih.gov/protein/119944062

Occurrence of Phenylalanine Ammonia-Lyase (PAL) in isolated tapetum cells of Tulipa anthers | SpringerLinkOccurrence of Phenylalanine Ammonia-Lyase (PAL) in isolated tapetum cells of Tulipa anthers | SpringerLink

Occurrence of Phenylalanine Ammonia-Lyase (PAL) in isolated tapetum cells ofTulipa anthers. ... It was our purpose to investigate the localization of the key phenylpropanoid enzyme, phenylalanine ammonia-lyase, within the ...
more infohttps://link.springer.com/article/10.1007%2FBF01281805

Glucosaminate ammonia-lyase | Springer for Research & DevelopmentGlucosaminate ammonia-lyase | Springer for Research & Development

Schomburg D., Salzmann M. (1990) Glucosaminate ammonia-lyase. In: Schomburg D., Salzmann M. (eds) Enzyme Handbook 1. Springer, ...
more infohttps://rd.springer.com/chapter/10.1007/978-3-642-86605-0_229

Purification and Characterization of Phenylalanine Ammonia Lyase from Trichosporon cutaneum : Figure 4Purification and Characterization of Phenylalanine Ammonia Lyase from Trichosporon cutaneum : Figure 4

Figure 4: Temperature dependence studies on the PAL enzyme from the yeast Trichosporon cutaneum. A temperature optimum of 32°C was observed ...
more infohttps://www.hindawi.com/journals/er/2013/670702/fig4/

Phenylalanine Ammonia-Lyase and Phenolic Compounds in Chamomile Tolerance to Cadmium and Copper ExcessPhenylalanine Ammonia-Lyase and Phenolic Compounds in Chamomile Tolerance to Cadmium and Copper Excess

Home » Phenylalanine Ammonia-Lyase and Phenolic Compounds in Chamomile Tolerance to Cadmium and Copper Excess ... Phenylalanine ammonia-lyase activity (PAL, EC 4.3.1.5), total phenolics, soluble proteins, malondialdehyde and metals ... Phenylalanine Ammonia-Lyase and Phenolic Compounds in Chamomile Tolerance to Cadmium and Copper Excess. ... The effects of nitrogen deficiency on selected physiological attributes, phenylalanine ammonia-lyase (PAL, EC. 4.3.1.5) ...
more infohttp://connection.ebscohost.com/c/articles/26618618/phenylalanine-ammonia-lyase-phenolic-compounds-chamomile-tolerance-cadmium-copper-excess

Aspartate ammonia-lyase elisa and antibodyAspartate ammonia-lyase elisa and antibody

Recombinant Protein and Aspartate ammonia-lyase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Aspartate ammonia-lyase. Aspartate ammonia-lyase ELISA Kit. Aspartate ammonia-lyase Recombinant. Aspartate ammonia-lyase ... Also known as Aspartate ammonia-lyase (Aspartase).. aspA ELISA Kit. aspA Recombinant. aspA Antibody. Cgl1503 ELISA Kit. Cgl1503 ... Below are the list of possible Aspartate ammonia-lyase products. If you cannot find the target and/or product is not available ...
more infohttps://www.mybiosource.com/protein_family.php?root=aspartate-ammonia-lyase

Histidine ammonia-lyase elisa and antibodyHistidine ammonia-lyase elisa and antibody

Recombinant Protein and Histidine ammonia-lyase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Histidine ammonia-lyase 1. Histidine ammonia-lyase 1 ELISA Kit. Histidine ammonia-lyase 1 Recombinant. Histidine ammonia-lyase ... Histidine ammonia-lyase 2. Histidine ammonia-lyase 2 ELISA Kit. Histidine ammonia-lyase 2 Recombinant. Histidine ammonia-lyase ... Histidine ammonia-lyase. Histidine ammonia-lyase ELISA Kit. Histidine ammonia-lyase Recombinant. Histidine ammonia-lyase ...
more infohttps://www.mybiosource.com/protein_family.php?root=histidine-ammonia-lyase

Dihydroxyphenylalanine ammonia-lyase | definition of dihydroxyphenylalanine ammonia-lyase by Medical dictionaryDihydroxyphenylalanine ammonia-lyase | definition of dihydroxyphenylalanine ammonia-lyase by Medical dictionary

What is dihydroxyphenylalanine ammonia-lyase? Meaning of dihydroxyphenylalanine ammonia-lyase medical term. What does ... Looking for online definition of dihydroxyphenylalanine ammonia-lyase in the Medical Dictionary? dihydroxyphenylalanine ammonia ... dihydroxyphenylalanine ammonia-lyase. dihydroxyphenylalanine ammonia-lyase. This enzyme name was retired in 2007, as ... Dihydroxyphenylalanine ammonia-lyase , definition of dihydroxyphenylalanine ammonia-lyase by Medical dictionary https://medical ...
more infohttp://medical-dictionary.thefreedictionary.com/dihydroxyphenylalanine+ammonia-lyase

Biochemical studies of phenylalanine ammonia-lyase encapsulated in erythrocytes | Biochemical Society TransactionsBiochemical studies of phenylalanine ammonia-lyase encapsulated in erythrocytes | Biochemical Society Transactions

Biochemical studies of phenylalanine ammonia-lyase encapsulated in erythrocytes. ULRICH SPRANDEL, NEPOMUK ZÖLLNER ... Biochemical studies of phenylalanine ammonia-lyase encapsulated in erythrocytes Message Subject (Your Name) has forwarded a ...
more infohttp://www.biochemsoctrans.org/content/18/4/654

Crystal Structures of Ethanolamine Ammonia-lyase Complexed with Coenzyme B12 Analogs and SubstratesCrystal Structures of Ethanolamine Ammonia-lyase Complexed with Coenzyme B12 Analogs and Substrates

... *. Naoki Shibata,‡§,1 Hiroko ... Ethanolamine ammonia-lyase (EAL) (EC 4.3.1.7) or ethanolamine deaminase catalyzes the AdoCbl-dependent conversion of ... N-terminal truncation of the Escherichia coli ethanolamine ammonia-lyase β-subunit does not affect the catalytic properties of ... ethanolamine ammonia-lyase. PA. 2-amino-1-propanol. SAD. single-wavelength anomalous dispersion.. ...
more infohttp://pubmedcentralcanada.ca/pmcc/articles/PMC2924083/

Phenylpropanoids, Phenylalanine Ammonia Lyase and Peroxidases in Elicitor-challenged Cassava (Manihot esculenta) Suspension...Phenylpropanoids, Phenylalanine Ammonia Lyase and Peroxidases in Elicitor-challenged Cassava (Manihot esculenta) Suspension...

Methods: Phenylalanine ammonialyase (PAL), phenylpropanoids and peroxidases (POD) were investigated in elicited cassava ... Phenylpropanoids, Phenylalanine Ammonia Lyase and Peroxidases in Elicitor-challenged Cassava (Manihot esculenta) Suspension ... Phenylpropanoids, Phenylalanine Ammonia Lyase and Peroxidases in Elicitor-challenged Cassava (Manihot esculenta) Suspension ... Phenylalanine Ammonia Lyase and Peroxidases in Elicitor-challenged Cassava (Manihot esculenta) Suspension Cells and Leaves. ...
more infohttps://www.gov.uk/dfid-research-outputs/phenylpropanoids-phenylalanine-ammonia-lyase-and-peroxidases-in-elicitor-challenged-cassava-manihot-esculenta-suspension-cells-and-leaves

Molecules | Free Full-Text | Involvement of Carbohydrate, Protein and Phenylanine Ammonia Lyase in Up-Regulation of Secondary...Molecules | Free Full-Text | Involvement of Carbohydrate, Protein and Phenylanine Ammonia Lyase in Up-Regulation of Secondary...

... protein synthesis and L-phenylalanine ammonia lyase (PAL; EC 4.3.1.5) activity in the Malaysian medicinal herb Labisia pumila ( ... Ibrahim, M.H.; Jaafar, H.Z. Involvement of Carbohydrate, Protein and Phenylanine Ammonia Lyase in Up-Regulation of Secondary ... Involvement of Carbohydrate, Protein and Phenylanine Ammonia Lyase in Up-Regulation of Secondary Metabolites in Labisia pumila ... Involvement of Carbohydrate, Protein and Phenylanine Ammonia Lyase in Up-Regulation of Secondary Metabolites in Labisia pumila ...
more infohttp://www.mdpi.com/1420-3049/16/5/4172

Identification and Use of cDNAS of Phenylalanine Ammonia-Lyase and 4-Coumarate:CoA LIGASE mRNAS in Studies of the Induction of...Identification and Use of cDNAS of Phenylalanine Ammonia-Lyase and 4-Coumarate:CoA LIGASE mRNAS in Studies of the Induction of...

Identification and Use of cDNAS of Phenylalanine Ammonia-Lyase and 4-Coumarate:CoA LIGASE mRNAS in Studies of the Induction of ... Kuhn D.N., Chappell J., Hahlbrock K. (1983) Identification and Use of cDNAS of Phenylalanine Ammonia-Lyase and 4-Coumarate:CoA ...
more infohttps://link.springer.com/chapter/10.1007/978-1-4684-4538-1_32

Highly Active and Specific Tyrosine Ammonia-Lyases from Diverse Origins Enable Enhanced Production of Aromatic Compounds in...Highly Active and Specific Tyrosine Ammonia-Lyases from Diverse Origins Enable Enhanced Production of Aromatic Compounds in...

... tyrosine ammonia-lyases (TAL; EC 4.3.1.23), phenylalanine ammonia-lyases (PAL; EC 4.3.1.24), or phenylalanine/tyrosine ammonia- ... Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol 113:175-179. doi:10.1104/pp.113.1.175. ... Some enzymes had both phenylalanine ammonia-lyase activity (PAL) and tyrosine ammonia-lyase activity (TAL), while others showed ... we aimed at increasing the range of characterized phenylalanine ammonia-lyases (PAL) and tyrosine ammonia-lyases (TAL), and in ...
more infohttps://aem.asm.org/content/81/13/4458

Synechocystis PCC 6803 cells heterologously expressing bacterial tyrosine ammonia lyase can use exogenous tyrosine for p...Synechocystis PCC 6803 cells heterologously expressing bacterial tyrosine ammonia lyase can use exogenous tyrosine for p...

Synechocystis PCC 6803 cells heterologously expressing bacterial tyrosine ammonia lyase can use exogenous tyrosine for p- ... We demonstrate that the Synechocystis PCC 6803 expressing tyrosine ammonia-lyase from Rhodobacter sphaeroides under Ptrc1O ...
more infohttp://uu.diva-portal.org/smash/record.jsf?pid=diva2:1185555

Suppression of phenylalanine ammonia lyase expression in sugar beet by the fungal pathogen Cercospora beticola is mediated at...Suppression of phenylalanine ammonia lyase expression in sugar beet by the fungal pathogen Cercospora beticola is mediated at...

"Suppression of phenylalanine ammonia lyase expression in sugar beet by the fungal pathogen Cercospora beticola is mediated at ... Suppression of phenylalanine ammonia lyase expression in sugar beet by the fungal pathogen... Schmidt, Klaus; Heberle, Brigitte ... Suppression of phenylalanine ammonia lyase expression in sugar beet by the fungal pathogen Cercospora beticola is mediated at ... Suppression of phenylalanine ammonia lyase expression in sugar beet by the fungal pathogen Cercospora beticola is mediated at ...
more infohttps://www.deepdyve.com/lp/springer_journal/suppression-of-phenylalanine-ammonia-lyase-expression-in-sugar-beet-by-Ip93XpclVb

Colocalization of l-Phenylalanine Ammonia-Lyase and Cinnamate 4-Hydroxylase for Metabolic Channeling in Phenylpropanoid...Colocalization of l-Phenylalanine Ammonia-Lyase and Cinnamate 4-Hydroxylase for Metabolic Channeling in Phenylpropanoid...

Bolwell, G.P., Sap, J., Cramer, C.L., Schuch, W., Lamb, C.J., and Dixon, R.A. (1985). L-Phenylalanine ammonia-lyase from ... Wanner, L.A., Li, G., Ware, D., Somssich, I.E., and Davis, K.R. (1995). The phenylalanine ammonia-lyase gene family in ... To determine whether isoforms of l-Phe ammonia-lyase (PAL), the first enzyme in the pathway, can associate with the next enzyme ... Allwood, E.G., Davies, D.R., Gerrish, C., Ellis, B.E., and Bolwell, G.P. (1999). Phosphorylation of phenylalanine ammonia-lyase ...
more infohttp://www.plantcell.org/content/16/11/3098?ijkey=d87b021e9874115aa9b013e41b86960c21f1aa01&keytype2=tf_ipsecsha

Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in...Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in...

Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in ... Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in ... Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in ... Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in ...
more infohttp://www.plantphysiol.org/content/108/1/39

Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity | Research Explorer |...Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity | Research Explorer |...

Phenylalanine ammonia lyases (PALs) catalyse the regio- and stereoselective hydroamination of cinnamic acid analogues to yield ... HomeResearchResearch ExplorerPublicationsBacterial Anabaena variabilis phenylalanine ammonia lyase: A... ... Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity. Research output: ...
more infohttps://www.research.manchester.ac.uk/portal/en/publications/bacterial-anabaena-variabilis-phenylalanine-ammonia-lyase-a-biocatalyst-with-broad-substrate-specificity

phenylalanine ammonia lyasephenylalanine ammonia lyase

Tag Archives: phenylalanine ammonia lyase. Polyphenols Flavonoid biosynthesis pathway. 26 October 2015. Dr. Nicola Tazzini ... Phenylalanine ammonia lyase (PAL). It is one of the most studied and best characterized enzymes of plant secondary metabolism. ... And, as phenylalanine ammonia lyase and chalcone synthase, it is induced by elicitors.. In the reaction catalysed by flavanone- ... 3 - Phenylalanine Ammonia Lyase. Therefore, it directs the flow of carbon from the shikimic acid pathway to the different ...
more infohttp://www.tuscany-diet.net/tag/phenylalanine-ammonia-lyase/
  • Van Havere2017, author={Van Havere, Robin}, title={Engineering of 3 methylaspartate ammonia-lyases for biobased adipic acid production}, abstract={The current traditional adipic acid production is a highly polluting process. (chalmers.se)
  • Phenylalanine ammonia-lyase activity (PAL, EC 4.3.1.5), total phenolics, soluble proteins, malondialdehyde and metals accumulation in four-week old chamomile ( Matricaria chamomilla) plants cultivated in nutrient solution and exposed to low (3 μM) and high (60 and 120 μM) levels of cadmium (Cd) or copper (Cu) for 7 days were studied. (ebscohost.com)
  • As a consequence, a complex pattern of phenylalanine ammonia lyase time course specific activity levels was evident. (semanticscholar.org)