Ammonia
Lyases
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
Chondroitinases and Chondroitin Lyases
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.
Chicory
Aldehyde-Lyases
Nitrosomonas
Carbon-Oxygen Lyases
Erwinia
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)
Oxo-Acid-Lyases
Nitrogen
Polygalacturonase
Hyperammonemia
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
Glutamate-Ammonia Ligase
Alginates
Glutamine
Hydrogen-Ion Concentration
Substrate Specificity
Ammonium Chloride
Nitrogen Radioisotopes
Hexuronic Acids
Isocitrate Lyase
Nitrification
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
Chondroitin ABC Lyase
Sphingomonas
Amino Acid Sequence
Cytochromes c1
Bacteroides
Glucuronic Acid
Flavobacterium
Adenylosuccinate Lyase
Streptococcus anginosus
Cloning, Molecular
Hevea
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
Manure
Nitrosomonas europaea
Carbon-Nitrogen Lyases
Glutamate Dehydrogenase
Carbon-Carbon Lyases
Glycosaminoglycans
Proteus vulgaris
Uronic Acids
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
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.
Amino Acids
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
Phenylalanine Ammonia-Lyase
Gills
Dermatan Sulfate
Crystallography, X-Ray
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
Glutamate Synthase
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
Glutamates
Bacillus
Archaea
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
N-Glycosyl Hydrolases
Urease
Fatty Acids, Volatile
Catalysis
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
Electrophoresis, Polyacrylamide Gel
Acidosis
Biocatalysis
Nitrogen Isotopes
Catalytic Domain
Models, Molecular
Chromatography, Gel
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.
Temperature
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
Air
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
Bacteria
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
Isoenzymes
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
Ketoglutaric Acids
Gene Expression Regulation, Bacterial
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)
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Histidine ammonia-lyase
Its systematic name is L-histidine ammonia-lyase (urocanate-forming). Histidine ammonia-lyase is a cytosolic enzyme catalyzing ... Histidine ammonia-lyase (EC 4.3.1.3, histidase, histidinase) is an enzyme that in humans is encoded by the HAL gene. It ... "Entrez Gene: histidine ammonia-lyase". Suchi M, Sano H, Mizuno H, Wada Y (September 1995). "Molecular cloning and structural ... Histidine+Ammonia-Lyase at the US National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text ...
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Tyrosine ammonia lyase (EC 4.3.1.23, L-tyrosine ammonia-lyase, TAL or Tyrase) is an enzyme in the natural phenols biosynthesis ... phenylalanine ammonia-lyase) EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase) Louie GV, Bowman ME, Moffitt MC, Baiga TJ, ... "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". ... Tyrosine+ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH) www.hhmi.org Portal: Biology v t ...
Dihydroxyphenylalanine ammonia-lyase
... ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ammonia-lyase. This enzyme participates in tyrosine metabolism. Magee WL, ... 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, entry deleted) is a non-existing enzyme that catalyzes the ... 4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming). Other names in common use include beta-(3,4-dihydroxyphenyl ...
Ethanolamine ammonia-lyase
NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction ethanolamine ⇌ {\displaystyle \ ... systematic name of this enzyme class is ethanolamine ammonia-lyase (acetaldehyde-forming). It is also called ethanolamine ...
Methylaspartate ammonia-lyase
NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction L-threo-3-methylaspartate ⇌ {\ ... 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). ... The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic ... The enzyme is a member of the ammonia lyase family, which cleaves carbon-nitrogen bonds. Like other lyases, PAL requires only ...
Threonine ammonia-lyase
... (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly ... 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 ...
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 ... The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction 2-amino-2-deoxy-D-gluconate = 2-dehydro-3- ... name of this enzyme class is 2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming). ...
Aspartate ammonia-lyase
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction L-aspartate ⇌ {\displaystyle \rightleftharpoons ... and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. As of late ... Portal: Biology v t e (CS1 maint: uses authors parameter, EC 4.3.1, Enzymes of known structure, All stub articles, Lyase stubs) ...
Diaminopropionate ammonia-lyase
... β-diaminopropionate ammonia-lyase, 2,3-diaminopropionate ammonia-lyase, and 2,3-diaminopropanoate ammonia-lyase. It employs one ... 2 NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... The enzyme diaminopropionate ammonia-lyase (EC 4.3.1.15) catalyzes the chemical reaction 2,3-diaminopropanoate + H2O ⇌ {\ ... Nagasawa T, Tanizawa K, Satoda T, Yamada H (1988). "Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification ...
Threo-3-hydroxy-D-aspartate ammonia-lyase
... (EC 4.3.1.27, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic ... Threo-3-hydroxy-D-aspartate+ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... name threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming). This enzyme catalyses the following chemical reaction ...
D-serine ammonia-lyase
The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the ... Portal: Biology v t e (EC 4.3.1, Pyridoxal phosphate enzymes, Enzymes of unknown structure, All stub articles, Lyase stubs). ... and D-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism. It employs one ...
Serine-sulfate ammonia-lyase
The systematic name of this enzyme class is L-serine-O-sulfate ammonia-lyase (pyruvate-forming). It is also called (L-SOS)lyase ... sulfate This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. ... The enzyme Serine-sulfate ammonia-lyase (EC 4.3.1.10) catalyzes the chemical reaction L-serine O-sulfate + H2O ⇌ {\displaystyle ...
L-serine ammonia-lyase
... specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine ammonia- ... The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction L-serine = pyruvate + NH3 (overall reaction) ( ... lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine ... This enzyme belongs to the family of lyases, ... deaminase, L-serine dehydratase, and L-serine hydro-lyase ( ...
Carbamoyl-serine ammonia-lyase
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction O-carbamoyl-L-serine + H2O = pyruvate ... 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 ...
Threo-3-hydroxyaspartate ammonia-lyase
NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... The enzyme 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. Wada M, Matsumoto T, Nakamori S, Sakamoto M, Kataoka M, Liu JQ, Itoh N, Yamada H ... systematic name of this enzyme class is threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common ...
3-aminobutyryl-CoA ammonia-lyase
NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... The enzyme 3-aminobutyryl-CoA ammonia-lyase (EC 4.3.1.14) catalyzes the chemical reaction L-3-aminobutyryl-CoA ⇌ {\displaystyle ... and L-3-aminobutyryl-CoA ammonia-lyase. Jeng I, Barker HA (October 1974). "Purification and properties of l-3-aminobutyryl ... systematic name of this enzyme class is L-3-aminobutyryl-CoA ammonia-lyase (crotonoyl-CoA-forming). Other names in common use ...
Beta-alanyl-CoA ammonia-lyase
NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... The enzyme β-Alanyl-CoA ammonia-lyase (EC 4.3.1.6) catalyzes the chemical reaction β-alanyl-CoA ⇌ {\displaystyle \ ... This enzyme is also called β-alanyl coenzyme A ammonia-lyase. This enzyme participates in β-alanine metabolism and propanoate ... Portal: Biology v t e (EC 4.3.1, Enzymes of unknown structure, All stub articles, Lyase stubs). ...
Erythro-3-hydroxyaspartate ammonia-lyase
NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The ... erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating); erythro-3-hydroxy-Ls-aspartate ammonia-lyase. It employs one cofactor ... The enzyme erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) catalyzes the chemical reaction erythro-3-hydroxy-L-aspartate ... systematic name of this enzyme class is erythro-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in ...
Argininosuccinate lyase
"ASL gene argininosuccinate lyase". NIH. U.S. Department of Health & Human Services. 2007. Jack, JJB (1982). "Actions of ammonia ... Ammonia is toxic in part because it affects the nervous system. There is biochemical evidence that shows rises in ammonia can ... ASL is a key enzyme in the conversion of ammonia to urea through the urea cycle. Ammonia builds to toxic levels, resulting in ... Ammonia (NH3) is a toxic substance for many aerobic organisms and must be excreted. Some aquatic organisms release the toxin ...
Eric Conn
Conn researched phenylalanine ammonia-lyase and cyanogenic glycosides. Notable students include the plant biochemist and ...
Pisatin
Wanner, L.A.; Ware, D.; Somssich, I.E.; Davis, K.R. (1995). "The phenylalanine ammonia-lyase gene family in Arabidopsis ...
Methionine gamma-lyase
Lastly, α-keto acid and ammonia are released from PLP. Because MGL has differing substrate specificity among organisms, the ... methionine lyase, methioninase, methionine dethiomethylase, L-methionine γ-lyase, and L-methionine methanethiol-lyase ( ... This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme ... The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing ...
Phenylpropanoid
Phenylalanine is first converted to cinnamic acid by the action of the enzyme phenylalanine ammonia-lyase (PAL). Some plants, ... "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nat. Plants. 2 (6): 16050. doi:10.1038/nplants.2016.50. ... use tyrosine to synthesize p-coumaric acid by the action of the bifunctional enzyme Phenylalanine/tyrosine ammonia-lyase (PTAL ...
PEGylation
Levy, Harvey L.; Sarkissian, Christineh N.; Stevens, Raymond C.; Scriver, Charles R. (June 2018). "Phenylalanine ammonia lyase ... Pegvaliase (Biomarin) - PEGylated recombinant phenylalanine ammonia-lyase for the treatment of Phenylketonuria, approved by the ...
Dehydroalanine
... was long thought to be an important electrophilic catalytic residue in histidine ammonia-lyase and phenylalanine ammonia-lyase ... "Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis". Biochemistry. 43 (36): 11403 ...
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 ...
Hesperidin
Wanner LA, Li G, Ware D, Somssich IE, Davis KR (January 1995). "The phenylalanine ammonia-lyase gene family in Arabidopsis ... in which the natural amino acid L-phenylalanine undergoes a deamination by phenylalanine ammonia lyase to afford (E)-cinnamate ... "Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in ...
Cinnamaldehyde
Kong, Jian-Qiang (2015-07-20). "Phenylalanine ammonia-lyase, a key component used for phenylpropanoids production by metabolic ... of cinnamaldehyde begins with deamination of L-phenylalanine into cinnamic acid by the action of phenylalanine ammonia lyase ( ...
Botrytis cinerea
They find it increases phenylalanine ammonia-lyase activity and production of phenolics. This in turn decreases L. sativa's ...
Ornithine cyclodeaminase
... specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is Lornithine ammonia ... and L-ornithine ammonia-lyase (cyclizing). This enzyme participates in arginine and proline biosynthesis. It employs one ... lyase (cyclizing; L-proline-forming). Other names in common use include ornithine cyclase, ornithine cyclase (deaminating), ... NH4+ This enzyme belongs to the family of lyases, ...
Nitrilase
The acylenzyme is hydrolyzed by ammonia, displacing the enzyme and forming the amide product. Most nitrilases are made up of a ... Nitrilase should not be confused with nitrile hydratase (nitrile hydro-lyase; EC 4.2.1.84) which hydrolyses nitriles to amides ... The thioimidate formed is subsequently hydrolyzed to the acylenzyme and ammonia is created as a byproduct. The acylenzyme can ... Nitrilase enzymes (nitrile aminohydrolase; EC 3.5.5.1) catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, ...
L-threo-3-Methylaspartate
Methylaspartate is an unusual amino acid formed by glutamate mutase and can be metabolised by methylaspartate ammonia-lyase. It ...
Angelicin
The phenylalanine undergoes a non-oxidative deamination by phenylalanine ammonia-lyase (PAL) to trans-cinnamic acid. Afterwards ...
Raymond C. Stevens
Phenylalanine ammonia lyase for phenylketonuria, Mol Genet Metab 99: 4-9. "UPDATE: FDA-Approved Oral Zeposia® (Ozanimod) for ... pegylated Phenylalanine ammonia-lyase) as treatments for mild and classical phenylketonuria (PKU). In 2008, Stevens started ... Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase J Mol Biol 380: ...
Hans Krebs (biochemist)
He found that citrulline acted as a catalyst in the metabolic reactions of urea from ammonia and carbon dioxide. He and ... One was malate synthase, which condenses acetate with glyoxylate to form malate, and the other was isocitrate lyase, which ...
Glyoxylic acid
This species reacts with ammonia to give hydroxyphenylglycine, a precursor to the drug amoxicillin. Reduction of the 4- ... The glyoxylate cycle is initiated through the activity of isocitrate lyase, which converts isocitrate into glyoxylate and ...
Cyanase
Cyanate is a toxic anion, and cyanase catalyzes the metabolism into the benign products of carbon dioxide and ammonia. Cyanase ... The enzyme cyanase (EC 4.2.1.104, also known as cyanate hydratase or cyanate lyase), catalyses the bicarbonate dependent ... a partial sequence of cyanate lyase from rice". Peptides. 42: 55-62. doi:10.1016/j.peptides.2012.12.015. PMID 23270672. S2CID ... which then spontaneously decomposes to carbon dioxide and ammonia: cyanate (OCN−) + HCO3− + H+ ⇌ {\displaystyle \ ...
Flavan-3-ol
... phenylalanine ammonia lyase (PAL), E2, tyrosine ammonia lyase (TAL), E3, cinnamate 4-hydroxylase, E4, 4-coumaroyl: CoA-ligase, ...
Marine protists
J, Stefels; L, Dijkhuizen; WWC, Gieskes (20 July 1995). "DMSP-lyase activity in a spring phytoplankton bloom off the Dutch ... Foraminiferans section showing chambers of a spiral foram Live Ammonia tepida streaming granular ectoplasm for catching food ...
Transsulfuration pathway
... which is attacked by water to form pyruvate and ammonia (catalysed by the metC-encoded cystathionine β-lyase). The production ... In Klebsiella pneumoniae the cystathionine β-synthase is encoded by mtcB, while the γ-lyase is encoded by mtcC. Humans are ... Methionine gamma-lyase (mdeA) which breaks down methionine at the thioether and amine bounds Note: MetC, metB, metZ are closely ... Cystathionine γ-lyase (no common gene name) which joins an activated serine ester (acetyl or succinyl) with homocysteine to ...
Methylmalonyl-CoA mutase deficiency
Ammonia test, blood count, CT scan, MRI scan, electrolyte levels, genetic testing, methylmalonic acid blood test, and blood ... which is hydrolyzed by cystathione gamma lyase to create 2-oxobutanoate. This substrate is transformed to propionyl-CoA and ... such as ammonia-dependent-carbamoyl-phosphate synthase or CPS1), and inhibits its mechanism of action. The combination of ... which is hydrolyzed by cystathione gamma lyase to create 2-oxobutanoate. This substrate is transformed to propanoyl-CoA and ...
EAL
... a conserved protein domain Ethanolamine ammonia-lyase Echelle Atomique Libre (Free Atomic Scale), a time scale underlying ...
PAL (disambiguation)
... a security device for nuclear weapons Phenylalanine ammonia-lyase, a class of enzymes Physical activity level, a way of ...
Aminodeoxychorismate synthase
Purification of aminodeoxychorismate lyase and cloning of pabC". J. Biol. Chem. 266 (20): 12971-5. doi:10.1016/S0021-9258(18) ... The first step occurs with PabA abstracting ammonia from glutamine. The second step occurs when PabB reacts both substrates ( ... can be converted to para-aminobenzoic acid by the enzyme 4-amino-4-deoxychorismate lyase (PabC). This enzyme belongs to the ... chorismate and ammonia) to synthesize 4-amino-4-deoxychorismate. In plants such as Arabidopsis thaliana, aminodeoxychorismate ...
List of EC numbers (EC 6)
... lyase] ligase EC 6.2.1.23: dicarboxylate-CoA ligase EC 6.2.1.24: phytanate-CoA ligase EC 6.2.1.25: benzoate-CoA ligase EC 6.2. ... aspartate-ammonia ligase (ADP-forming) EC 6.3.1.5: NAD+ synthase EC 6.3.1.6: glutamate-ethylamine ligase EC 6.3.1.7: 4- ... aspartate-ammonia ligase EC 6.3.1.2: glutamine synthetase EC 6.3.1.3: Now EC 6.3.4.13, phosphoribosylamine-glycine ligase EC ... diphthine-ammonia ligase EC 6.3.1.15: 8-demethylnovobiocic acid synthase * EC 6.3.1.16: The enzyme was discovered at the public ...
Rosavin
Phenylalanine ammonia lyase (PAL) then converts phenolpyruvate to phenylalanine by using L-glutamate as an amine donor, which ...
Phenylpropanoids metabolism
Phenylalanine ammonia-lyase (PAL, a.k.a. phenylalanine/tyrosine ammonia-lyase) is an enzyme that transforms L-phenylalanine and ...
Phenylalanine
... is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. Phenylalanine is biosynthesized via the ... In 1882, Erlenmeyer and Lipp first synthesized phenylalanine from phenylacetaldehyde, hydrogen cyanide, and ammonia. The ...
Argininosuccinic aciduria
The urea cycle cannot proceed normally, and nitrogen accumulates in the bloodstream in the form of ammonia. Ammonia is ... the enzyme argininosuccinate lyase, involved in the conversion of arginino succinate to arginine within the urea cycle, is ... Plasma concentrations of ammonia (>150 μmol/L) and citrulline (200-300 μmol/L) are elevated. Elevated levels of ... Argininosuccinic aciduria may become evident in the first few days of life because of high blood ammonia, or later in life ...
TAL
... an organic compound Tyrosine ammonia lyase, an enzyme Technology Alert List, a list created by the United States government of ...
Arginine
... plays an important role in cell division, wound healing, removing ammonia from the body, immune function, and the ... in the urea cycle by the sequential action of the cytosolic enzymes argininosuccinate synthetase and argininosuccinate lyase. ... the resulting ammonia toxicity can be lethal. This is not a problem in practice, because meat contains sufficient arginine to ... their highly efficient protein catabolism produces large quantities of ammonia which need to be processed through the urea ...
7-carboxy-7-deazaguanine synthase
8-tetrahydropterin ammonia-lyase. This enzyme catalyses the following chemical reaction 6-carboxy-5,6,7,8-tetrahydropterin ⇌ {\ ...
Pegvaliase
Chemically, it is a pegylated derivative of the enzyme phenylalanine ammonia-lyase that metabolizes phenylalanine to reduce its ...
Development of a Protease Stable Phenylalanine Ammonia Lyase :: Codexis, Inc. (CDXS)
4.3.1.14: 3-Aminobutyryl-CoA ammonia-lyase - BRENDA Enzyme Database
Structure-based epitope and PEGylation sites mapping of phenylalanine ammonia-lyase for enzyme substitution treatment of...
Red anthocyanins contents and the relationships with phenylalanine ammonia lyase (PAL) activity, soluble sugar and chlorophyll...
Red anthocyanins contents and the relationships with phenylalanine ammonia lyase (PAL) activity, soluble sugar and chlorophyll ... Cheng Guiwen W., Breen Patrick J. (1991): Activity of Phenylalanine Ammonia-Lyase (PAL) and Concentrations of Anthocyanins and ... Cheng Guiwen W., Breen Patrick J. (1991): Activity of Phenylalanine Ammonia-Lyase (PAL) and Concentrations of Anthocyanins and ... The accumulation, distribution and content of anthocyanins in root are related to phenylalanine ammonia lyase (PAL) activity, ...
Ornithine cyclase (deaminating). Purification of a protein that converts ornithine to proline and definition of the optimal...
Human HAL(Histidine Ammonia Lyase) ELISA Kit - ELISA Kits
Human HAL(Histidine Ammonia Lyase) ELISA Kit. Human HAL(Histidine Ammonia Lyase) ELISA Kit. Contact us: [email protected] ... Histidine ammonia-lyase defects cause histidinemia which is characterized by increased histidine and histamine and decreased ... Description: Histidine ammonia-lyase is a cytosolic enzyme catalyzing the first reaction in histidine catabolism, the ... Histidine ammonia-lyase defects cause histidinemia which is characterized by increased histidine and histamine and decreased ...
Effect of thyme oil vapours exposure on phenylalanine ammonia-lyase (PAL) and lipoxygenase (LOX) genes expression, and control...
... vapours on the expression of phenylalanine ammonia-lyase (PAL) and lipoxygenase (LOX) genes, and control of anthracnose was ... Abstract : The effect of thyme oil (96 μL L−1) vapours on the expression of phenylalanine ammonia-lyase (PAL) and lipoxygenase ... Effect of thyme oil vapours exposure on phenylalanine ammonia-lyase (PAL) and lipoxygenase (LOX) genes expression, and control ... Effect of thyme oil vapours exposure on phenylalanine ammonia-lyase (PAL) and lipoxygenase (LOX) genes expression, and control ...
HAL gene: MedlinePlus Genetics
IMSEAR at SEARO: Identification Of Phenyl Alanine Ammonia Lyase Gene Involved In The Synthesis Of Anacardic Acid In Anacardium...
Sija S. L.. Identification Of Phenyl Alanine Ammonia Lyase Gene Involved In The Synthesis Of Anacardic Acid In Anacardium ... Identification Of Phenyl Alanine Ammonia Lyase Gene Involved In The Synthesis Of Anacardic Acid In Anacardium Occidentale L. ... Phenylalanine ammonia-lyase (PAL) shows a dominant role in the biosynthesis of poly phenolic compounds, which are involved in ... method and the presence of phenyl alanine ammonia lyase gene also plays a role in the biosynthesis of anacardic acid in young ...
JoF | Free Full-Text | Monitoring of Host Suitability and Defense-Related Genes in Wheat to Bipolaris sorokiniana
In the present study, expression levels of PR proteins, phenylalanine ammonia-lyase, catalase, ascorbate peroxidase, and ... In the present study, expression levels of PR proteins, phenylalanine ammonia-lyase, catalase, ascorbate peroxidase, and ... the role of phenylalanine ammonia-lyase (PAL) involving in the production of defense-related compounds and guaiacol peroxidase ... Effects of Phenylalanine Ammonia Lyase (PAL) knockdown on cell wall composition, biomass digestibility, and biotic and abiotic ...
Hein WIJMA | Research Associate | Dr. | University of Groningen, Groningen | RUG | Department of Biochemistry
Bacterial microcompartments | Nature Reviews Microbiology
Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates. J. Biol. Chem. 285, 26484- ... Purification and some properties of wild-type and N-terminal-truncated ethanolamine ammonia-lyase of Escherichia coli. J. ... Sagermann, M., Ohtaki, A. & Nikolakakis, K. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase ... Structure and function of CutC choline lyase from human microbiota bacterium Klebsiella pneumoniae. J. Biol. Chem. 290, 21732- ...
MMRRC:040290-MU
Copper ions suppress abscisic acid biosynthesis to enhance defence against Phytophthora infestans in potato (Journal Article) |...
SCOPe 2.01: Domain d1eb4a : 1eb4 A
Using RNA-Seq for gene identification, polymorphism detection and transcript profiling in two alfalfa genotypes with divergent...
Sol Genomics Network
Sequence search - BRENDA Enzyme Database
Argininosuccinate Lyase (ASL) Deficiency Differential Diagnoses
... lyase deficiency results in defective cleavage of ASA. This leads to an accumulation of ASA in cells and an excessive excretion ... Ammonia Control in Children Ages 2 Months through 5 Years with Urea Cycle Disorders: Comparison of Sodium Phenylbutyrate and ... encoded search term (Argininosuccinate Lyase (ASL) Deficiency) and Argininosuccinate Lyase (ASL) Deficiency What to Read Next ... Argininosuccinate Lyase (ASL) Deficiency Differential Diagnoses. Updated: Jan 07, 2019 * Author: Karl S Roth, MD; Chief Editor ...
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Temporal accumulation patterns of defence response gene transcripts in relation to resistant reactions in oat inoculated with...
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Phenylalanine15
- reported in 1980 that an encapsulated orally-administered Phenylalanine Ammonia Lyase (PAL) reduced blood Phe levels by 25% in a single patient, presumably by degrading Phe digested protein in the small intestine. (codexis.com)
- Red anthocyanins contents and the relationships with phenylalanine ammonia lyase (PAL) activity, soluble sugar and chlorophyll contents in carmine radish (Raphanus sativus L. (agriculturejournals.cz)
- Zhang Z., Sun C., Yao Y., Mao Z., Sun G., Dai Z. (2019): Red anthocyanins contents and the relationships with phenylalanine ammonia lyase (PAL) activity, soluble sugar and chlorophyll contents in carmine radish ( Raphanus sativus L.) . Hort. (agriculturejournals.cz)
- The accumulation, distribution and content of anthocyanins in root are related to phenylalanine ammonia lyase (PAL) activity, soluble sugar and chlorophyll contents. (agriculturejournals.cz)
- Cheng Guiwen W., Breen Patrick J. (1991): Activity of Phenylalanine Ammonia-Lyase (PAL) and Concentrations of Anthocyanins and Phenolics in Developing Strawberry Fruit. (agriculturejournals.cz)
- Description: A sandwich ELISA for quantitative measurement of Human L Phenylalanine ammonia lyase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (myelisakit.com)
- The effect of thyme oil (96 μL L−1) vapours on the expression of phenylalanine ammonia-lyase (PAL) and lipoxygenase (LOX) genes, and control of anthracnose was investigated in naturally infected 'Hass' and 'Ryan' avocado fruit stored for 21 d at 7-7.5 °C, and thereafter kept for 5 d at 20 °C, simulating the supply chain conditions. (univ-reunion.fr)
- Anacardic acids, a class of medicinally and industrially important phenolic compounds is found in a variety of dicotyledonous families chiefly in Cashew (Anacardium occidentale L). Phenylalanine ammonia-lyase (PAL) shows a dominant role in the biosynthesis of poly phenolic compounds, which are involved in the defense mechanism in harsh environments related to various stimuli. (who.int)
- These included phenylalanine ammonia lyase, chalcone synthase, sesquiterpene cyclase, and HMG1 (3-hydroxy-3-methylglutaryl CoA reductase). (bioone.org)
- The activity of the enzymes phenylalanine ammonia lyase and peroxidase were also found to be higher in striped root tissues. (scirp.org)
- Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar. (rothamsted.ac.uk)
- Phosphoinositide-specific phospholipase C signaling mediates expression of two phenylalanine ammonia lyase genes induced by salicylic acid in Capsicum chinense cells.Journal of Plant Biochemistry and Biotechnology. (cicy.mx)
- During his Ph.D. thesis research on coumarin metabolism in Melilotus alba with Professor Eric Conn, he obtained the first experimental evidence for the existence of phenylalanine ammonia lyase-the key regulatory enzyme controlling the flow of carbon into phenylpropanoid metabolism. (apsnet.org)
- Anabaena variabilis double mutant (C503S/C565S) phenylalanine ammonia-lyase (PAL) is an appealing enzyme in the enzyme-replacement therapy of phenylketonuria. (mysciencework.com)
- Phenylalanine ammonia lyase (PAL): From discovery to enzyme substitution therapy for phenylketonuria. (cdc.gov)
Histidine Ammon4
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Histidine Ammonia Lyase (HAL) in Tissue homogenates, cell lysates and other biological fluids. (myelisakit.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Histidine Ammonia Lyase (HAL) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (myelisakit.com)
- Description: A sandwich ELISA kit for detection of Histidine Ammonia Lyase from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (myelisakit.com)
- PhD thesis in protein crystallography "X-ray crystallographic structure solution of Histidine Ammonia-Lyase from Pseudomonas putida by multiple isomorphous replacement. (unibas.ch)
Enzymes4
- The enzymes often display high en. (researchgate.net)
- In support of this hypothesis, the recycling enzymes, argininosuccinate synthase (AS) and argininosuccinate lyase (AL), have been shown to colocalize with eNOS in caveolae, a subcompartment of the plasma membrane. (biologists.com)
- Carbon-nitrogen (C−N) lyases are enzymes that normally catalyze the cleavage of C−N bonds. (rug.nl)
- Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA . (bvsalud.org)
Concentrations2
- Hepatic ammonia concentrations decreased with increased duration of crowding. (biologists.com)
- These drugs lower blood ammonia concentrations by conjugation reactions involving acylation of amino acids. (medscape.com)
Gene4
- IMSEAR at SEARO: Identification Of Phenyl Alanine Ammonia Lyase Gene Involved In The Synthesis Of Anacardic Acid In Anacardium Occidentale L. (who.int)
- Sija S. L.. Identification Of Phenyl Alanine Ammonia Lyase Gene Involved In The Synthesis Of Anacardic Acid In Anacardium Occidentale L.. International Journal of Pharmaceutical Sciences and Drug Research. (who.int)
- The current study was conducted to find out the presence of anacardic acid in ethyl acetate extract of young leaves of cashew using high performance thin layer chromatography (HPTLC) method and the presence of phenyl alanine ammonia lyase gene also plays a role in the biosynthesis of anacardic acid in young leaves was also confirmed by cDNA synthesis from a cellular mRNA template connected to the polymerase chain reaction (PCR). (who.int)
- Argininosuccinate lyase (ASL) deficiency: mutation analysis in 27 patients and a completed structure of the human ASL gene. (medscape.com)
Argininosuccinate synthetase2
- Quantitative PCR was utilized to determine liver GS, CPS, OCT, ARG, argininosuccinate synthetase (ASS) and argininosuccinate lyase (ASL) mRNA expression. (biologists.com)
- Ammonul must be administered with arginine for carbamyl phosphate synthetase (CPS), ornithine transcarbamylase (OTC), argininosuccinate synthetase (ASS), or argininosuccinate lyase (ASL) deficiencies. (medscape.com)
Deficiency8
- Nagamani SC, Erez A, Lee B. Argininosuccinate lyase deficiency. (medscape.com)
- Long-term outcome of patients with argininosuccinate lyase deficiency diagnosed by newborn screening in Austria. (medscape.com)
- Argininosuccinate lyase deficiency: longterm outcome of 13 patients detected by newborn screening. (medscape.com)
- Detection of neonatal argininosuccinate lyase deficiency by serum tandem mass spectrometry. (medscape.com)
- No routine laboratory data assist diagnosis of argininosuccinate (ASA) lyase deficiency. (medscape.com)
- All 50 states in the United States include argininosuccinate (ASA) lyase deficiency in their newborn screening programs. (medscape.com)
- Carbamoyl phosphate synthetase (CPS) deficiency is a urea cycle defect that results from a deficiency in an enzyme that mediates the normal path for incorporation of ammonia. (medscape.com)
- In patients with homozygous CPS I deficiency, the ability to fix waste nitrogen is completely absent, resulting in increasing levels of free ammonia with the attendant effects on the CNS. (medscape.com)
Protein2
- The results revealed that at 8oC and after 75 days past, phenylalanin ammonia-lyase activity and total protein increased concomitantly with total ANTHOCYANIN , but antioxidant capacity and total phenols decreased. (sid.ir)
- By contrast, functional analysis using the SEED ontology found that sucrose induced changes in protein relative abundance patterns for pathways involving glycolysis, lactate production, aciduricity, and ammonia/glutamate metabolism that were conserved across taxonomically diverse dysbiotic oral microcosm biofilm communities. (biomedcentral.com)
Amino1
- This review focuses on recent (last five years) applications of native and engineered C−N lyases, either as stand-alone biocatalysts or as part of multienzymatic and chemoenzymatic cascades, in enantioselective synthesis of noncanonical amino acids and dinitrogen-fused heterocycles, which are useful tools for neurobiological research and important synthetic precursors to pharmaceuticals and food additives. (rug.nl)
Urea4
- Ammonia control and neurocognitive outcome among urea cycle disorder patients treated with glycerol phenylbutyrate. (medscape.com)
- Ammonia Control in Children Ages 2 Months through 5 Years with Urea Cycle Disorders: Comparison of Sodium Phenylbutyrate and Glycerol Phenylbutyrate. (medscape.com)
- As with all other urea cycle disorders, clinical suspicion is essential and should prompt the clinician to obtain blood ammonia levels, which are significantly elevated in symptomatic patients. (medscape.com)
- Carglumic acid acts as an activator of carbamoyl phosphate synthetase (CPS 1), improves or restores the function of the urea cycle, and facilitates ammonia detoxification and urea production. (medscape.com)
Absent1
- Neonatal argininosuccinic aciduria with normal brain and kidney but absent liver argininosuccinate lyase activity. (medscape.com)
Activity1
- Overall, activity of the cycle is regulated by the rate of synthesis of N -acetylglutamate, the enzyme activator of CPS I, which initiates incorporation of ammonia into the cycle. (medscape.com)
Production1
- Requirement of argininosuccinate lyase for systemic nitric oxide production. (medscape.com)
Histidine9
- Structures of Two Histidine Ammonia-Lyase Modifications and Implications for the Catalytic Mechanism. (expasy.org)
- The enzyme histidine ammonia lyase (HAL) undergoes a related posttranslational modification to generate an electrophile from the tripeptide loop sequence Ala-Ser-Gly ( 19 ). (pnas.org)
- This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). (enzyme-database.org)
- Schwede, T.F., Rétey, J. and Schulz, G.E. Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. (enzyme-database.org)
- which is mediated by the enzyme histidine ammonia-lyase. (bovinedb.ca)
- Histidine ammonia-lyase is a cytosolic enzyme catalyzing the first reaction in histidine catabolism, the nonoxidative deamination of L-histidine to trans-urocanic acid. (nih.gov)
- Histidine ammonia-lyase defects cause histidinemia which is characterized by increased histidine and histamine and decreased urocanic acid in body fluids. (nih.gov)
- These together with our earlier finding that histidine ammonia-lyase (HAL) gene in histidine catabolic pathway is similarly regulated by T3 in the intestine suggest that histidine catabolism plays a critical role in the formation of adult intestinal stem cells during metamorphosis. (nih.gov)
- METHODS AND RESULTS: By conducting whole exome sequencing on 1152 African Americans in the Atherosclerosis Risk in Communities (ARIC) study and focusing on loss-of-function (LoF) variants, we identified 3 novel rare LoF variants in HAL, a gene that encodes histidine ammonia-lyase in the first step of histidine catabolism. (nih.gov)
Aspartate ammon3
- Aspartate ammonia-lyase homotetramer, Bacillus sp. (wikipedia.org)
- The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming) . (wikipedia.org)
- Other names in common use include aspartase , fumaric aminase , L-aspartase , and L-aspartate ammonia-lyase . (wikipedia.org)
Argininosuccinate lyase3
- Nagamani SC, Erez A, Lee B. Argininosuccinate lyase deficiency. (medscape.com)
- Requirement of argininosuccinate lyase for systemic nitric oxide production. (medscape.com)
- ASA is caused by mutations in the ASL gene (7q11.21) that encodes the enzyme argininosuccinate lyase. (orpha.net)
Tyrosine ammonia-lyase1
- They are synthesized in plants and some fungi through the phenylalanine ammonia lyase (PAL) and tyrosine ammonia lyase (TAL) pathways. (bvsalud.org)
Activities of phenylalanine ammon3
- Compared with the wounded water control, Si treatment induced a significant increase in the activities of phenylalanine ammonia-lyase, polyphenoloxidase, and peroxidase in sweet cherry fruit but did not increase the levels of lignin. (apsnet.org)
- Sugar beet seedlings treated with both types of CWP through their roots showed enhanced activities of phenylalanine ammonia lyase and chitinase, and D-type-treated seedlings also showed significantly higher cell wall-bound phenolic compounds, mainly ferulic acid, compared with the distilled-water-treatment control. (apsnet.org)
- The activities of phenylalanine ammonia-lyase and peroxidase enzymes were higher in plant growth-promoting bacteria treated and pathogen inoculated plants as compared to the control plants lacking the bacteria. (researchsquare.com)
Cleave carbon-nitrogen bonds1
- This enzyme belongs to the family of lyases , specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
Deamination1
- It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. (genome.jp)
Reaction5
- In biochemistry , a lyase is an enzyme that catalyzes the breaking (an "elimination" reaction ) of various chemical bonds by means other than hydrolysis (a "substitution" reaction ) and oxidation , often forming a new double bond or a new ring structure. (ipfs.io)
- Lyases differ from other enzymes in that they require only one substrate for the reaction in one direction, but two substrates for the reverse reaction. (ipfs.io)
- A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which catalyses first the γ-elimination of O-succinylhomoserine (with succinate as a leaving group) and then the addition of sulfide to the vinyl intermediate, this reaction was first classified as a lyase (EC 4.2.99.9), but was then reclassified as a transferase (EC 2.5.1.48). (ipfs.io)
- Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. (string-db.org)
- Compound 5 is fumaric acid generated in the reaction that converts ASA to arginine (6), which is mediated by ASA lyase. (medscape.com)
Plasma ammonia3
Chalcone synthase2
- Induction of chalcone synthase and phenylalanine ammonia-lyase by salicylic acid and Colletotrichum lindemuthianum in common bean. (academicjournals.org)
- UV-B radiation induced transcription of strawberry genes associated with disease resistance, such as phenylalanine ammonia lyase (PAL), chalcone synthase (CHS), chalcone isomerase (CHI), β-1,3-glucanase, and osmotin-like protein. (ishs.org)
Cystathionine gamma1
- EC 4.4.1.1 , cystathionine gamma-lyase). (genome.jp)
Phenylketonuria1
- We have recently observed promising success in a mouse model for treating the metabolic disorder phenylketonuria with phenylalanine ammonia lyase (PAL) from Rhodosporidium toruloides and Anabaena variabilis. (scripps.edu)
Pathway7
- Phenylalanine ammonia-lyase (PAL) is the first committed enzyme in the phenylpropanoid pathway. (ashs.org)
- A possible utilization pathway for citric acid was proposed linking it to acetyl-CoA through ATP-citrate lyase after isomerization to isocitrate catalyzed by aconitase [ 8 ]. (biomedcentral.com)
- Phenylalanine ammonia lyase (PAL) and p -coumarate 3-hydroxylase (C3H) are key enzymes in the phenylpropanoid pathway. (geneticsmr.com)
- In cattle, urocanic acid is involved in the metabolic pathway called the ammonia recycling pathway. (bovinedb.ca)
- GapMind also includes two other pathways: an oxidative pathway via glucosaminate ammonia-lyase, and a transmembrane transacetylase (NagX) pathway. (lbl.gov)
- Glucosaminate is then taken up and converted to 2-keto-3-deoxygluconate by an ammonia-lyase (EC 4.3.1.9 ) and phosphorylated (by kdgK) to enter the Entner-Doudoroff pathway. (lbl.gov)
- These molecules are produced by the phenyl ammonia lyase pathway. (bvsalud.org)
Encodes1
- ASL encodes a member of the lyase 1 family. (thermofisher.com)
Accumulation1
- This leads to accumulation of alanine and glutamine (transamination products of pyruvate and glutamate, respectively) and, finally, of ammonia. (medscape.com)
Blood ammonia levels2
- Hemodialysis, if available, reduces the blood ammonia levels more efficiently and quickly. (medscape.com)
- Failure to suspect hyperammonemia and to obtain blood ammonia levels results in certain morbidity and, likely, death because routine laboratory test findings are unrevealing. (medscape.com)
Maize1
- Potassium influenced phenylalanine ammonia-lyase, peroxidases and polyphenol oxidases in Fusarium graminearum infected maize (Zea mays L. (escholarship.org)
Argininosuccinic Aciduria1
- Argininosuccinic aciduria is an inherited disorder that causes ammonia to accumulate in the blood. (nih.gov)
Catalyzes3
- METase catalyzes the α, γ-elimination of methionine to α-ketobutyrate, methanethiol, and ammonia. (biovision.com)
- The encoded protein forms a cytosolic homotetramer and primarily catalyzes the reversible hydrolytic cleavage of argininosuccinate into arginine and fumarate, an essential step in the liver in detoxifying ammonia via the urea cycle. (thermofisher.com)
- Methionine γ-lyse (MGL) catalyzes the α, γ-elimination of l-methionine and its derivatives as well as the α, β-elimination of l-cysteine and its derivatives to produce α-keto acids, volatile thiols, and ammonia. (elsevier.com)
Recombinant1
- Other product candidates include PEG-PAL (PEGylated recombinant phenylalanine ammonia lyase), which is currently in Phase 1 clinical development for the treatment of PKU. (science20.com)
Hemodialysis1
- If ammonia levels do not normalize, hemodialysis is the next step. (nih.gov)
Hyperammonemia3
- [ 40 ] Hyperammonemia is a life-threatening condition, as elevated ammonia is a toxin especially on the central nervous system. (medscape.com)
- It is very important to remember that the first step in evaluating suspected hyperammonemia is to obtain an accurate blood ammonia level. (medscape.com)
- [ 42 , 43 ] The severely elevated ammonia level associated with prematurity is known as transient hyperammonemia of the newborn (THAN). (medscape.com)
1.141
- EC 6.3.2.22: Now EC 6.3.1.14 , diphthine-ammonia ligase. (wikibedia.ru)
Nitrogen3
- Ammonia is a compound of nitrogen and hydrogen, but it cannot be formed by the direct union of these gases. (dictionary.com)
- This diet helps produce equivalent quantities of ornithine for enhancement of urea cycle activity up to the point of argininosuccinate (ASA) lyase and, thus, enhances waste nitrogen incorporation. (medscape.com)
- An elevated ammonia level ≥ 100 µmol/L indicates an abnormality in nitrogen balance. (medscape.com)
Promoter1
- bean Phe ammonia lyase promoter. (87paydays.info)
Characterization1
- Purification and Characterization of Anabaena flos-aquae Phenylalanine Ammonia-Lyase as a Novel Approach for Myristicin Biotransformation. (nih.gov)
Metabolic1
- and (2), an irreversible dedifferentiation of the affected but viable cells accompanied by permanent metabolic alterations, increase in ON SECONDARY COLONY DEVELOPMENT IN BACTERIA growth-rate, and functional release from en- vironmental inhibition. (nih.gov)
Ammonium3
- Ammonium hydroxide forms when ammonia dissolves in water. (nih.gov)
- Ammonium hydroxide can also release ammonia gas into the air. (nih.gov)
- The concentration of ammonia and ammonium ions in the blood is normally very low. (microbenotes.com)
Metabolism1
- Methionine gamma-lyase (EC 4.4.1.11) from Pseudomonas putida is a PLP-dependent enzyme which plays a central role in sulfur amino acid metabolism. (biovision.com)
Arginine1
- acid arginine (a building block of proteins) and ammonia to accumulate gradually in the blood. (nih.gov)
Acid2
- They are dissolved by strong hydrochloric acid, and recrystallize as octahedra upon addition of ammonia. (dictionary.com)
- His results for ammonia, as well as nitric acid, are given in the subjoined table. (dictionary.com)
Clinical1
- In the newborn period, a normal ammonia level is less than 50 µmol/L. [ 39 ] A blood ammonia level between 70 and 100 µmol/L should be viewed in conjunction with clinical findings. (medscape.com)
Liver4
- Ammonia (NH3) is produced by cells throughout the body, especially the intestines, liver, and kidneys. (nih.gov)
- is also used to reduce the amount of ammonia in the blood of patients with liver disease. (nih.gov)
- Ammonia travels to the liver from other tissues, mainly in the form of alanine and glutamine. (microbenotes.com)
- Ammonia is also produced by bacteria in the gut and travels to the liver via the hepatic portal vein. (microbenotes.com)