5-Aminolevulinate Synthetase: An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.Aminolevulinic Acid: A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.Porphobilinogen Synthase: An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.Anemia, Sideroblastic: Anemia characterized by the presence of erythroblasts containing excessive deposits of iron in the marrow.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.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.2',5'-Oligoadenylate Synthetase: An enzyme that catalyzes the conversion of ATP into a series of (2'-5') linked oligoadenylates and pyrophosphate in the presence of double-stranded RNA. These oligonucleotides activate an endoribonuclease (RNase L) which cleaves single-stranded RNA. Interferons can act as inducers of these reactions. EC 2.7.7.-.Hydroxymethylbilane Synthase: An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8Heptanoates: Salts and esters of the 7-carbon saturated monocarboxylic acid heptanoic acid.Boranes: The collective name for the boron hydrides, which are analogous to the alkanes and silanes. Numerous boranes are known. Some have high calorific values and are used in high-energy fuels. (From Grant & Hackh's Chemical Dictionary, 5th ed)Hemin: Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.Allylisopropylacetamide: An allylic compound that acts as a suicide inactivator of CYTOCHROME P450 by covalently binding to its heme moiety or surrounding protein.Dicarbethoxydihydrocollidine: 1,4-Dihydro-2,4,6-trimethyl-3,5-pyridinedicarboxylic acid diethyl ester.Amino Acids, Neutral: Amino acids with uncharged R groups or side chains.Rhodobacter capsulatus: Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.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.Genetic Diseases, X-Linked: Genetic diseases that are linked to gene mutations on the X CHROMOSOME in humans (X CHROMOSOME, HUMAN) or the X CHROMOSOME in other species. Included here are animal models of human X-linked diseases.PorphobilinogenPeptide Synthases: Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.Keratosis: Any horny growth such as a wart or callus.Kinetics: The rate dynamics in chemical or physical systems.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Pyridoxal Phosphate: This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).Porphyrins: A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.Schiff Bases: Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)Ferrochelatase: A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Intramolecular Transferases: Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.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.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.Pyridoxal: The 4-carboxyaldehyde form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.Erythroblasts: Immature, nucleated ERYTHROCYTES occupying the stage of ERYTHROPOIESIS that follows formation of ERYTHROID PRECURSOR CELLS and precedes formation of RETICULOCYTES. The normal series is called normoblasts. Cells called MEGALOBLASTS are a pathologic series of erythroblasts.Immunologic Tests: Immunologic techniques involved in diagnosis.Aspartate-tRNA Ligase: An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.Methionine-tRNA Ligase: An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.Tryptophan-tRNA Ligase: An enzyme that activates tryptophan with its specific transfer RNA. EC 6.1.1.2.Iron-Regulatory Proteins: Proteins that regulate cellular and organismal iron homeostasis. They play an important biological role by maintaining iron levels that are adequate for metabolic need, but below the toxicity threshold.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Protoporphyrins: Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.Isoleucine-tRNA Ligase: An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.Aspartate-Ammonia Ligase: An enzyme that catalyzes the formation of asparagine from ammonia and aspartic acid, in the presence of ATP. EC 6.3.1.1.Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Pyridoxine: The 4-methanol form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. Although pyridoxine and Vitamin B 6 are still frequently used as synonyms, especially by medical researchers, this practice is erroneous and sometimes misleading (EE Snell; Ann NY Acad Sci, vol 585 pg 1, 1990).Phenylalanine-tRNA Ligase: An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.Tyrosine-tRNA Ligase: An enzyme that activates tyrosine with its specific transfer RNA. EC 6.1.1.1.Photochemotherapy: Therapy using oral or topical photosensitizing agents with subsequent exposure to light.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.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.Circular Dichroism: A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Leucine-tRNA Ligase: An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.Serine-tRNA Ligase: An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.Valine-tRNA Ligase: An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9Cloning, 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.Argininosuccinate Synthase: An enzyme of the urea cycle that catalyzes the formation of argininosuccinic acid from citrulline and aspartic acid in the presence of ATP. Absence or deficiency of this enzyme causes the metabolic disease CITRULLINEMIA in humans. EC 6.3.4.5.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Enzyme Induction: An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.Glutamate-tRNA Ligase: An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.
delta-Aminolevulinate synthetases in the liver cytosol fraction and mitochondria of mice treated with allylisopropylacetamide and 3,5-dicarbethoxyl-1,4-dihydrocollidine. (1/369)
Hepatic delta-aminolevulinate (ALA) synthetase was induced in mice by the administration of allylisopropylacetamide (AIA) and 3,5-dicarbethoxy-1,4-dihydrocollidine (DDC). In both cases, a significant amount of ALA synthetase accumulated in the liver cytosol fraction as well as in the mitochondria. The apparent molecular weight of the cytosol ALA synthetase was estimated to be 320,000 by gel filtration, but when the cytosol ALA synthetase was subjected to sucrose density gradient centrifugation, it showed a molecular weight of 110,000. In the mitochondria, there were two different sizes of ALA synthetase with molecular weights of 150,000 and 110,000, respectively; the larger enzyme was predominant in DDC-treated mice, whereas in AIA-treated mice and normal mice the enzyme existed mostly in the smaller form. When hemin was injected into mice pretreated with DDC, the molecular size of the mitochondrial ALA synthetase changed from 150,000 to 110,000. The half-life of ALA synthetase in the liver cytosol fraction was about 30 min in both the AIA-treated and DDC-treated mice. The half-life of the mitochondrial ALA synthetase in AIA-treated mice and normal mice was about 60 min, but in DDC-treated mice the half-life was as long as 150 min. The data suggest that the cytosol ALA synthetase of mouse liver is a protein complex with properties very similar to those of the cytosol ALA synthetase of rat liver, which has been shown to be composed of the enzyme active protein and two catalytically inactive binding proteins, and that ALA synthetase may be transferred from the liver cytosol fraction to the mitochondria with a size of about 150,000 daltons, followed by its conversion to enzyme with a molecular weight of 110,000 within the mitochondria. The process of intramitochondrial enzyme degradation seems to be affected in DDC-treated animals. (+info)Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. (2/369)
X-linked sideroblastic anemia (XLSA) in four unrelated male probands was caused by missense mutations in the erythroid-specific 5-aminolevulinate synthase gene (ALAS2). All were new mutations: T647C, C1283T, G1395A, and C1406T predicting amino acid substitutions Y199H, R411C, R448Q, and R452C. All probands were clinically pyridoxine-responsive. The mutation Y199H was shown to be the first de novo XLSA mutation and occurred in a gamete of the proband's maternal grandfather. There was a significantly higher frequency of coinheritance of the hereditary hemochromatosis (HH) HFE mutant allele C282Y in 18 unrelated XLSA hemizygotes than found in the normal population, indicating a role for coinheritance of HFE alleles in the expression of this disorder. One proband (Y199H) with severe and early iron loading coinherited HH as a C282Y homozygote. The clinical and hematologic histories of two XLSA probands suggest that iron overload suppresses pyridoxine responsiveness. Notably, reversal of the iron overload in the Y199H proband by phlebotomy resulted in higher hemoglobin concentrations during pyridoxine supplementation. The proband with the R452C mutation was symptom-free on occasional phlebotomy and daily pyridoxine. These studies indicate the value of combined phlebotomy and pyridoxine supplementation in the management of XLSA probands in order to prevent a downward spiral of iron toxicity and refractory anemia. (+info)Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania). (3/369)
1. Activity of 5-aminolaevulinate synthetase was measured in the midgut and other tissues of the last larval instar of the southern armyworm (Spodoptera eridania Cramer, formerly Prodenia eridania Cramer). 2. Optimum conditions for measuring the activity were established with respect to all variables involved and considerable differences from those reported for mammalian enzyme preparations were found. 3. Maximum activity (20 nmol/h per mg of protein) occurs 18-24 h after the fifth moult and thereafter decreases to trace amounts as the larvae age and approach pupation. 4. Synthetase activity was rapidly induced by oral administration (in the diet) of pentamethylbenzene, phenobarbital, diethyl 1,4-dihydro-2,4,6-trimethylpyridine-3, 5-dicarboxylate, and 2-allyl-2-isopropylacetamide. 5. Puromycin inhibited the induction of synthetase by pentamethylbenzene. 6. Induction of 5-aminolaevulinate synthetase correlated well with the induction of microsomal N-demethylation of p-chloro-N-methylaniline, except for phenobarbital, which induced the microsomal oxidase relatively more than the synthetase. (+info)Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release. (4/369)
5-Aminolevulinate synthase (ALAS) is the first enzyme of the heme biosynthetic pathway in non-plant eukaryotes and the alpha-subclass of purple bacteria. The pyridoxal 5'-phosphate cofactor at the active site undergoes changes in absorptive properties during substrate binding and catalysis that have allowed us to study the kinetics of these reactions spectroscopically. Rapid scanning stopped-flow experiments of murine erythroid 5-aminolevulinate synthase demonstrate that reaction with glycine plus succinyl-CoA results in a pre-steady-state burst of quinonoid intermediate formation. Thus, a step following binding of substrates and initial quinonoid intermediate formation is rate-determining. The steady-state spectrum of the enzyme is similar to that formed in the presence of 5-aminolevulinate, suggesting that release of this product limits the overall rate. Reaction of either glycine or 5-aminolevulinate with ALAS is slow (kf = 0.15 s-1) and approximates kcat. The rate constant for reaction with glycine is increased at least 90-fold in the presence of succinyl-CoA and most likely represents a slow conformational change of the enzyme that is accelerated by succinyl-CoA. The slow rate of reaction of 5-aminolevulinate with ALAS is 5-aminolevulinate-independent, suggesting that it also represents a slow isomerization of the enzyme. Reaction of succinyl-CoA with the enzyme-glycine complex to form a quinonoid intermediate is a biphasic process and may be irreversible. Taken together, the data suggest that turnover is limited by release of 5-aminolevulinate or a conformational change associated with 5-aminolevulinate release. (+info)Phylogenetic analysis of the 5-aminolevulinate synthase gene. (5/369)
The evolution of 5-aminolevulinate synthase (ALS) was studied by acquiring sequence data and generating phylogenetic trees. Gene sequences were already available for a variety of vertebrates (which have both a housekeeping and an erythroid form of the gene), fungi, alpha-proteobacteria, and one protist and one protostome. In order to generate representative trees, ALS sequence data were acquired from various deuterostomes and protostomes. The species and tissues selected for study were beluga whale liver, hagfish blood, sea urchin gonadal tissue, cuttlefish hepatopancreas, horseshoe crab hepatopancreas, and bloodworm blood. The new sequences and those previously published were examined for the presence of heme-regulatory motifs (HRMs) and iron-responsive elements (IREs). The HRMs are present in almost all eukaryotic species, which suggests their fundamental role in the regulation of ALS. The IREs are present in all vertebrate erythroid forms of ALS, which indicates that in those animals, expression of the erythroid form of the enzyme and, hence, hemoglobin production can be influenced by the intracellular content of iron. The new sequences were aligned with previously reported ALS sequences, and phylogenetic analyses were performed. The resulting trees provided evidence regarding the timing of the gene duplication event that led to the two forms of the ALS gene in vertebrates. It appears that the housekeeping and erythroid forms of ALS probably arose before the divergence of hagfish from the deuterostome line leading to the vertebrates. The data also add to the evidence indicating that alpha-proteobacteria are the nearest contemporary relatives of mitochondria. (+info)Respiratory uncoupling induces delta-aminolevulinate synthase expression through a nuclear respiratory factor-1-dependent mechanism in HeLa cells. (6/369)
Nuclear respiratory factor (NRF)-1 appears to be important for the expression of several respiratory genes, but there is no direct evidence that NRF-1 transduces a physiological signal into the production of an enzyme critical for mitochondrial biogenesis. We generated HeLa cells containing plasmids allowing doxycycline-inducible expression of uncoupling protein (UCP)-1. In the absence of doxycycline, UCP-1 mRNA and protein were undetectable. In the presence of doxycycline, UCP-1 was expressed and oxygen consumption doubled. This rise in oxygen consumption was associated with an increase in NRF-1 mRNA. It was also associated with an increase in NRF-1 protein binding activity as determined by electrophoretic mobility shift assay using a functional NRF-1 binding site from the delta-aminolevulinate (ALA) synthase promoter. Respiratory uncoupling also caused a time-dependent increase in protein levels of ALA synthase, an early marker for mitochondrial biogenesis. ALA synthase induction by respiratory uncoupling was prevented by transfecting cells with an oligonucleotide antisense to the region of the NRF-1 initiation codon; a scrambled oligonucleotide with the same base composition had no effect. Respiratory uncoupling increases oxygen consumption and lowers energy reserves. In HeLa cells, uncoupling also increases ALA synthase, an enzyme critical for mitochondrial respiration, but only if translatable mRNA for NRF-1 is available. These data suggest that the transcription factor NRF-1 plays a key role in cellular adaptation to energy demands by translating physiological signals into an increased capacity for generating energy. (+info)Characterization of the rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes, HemA and HemT, isolated from recombinant Escherichia coli. (7/369)
The hemA and hemT genes encoding 5-aminolaevulinic acid synthase (ALAS) from the photosynthetic bacterium Rhodobacter sphaeroides, were cloned to allow high expression in Escherichia coli. Both HemA and HemT appeared to be active in vivo as plasmids carrying the respective genes complemented an E. coli hemA strain (glutamyl-tRNA reductase deficient). The over-expressed isoenzymes were isolated and purified to homogeneity. Isolated HemA was soluble and catalytically active whereas HemT was largely insoluble and failed to show any activity ex vivo. Pure HemA was recovered in yields of 5-7 mg x L-1 of starting bacterial culture and pure HemT at 10 mg x L-1 x HemA has a final specific activity of 13 U x mg-1 with 1 unit defined as 1 micromol of 5-aminolaevulinic acid formed per hour at 37 degrees C. The Km values for HemA are 1.9 mM for glycine and 17 microM for succinyl-CoA, with the enzyme showing a turnover number of 430 h-1. In common with other ALASs the recombinant R. sphaeroides HemA requires pyridoxal 5'-phosphate (PLP) as a cofactor for catalysis. Removal of this cofactor resulted in inactive apo-ALAS. Similarly, reduction of the HemA-PLP complex using sodium borohydride led to > 90% inactivation of the enzyme. Ultraviolet-visible spectroscopy with HemA suggested the presence of an aldimine linkage between the enzyme and pyridoxal 5'-phosphate that was not observed when HemT was incubated with the cofactor. HemA was found to be sensitive to reagents that modify histidine, arginine and cysteine amino acid residues and the enzyme was also highly sensitive to tryptic cleavage between Arg151 and Ser152 in the presence or absence of PLP and substrates. Antibodies were raised to both HemA and HemT but the respective antisera were not only found to bind both enzymes but also to cross-react with mouse ALAS, indicating that all of the proteins have conserved epitopes. (+info)A photosensitising adenovirus for photodynamic therapy. (8/369)
We have developed a new approach to photodynamic therapy based on adenoviral transduction of the rate-limiting enzyme in heme synthesis. Conventional phototherapy uses porphyrin-based chemical photosensitisers, including delta-aminolaevulinic acid (ALA) which is converted to protoporphyrin IX (PpIX) by the enzymes of the heme biosynthetic pathway. The lack of a specific mechanism for targeting chemical photosensitisers and PpIX to tumour cells means that therapeutic irradiation can damage normal tissue and exposure to sunlight following treatment can cause severe burns. The rate limiting enzyme in PpIX synthesis is ALA-synthase (ALA-S). We have developed a new yeast vector system for manipulation of the adeno- virus genome and used it to construct a virus expressing a mutant form of ALA-S lacking the iron response elements which regulate ALA-S translation and the heme regulatory motifs which regulate import of ALA-S into mitochondria. The virus induces a large increase in PpIX expression and confers photosensitivity on cultured cells. Unlike conventional photodynamic therapy, a viral approach makes it possible to restrict photosensitivity by biological rather than purely physical or chemical means. As with HSV thymidine kinase, ALA-S expression is a general mechanism for sensitisation to a therapeutic agent which can easily be adapted to whatever means of gene delivery is most effective. (+info)... succinyl-CoA synthetase, and mitoferrin-1. Multiple studies have suggested the existence of an oligomeric complex that enables ... 269 (1): 390-5. PMID 8276824. Wang X, Poh-Fitzpatrick M, Carriero D, Ostasiewicz L, Chen T, Taketani S, Piomelli S (April 1993 ... 89 (1): 281-5. doi:10.1073/pnas.89.1.281. PMC 48220 . PMID 1729699. Lamoril J, Boulechfar S, de Verneuil H, Grandchamp B, ... 378 (5): 1074-1083. doi:10.1016/j.jmb.2008.03.040. PMC 2852141 . PMID 18423489. Bencze, Krisztina Z.; Yoon, Taejin; Mill?n- ...
... amino acyl-trna synthetases MeSH D08.811.464.263.200.050 --- alanine-tRNA ligase MeSH D08.811.464.263.200.100 --- arginine-tRNA ... atp synthetase complexes MeSH D08.811.913.696.650.150.500 --- proton-translocating atpases MeSH D08.811.913.696.650.150.500.249 ... fatty acid synthetase complex MeSH D08.811.600.391 --- glycine decarboxylase complex MeSH D08.811.600.391.100 --- ... uroporphyrinogen iii synthetase MeSH D08.811.520.241.700 --- polysaccharide-lyases MeSH D08.811.520.241.700.350 --- ...
Succinyl-CoA synthetase (SCS) is a mitochondrial matrix enzyme that acts as a heterodimer, being composed of an invariant alpha ... Succinyl-CoA synthetase SUCLG1 SUCLG2 GRCh38: Ensembl release 89: ENSG00000136143 - Ensembl, May 2017 GRCm38: Ensembl release ... Furuyama K, Sassa S (March 2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is ... Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), also known as ADP-forming succinyl-CoA synthetase (SCS- ...
... argininosuccinate synthetase BNC2: zinc finger protein basonuclin-2 C9orf64: chromosome 9 open reading frame 64 C9orf78: ... aminolevulinate, delta-, dehydratase ALS4: amyotrophic lateral sclerosis 4 ANGPTL2: angiopoietin-related protein 2 ASS: ... 5 (2): 157-74. doi:10.1089/109065701753145664. PMID 11551106. Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and ... 11 (5): 206. doi:10.1186/gb-2010-11-5-206. PMC 2898077 . PMID 20441615. "Statistics & Downloads for chromosome 9". HUGO Gene ...
LARS2: leucyl-tRNA synthetase, mitochondrial. *LIMD1: LIM domain-containing protein 1. *LINC00312: Long intergenic non-protein- ... ALAS1: aminolevulinate, delta-, synthase 1. *APEH: encoding enzyme Acylamino-acid-releasing enzyme ... doi:10.1186/gb-2010-11-5-206. PMC 2898077. PMID 20441615.. *^ "Statistics & Downloads for chromosome 3". HUGO Gene Nomenclature ... So CCDS's gene number prediction represents a lower bound on the total number of human protein-coding genes.[5] ...
Delta-aminolevulinate synthase 2 also known as ALAS2 is a protein that in humans is encoded by the ALAS2 gene. ALAS2 is an ... Furuyama K, Sassa S (Mar 2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is ... "Entrez Gene: Delta-aminolevulinate synthase 2". Human ALAS2 genome location and ALAS2 gene details page in the UCSC Genome ... Cotter PD, Willard HF, Gorski JL, Bishop DF (May 1992). "Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) ...
Partial list of the genes located on p-arm (short arm) of human chromosome 3: ALAS1: aminolevulinate, delta-, synthase 1 APEH: ... leucyl-tRNA synthetase, mitochondrial LIMD1: LIM domain-containing protein 1 LINC00312: Long intergenic non-protein-coding RNA ... 11 (5): 206. doi:10.1186/gb-2010-11-5-206. PMC 2898077 . PMID 20441615. "Statistics & Downloads for chromosome 3". HUGO Gene ... ETS variant 5 FAM43A: family with sequence similarity 43 member A FAM162A: family with sequence similarity 162 member A GYG1: ...
Additionally, alcohol has been shown to increase the activity of the delta-aminolevulinic acid synthetase (ALA synthetase), the ... 14 (38): 5913-5. doi:10.3748/wjg.14.5913. PMC 2751904 . PMID 18855993. Sökmen, M; Demirsoy, H; Ersoy, O; Gökdemir, G; Akbayir, ... 18 (3): 200-5. PMID 17891697. Frank, J; Poblete-Gutiérrez, P; Weiskirchen, R; Gressner, O; Merk, H. F.; Lammert, F (2006). " ... 58 (5): 1089-97. doi:10.1172/JCI108560. PMC 333275 . PMID 993332. Di Padova, C.; Marchesi, L.; Cainelli, T.; Gori, G.; ...
AKs are one of the most common dermatologic lesions for which photodynamic therapy using topical methyl aminolevulinate (MAL) ... destroys AKs by blocking methylation of thymidylate synthetase, thereby interrupting DNA and RNA synthesis. This in turn ... Topical 5-FU is the most utilized treatment for AK, and often results in effective removal of the lesion. Overall, there is a ... 5-FU may be up to 90% effective in treating non-hyperkeratotic lesions. The most commonly used application regimen consists of ...
There are two different asparagine synthetases found in bacterial species. These two synthetases, which are both referred to as ... Porphyrins are synthesized from glycine and succinyl CoA, which condense to give δ-aminolevulinate. Two molecules of this ... When there is too much of any one of them, that one will allosterically control the DAHP synthetase by "turning it off". With ... The conversion of glutamate to glutamine is regulated by glutamine synthetase (GS) and is a highly significant step in nitrogen ...
... which is made of both nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) modules. Nonribosomal peptides and ... Pingyangmycin (Bleomycin A5). References[edit]. *^ a b c d e f g h i j k l m n o p q r "Bleomycin Sulfate". The American ... 3-{[(2'-{(5S,8S,9S,10R,13S)-15-{6-amino-2- [(1S)-3-amino-1-{[(2S)-2,3-diamino-3-oxopropyl]amino}-3-oxopropyl] -5- ... 5: 13419. doi:10.1038/srep13419. PMC 4542162. PMID 26289670. Archived from the original on 2016-05-03. In our studies, mice ...
Looking for Erythroid 5-aminolevulinate synthetase deficiency? Find out information about Erythroid 5-aminolevulinate ... synthetase deficiency. A usually hereditary, pathologic disorder of porphyrin metabolism characterized by porphyrinuria and ... The little-known disease porphyria is... Explanation of Erythroid 5-aminolevulinate synthetase deficiency ... redirected from Erythroid 5-aminolevulinate synthetase deficiency). Also found in: Dictionary, Thesaurus, Medical. porphyria. [ ...
67417 Ears2; glutamyl-tRNA synthetase 2, mitochondrial 107508 Eprs; glutamyl-prolyl-tRNA synthetase 17025 Alad; aminolevulinate ... glutamyl-tRNA synthetase [EC:6.1.1.17] K14163 EPRS; bifunctional glutamyl/prolyl-tRNA synthetase [EC:6.1.1.17 6.1.1.15] K01698 ... 15159 Hccs; holocytochrome c synthetase 12870 Cp; ceruloplasmin 15203 Heph; hephaestin 14297 Fxn; frataxin K00643 E2.3.1.37; 5- ... 22247 Umps; uridine monophosphate synthetase 17960 Nat1; N-acetyl transferase 1 17961 Nat2; N-acetyltransferase 2 (arylamine N- ...
... was used to unravel the diversity and phylogeny of genes encoding 5-aminolevulinic acid synthases (ALASs, hemA gene products) ... was used to unravel the diversity and phylogeny of genes encoding 5-aminolevulinic acid synthases (ALASs, hemA gene products) ... Mayer, S. M., and Beale, S. I. (1992). Succinyl-coenzyme A synthetase and its role in delta-aminolevulinic acid biosynthesis in ... This specifically concerns hemA alleles encoding cyclizing type of aminolevulinate synthase, as a part of the C5N-encoding gene ...
... succinyl-CoA synthetase, and mitoferrin-1. Multiple studies have suggested the existence of an oligomeric complex that enables ... 269 (1): 390-5. PMID 8276824. Wang X, Poh-Fitzpatrick M, Carriero D, Ostasiewicz L, Chen T, Taketani S, Piomelli S (April 1993 ... 89 (1): 281-5. doi:10.1073/pnas.89.1.281. PMC 48220 . PMID 1729699. Lamoril J, Boulechfar S, de Verneuil H, Grandchamp B, ... 378 (5): 1074-1083. doi:10.1016/j.jmb.2008.03.040. PMC 2852141 . PMID 18423489. Bencze, Krisztina Z.; Yoon, Taejin; Mill?n- ...
... amino acyl-trna synthetases MeSH D08.811.464.263.200.050 --- alanine-tRNA ligase MeSH D08.811.464.263.200.100 --- arginine-tRNA ... atp synthetase complexes MeSH D08.811.913.696.650.150.500 --- proton-translocating atpases MeSH D08.811.913.696.650.150.500.249 ... fatty acid synthetase complex MeSH D08.811.600.391 --- glycine decarboxylase complex MeSH D08.811.600.391.100 --- ... uroporphyrinogen iii synthetase MeSH D08.811.520.241.700 --- polysaccharide-lyases MeSH D08.811.520.241.700.350 --- ...
A transcription factor that controls the expression of variety of proteins including CYTOCHROME C and 5-AMINOLEVULINATE ... SYNTHETASE. It plays an important role in maintenance of the RESPIRATORY CHAIN of MITOCHONDRIA. ...
Differential effects of metalloporphyrins on messenger RNA levels of delta-aminolevulinate synthase and heme oxygenase. Studies ... "Differential effects of metalloporphyrins on messenger RNA levels of delta-aminolevulinate synthase and heme oxygenase. Studies ... 5-Aminolevulinate Synthetase; Animals; Cells, Cultured; Chick Embryo; Heme Oxygenase (Decyclizing); Liver; Metalloporphyrins; ...
5-Aminolevulinate Synthetase; Animals; Cells, Cultured; Chick Embryo; Cytochrome P-450 Enzyme System; Deferoxamine; Heme; Liver ...
Chlorophyll Biosynthesis: Various Chlorophyllides as Exogenous Substrates for Chlorophyll Synthetase. Benz, Jürgen / Rüdiger, ... 5-year IMPACT FACTOR: 0.912. CiteScore 2017: 0.92. SCImago Journal Rank (SJR) 2017: 0.288. Source Normalized Impact per Paper ( ... Darstellung 5′.5″-phosphatverknüpfter Dinucleoside / Preparation of 5′,5″-Phosphate Linked Dinucleosides. Bomemann, Siegmar / ... An Evolutionary Tree Based on Monoclonal Antibody-Recognized Surface Features of a Plastid Enzyme (5-Aminolevulinate ...
aminolevulinate, delta-, synthetase 2. 0.813. nkx2.2a. NK2 transcription factor related 2a. 0.812. ...
Association between δ-aminolevulinate dehydratase G177C polymorphism and blood lead levels in brain tumor patients. Taha MM, ... Influence of the common human delta-aminolevulinate dehydratase polymorphism on lead body burden. Wetmur JG. Wetmur JG. Environ ... 2015 Sep;3(5):995-1000. doi: 10.3892/mco.2015.589. Epub 2015 Jun 25. Mol Clin Oncol. 2015. PMID: 26623039 Free PMC article. ... 5 μg/dL). We also tested whether the ALAD genotype modified the relationship between blood lead level and mortality. ...
We show that the rate-limiting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the ...
IMSEAR is the collaborative product of Health Literature, Library and Information Services (HELLIS) Network Member Libraries in the WHO South-East Asia Region ...
amide synthetase. hypothetical protein, partial, Streptomyces sp. NRRL WC-3742, WP_078910860 ... BiosynthesisC5NPolyketide synthaseRubromycin Streptomyces Introduction. Hyaluromycin is a hyaluronidase inhibitor isolated from ... 5]. The strain grow well on ISP 3, ISP 4 and yeast-starch agars but poor on ISP 2, ISP 5, ISP 6, ISP 7, glucose-asparagine, ... The detected menaquinones were identified as MK-9(H8), MK-9(H6), MK-9(H4) and MK-9(H10) (5:37:57:1). The principal polar lipids ...
... delta-ALA synthetase , aminolevulinate, delta, synthase 1 , delta-ALA synthetase 1 , ALA-synthase , aminolevulinate, delta-, ... anti-Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 2 Antikörper * anti-Aminoacyl tRNA Synthetase ... delta-aminolevulinate synthase 1 , migration-inducing protein 4 , aminolevulinate synthase H , succinyl-CoA: glycine C-succinyl ... Show all anti-Aminolevulinate, delta-, Synthase 1 (ALAS1) Antikörper with Pubmed References. * Human Polyclonal ALAS1 Primary ...
Aminolevulinate dehydratase deficiency porphyria Synonyms: 5-Aminolevulinic acid dehydratase deficiency porphyria, ALA ... Synonyms: Erythrohepatic protoporphyria, EPP, Heme synthetase deficiency, Ferrochelatase deficiency Hepatoerythropoietic ...
Delta-aminolevulinate dehydratase deficiency porphyria see ALA dehydratase deficiency Dementia see CADASIL ... Heme synthetase deficiency see erythropoietic protoporphyria Hemochromatoses see hemochromatosis hemochromatosis hemoglobin M ... Erythroid 5-aminolevulinate synthetase deficiency see X-linked sideroblastic anemia Erythropoietic porphyria see congenital ... 5-ALA dehydratase-deficient porphyria see ALA dehydratase deficiency 5-aminolaevulinic dehydratase deficiency porphyria see ALA ...
2010, 5: e9181-10.1371/journal.pone.0009181.PubMedPubMed CentralView ArticleGoogle Scholar. ... 2004, 5: 123-135. 10.1038/nrg1271.View ArticleGoogle Scholar. *. Minorsky PV: The hot and the classic. Plant Physiol. 2003, 132 ... 10.1016/S1055-7903(03)00194-5.PubMedView ArticleGoogle Scholar. *. Timmis JN, Ayliffe MA, Huang CY, Martin W: Endosymbiotic ... 10.1016/S0168-9525(00)02209-5.PubMedView ArticleGoogle Scholar. *. Martin W: Mosaic bacterial chromosomes - a challenge en ...
aminolevulinate, delta-, synthetase 2. 0.062. capns1a. calpain, small subunit 1 a. 0.062. ... hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase. 0.023. ... tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta polypeptide b. 0.064. ...
Looking for online definition of erythrogenic in the Medical Dictionary? erythrogenic explanation free. What is erythrogenic? Meaning of erythrogenic medical term. What does erythrogenic mean?
5-Aminolevulinate synthase catalysis: The catcher in heme biosynthesis. Mol Genet Metab. 2019 11; 128(3):178-189. PMID: ... Molecular dynamics analysis of the structural and dynamic properties of the functionally enhanced hepta-variant of mouse 5- ... aminolevulinate synthase. J Biomol Struct Dyn. 2018 01; 36(1):152-165. PMID: 27928941. ... the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5- ...
holocarboxylase synthetase products*ADM2 products*adrenomedullin products*Hrs products*Prnp products*Vash1 products ... Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol ... A Kruppel-like factor KLF15 contributes fasting-induced transcriptional activation of mitochondrial acetyl-CoA synthetase gene ... 1990;5:166-71 pubmed ..m2, and if the PVR is greater than 4 units.m2 with the oxygen inhalation test or 7 units.m2 with the ...
These data indicate that the Cyp2a-4/5 complex is regulated in a different way in DBA/2 and C57BL/6 mice and that some ... 5 aminolevulinate synthetase*nuclease protection assays*steroid 16 alpha hydroxylase*beta naphthoflavone*ferrochelatase* ... Salonpää P, Iscan M, Pasanen M, Arvela P, Pelkonen O, Raunio H. Cerium-induced strain-dependent increase in Cyp2a-4/5 ( ... Effect of pyrazole, cobalt and phenobarbital on mouse liver cytochrome P-450 2a-4/5 (Cyp2a-4/5) expression. Biochem J. 1992;286 ...
Glutathione synthetase. Glycine amidinotransferase, mitochondrial. Serine--pyruvate aminotransferase. Serine ... The average adult ingests 3 to 5 grams of glycine daily. Glycine is involved in the bodys production of DNA, phospholipids and ... The average adult ingests 3 to 5 grams of glycine daily. Glycine is involved in the bodys production of DNA, phospholipids and ... 5-aminolevulinate synthase, nonspecific, mitochondrial. Glycine receptor subunit alpha-1. Glycine receptor subunit alpha-2. ...
Aminolevulinate dehydratase deficiency porphyria Synonyms: 5-Aminolevulinic acid dehydratase deficiency porphyria, ALA ... Synonyms: Erythrohepatic protoporphyria, EPP, Heme synthetase deficiency, Ferrochelatase deficiency Erythropoietic uroporphyria ...
BiosynthesisALAS2ErythroidFerrochelataseCyclizing 5-aminolevAcyl-CoA synthetaseALADDeficiencyEnzymePorphyrinALAS1GeneMetabolismGenesGlycineGlutamine synthetaseProteinsPrecursorKinaseAutosomal recessiveThymidylateCytochromeEnzymesAcidImiquimodExonucleaseAnemiaDelta0.04MoleculesLiverAmideGlutathioneUrineBasalCompounds
- We show that the rate-limiting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the peroxisome proliferator-activated receptor gamma coactivator 1alpha (PGC-1alpha). (nih.gov)
- 5-Aminolevulinate synthase catalysis: The catcher in heme biosynthesis. (harvard.edu)
- Regulation of haem biosynthesis in normoblastic erythropoiesis: role of 5-aminolaevulinic acid synthase and ferrochelatase. (naver.com)
- A comparative study of the inhibition of these two enzymes under in vivo and in vitro conditions showed that 5-aminolevulinic acid dehydratase is the major site of action of heavy metals in porphyrin biosynthesis. (bvsalud.org)
- Indicate which statement is true of tetrapyrrole biosynthesis in both animals and plants: A) δ -aminolevulinate is a tetrapyrrole precursor. (foodelphi.com)
- Which statement about the carbamoyl phosphate synthetase of mammals, which is used for pyrmidine biosynthesis, is true? (foodelphi.com)
- Distribution of the two pathways of 5-aminolevulinic acid biosynthesis in prokaryotes. (asmscience.org)
- 1988. Biosynthesis of δ-aminolevulinate in greening barley leaves. (asmscience.org)
- Erythropoietic protoporphyria (EPP) and X-linked protoporphyria (XLP) are inborn errors of heme biosynthesis with the same phenotype but resulting from autosomal recessive loss-of-function mutations in the ferrochelatase ( FECH ) gene and gain-of-function mutations in the X-linked erythroid-specific 5-aminolevulinate synthase ( ALAS2 ) gene, respectively. (springer.com)
- ALAS2 is a specific erythroid isoform of 5-aminolevulinate synthetase (ALAS) and is essential for synthesis of hemoglobin in erythroid cells. (spaceshipsla.com)
- XLSA is caused by mutations in the erythroid-specific gene coding 5-aminolevulinate synthase (ALAS2). (cdc.gov)
- Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts. (springer.com)
- An important gene associated with Anemia, Sideroblastic, 1 is ALAS2 (5'-Aminolevulinate Synthase 2), and among its related pathways/superpathways are Metabolism and Porphyrin and chlorophyll metabolism . (malacards.org)
- Anti-Correlation between the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5-Aminolevulinate Synthase. (harvard.edu)
- Transfection experiments showed that both Stat1α and Stat3 inhibited the induction by EPO of γ-globin and erythroid-specific 5-aminolevulinate synthetase transcripts, resulting in a reduction of the percentage of hemoglobin-positive cells. (ashpublications.org)
- Thus, we suggest the following four proteins for laboratory validation: delta-aminolevulinic acid dehydratase, ferrochelatase, ribose-5 phosphate isomerase and mitochondrial tyrosyl-tRNA synthetase. (beds.ac.uk)
- Recently, it has been shown that formation of the C 5 N unit and its attachment to core structures of antibiotics is directed by three enzymes: cyclizing 5-aminolevulinate synthase (cALAS encoded by a hemA homolog), amide synthase (AMS) and aminolevulinate-CoA ligase (ALL). (frontiersin.org)
- acyl-CoA synthetase long-chain family mem. (broadinstitute.org)
- The 5-aminolevulinic acid dehydratase (ALAD) G177C genetic polymorphism (rs 1800435) affects lead toxicokinetics and may alter the adverse effects of lead exposure. (cdc.gov)
- Comprehensive analysis of 5-aminolevulinic acid dehydrogenase (ALAD) variants and renal cell carcinoma risk among individuals exposed to lead. (cdc.gov)
- The last show a very variable degree of pyridoxine responsiveness, from 90% in X-linked sideroblastic anaemia (δ-aminolevulinate synthase deficiency) through 50% in homocystinuria (cystathionine β-synthase deficiency) to 5% in ornithinaemia with gyrate atrophy (ornithine δ-aminotransferase deficiency). (springer.com)
- 5. In Anglo-Saxon populations, neural tube defects, ranging from spina bifida to anencephaly (including hydrocephalus) are the most prevalent types of cerebral deficiency. (fondationlejeune.org)
- [5] Additionally, patients will often void a wine-red color urine with an increased concentration of uroporphyrin I due to their enzymatic deficiency. (wikipedia.org)
- 5 of these proteins are known to be associated with diseases, including ribose 5-phosphate isomerase deficiency, myopathy with lactic acidosis and sideroblastic anaemia, anemia due to disorders of glutathione metabolism, and two porphyrias, and we suspect the sixth enzyme to have disease associations which are not yet classified or understood based on the work described herein. (beds.ac.uk)
- 4-6) The increased ALA synthetase activity results in elevated levels of heme precursors proximal to the site of the specific enzyme deficiency. (medpdfarticles.com)
- GLRX5 gene codes for glutaredoxin 5, a mitochondrial enzyme, with an essential role in the formation of iron/sulfur clusters (Fe/S cluster). (bloodgenetics.com)
- Each type of porphyria has a characteristic pattern of overproduction and accumulation of heme precursors based upon the location of the dysfunctional enzyme in the The rate limiting step in heme synthesis is the condensation of succinyl CoA and glycine to form delta-amino levulinic acid (ALA), (2, 3) catalyzed by the mitochondrial enzyme ALA synthetase. (medpdfarticles.com)
- Methyl aminolevulinate cream is a porphyrin precursor used in combination with narrow-band, red-light illumination for nonhyperkeratotic, nonpigmented actinic keratoses. (medscape.com)
- Patients excrete increased levels of porphyrin precursors, 5-AMINOLEVULINATE and COPROPORPHYRINS. (curehunter.com)
- Decreased negative feedback from heme contributes to the elevated "baseline" ALA synthetase activity which is The manifestions of the disease are thought to be due to increased ALA synthetase activity, increased porphyrin accumulation in the tissues, or decreased heme production. (medpdfarticles.com)
- Auf www.antikoerper-online.de finden Sie aktuell 79 Aminolevulinate, delta-, Synthase 1 (ALAS1) Antikörper von 20 unterschiedlichen Herstellern. (antikoerper-online.de)
- Alternative splicing of human ALAS1 generates two mRNAs with different 5'-UTRs: a major one, where exon 1B is omitted, and a minor form containing exon 1B. (antikoerper-online.de)
- A combined approach, comprising PCR screening and genome mining, was used to unravel the diversity and phylogeny of genes encoding 5-aminolevulinic acid synthases (ALASs, hemA gene products) in streptomycetes-related strains. (frontiersin.org)
- We consider the presence of this gene triad to be a specific genetic marker of the C 5 N unit biosynthetic pathway that "tags" producers of C 5 N-containing metabolites among others. (frontiersin.org)
- The principal aim of our work was to show the potential of the hemA -targeted genetic screening in identification of novel putative biosynthetic gene clusters encoding C 5 N-containing metabolites. (frontiersin.org)
- 1 In addition to these well-established functions as a prosthetic group, recent reports have revealed that heme regulates several transcription factors, including Bach1, 2 ⇓ ⇓ - 5 NPAS2, 6 and REV-ERBs, 7 and modulates gene expression as an inter- and intracellular signaling molecule in mammals. (bloodjournal.org)
- The expression of calcitonin gene-related peptide (CGRP) in the spinal dorsal horn (L2-3 and L4-5) was examined to evaluate central sensitization. (bvsalud.org)
- Unlike "classical" primary metabolism ALAS, the C 5 N unit-forming c yclizing ALAS (cALAS) catalyses intramolecular cyclization of nascent 5-aminolevulinate. (frontiersin.org)
- In actinomycetes, these genes were believed to be directly connected with the production of secondary metabolites carrying the C 5 N unit, 2-amino-3-hydroxycyclopent-2-enone, with biological activities making them attractive for future use in medicine and agriculture. (frontiersin.org)
- First, we identified the genes that were differentially expressed in GBMs (3 datasets) compared to non-GBM brain tissues (5 datasets), or were associated with survival differences. (beds.ac.uk)
- Some α-Proteobacteria, fungi, and animals form ALA through condensation of glycine and succinyl-CoA by hemA -encoded aminolevulinate synthase in so called C4 or Shemin pathway. (frontiersin.org)
- The average adult ingests 3 to 5 grams of glycine daily. (selfdecode.com)
- 5-aminolevulinate from glycine: step 1/1. (abcam.com)
- A glutamine synthetase inhibitor, MSX, stimulated ammonium excretion and H 2 -production and pulses of MSX rather than a single dose favoured both the processes. (go.jp)
- A transcription factor that controls the expression of variety of proteins including CYTOCHROME C and 5-AMINOLEVULINATE SYNTHETASE. (umassmed.edu)
- 1 The binding of EPO to its specific receptor on the cell surface induces tyrosine phosphorylation and the activation of several proteins, including Janus kinase 2 (JAK2), 2 signal transducer and activator of transcription 5 (Stat5), 3-5 mitogen-associated protein kinases, 6 and phospholipase C-γ1. (ashpublications.org)
- 5-aminolevulinate (ALA) is a key precursor of a huge family of essential tetrapyrrole compounds. (frontiersin.org)
- The biosynthetic steps from the earliest universal precursor, 5-aminolevulinic acid (ALA), to protoporphyrin IX-based hemes constitute the major, common portion of the pathway, and other steps leading to specific groups of products can be considered branches off the main axis. (asmscience.org)
- An SJ, Park SK, Hwang IK, et al (2004) Vigabatrin inhibits pyridoxine-5′-phosphate oxidase, not pyridoxal kinase in the hippocampus of seizure prone gerbils. (springer.com)
- From early studies of kindreds with EPP, most investigators concluded that the disease displayed autosomal dominant inheritance with low penetrance and an increased propensity to develop chronic liver disease, 5 though autosomal recessive forms of EPP have also been described. (porphyriafoundation.org)
- It interferes with DNA synthesis by blocking methylation of deoxyuridylic acid and inhibiting thymidylate synthetase and, subsequently, cell proliferation. (medscape.com)
- Salonpää P, Iscan M, Pasanen M, Arvela P, Pelkonen O, Raunio H. Cerium-induced strain-dependent increase in Cyp2a-4/5 (cytochrome P4502a-4/5) expression in the liver and kidneys of inbred mice. (labome.org)
- The delta-aminolevulinic acid synthetase activity and the effect of exogenous delta-aminolevulinate on the synthesis of cytochrome c in the thoracic muscles of the tobacco horn worm during adult development. (pianolarge.ml)
- The basal activity of ALA synthetase is substantially lower than that of subsequent enzymes in the synthetic pathway, and therefore changes in ALA synthetase activity are rate limiting, controlling the rate of heme synthesis. (medpdfarticles.com)
- Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells. (antikoerper-online.de)
- 2.75%travasol Amino Acid InJ.W.eleC.W.5%dex. (drugbank.ca)
- Both 5-aminolevulinic acid dehydratase and porphobilinogen deaminase activities were inhibited by these metals. (bvsalud.org)
- Aoki Y, Muranaka S, Nakabayashi K, Ueda Y (1979) delta-Aminolevulinic acid synthetase in erythroblasts of patients with pyridoxine-responsive anemia. (springer.com)
- Topical 5% imiquimod is approved by the US Food and Drug Administration (FDA) for the treatment of nonfacial superficial BCCs that are less than 2 cm in diameter. (medscape.com)
- C) It contains a 3′ to 5′ exonuclease activity. (foodelphi.com)
- Total 14 patients had acute myeloid leukemia, 10 had acute lymphoblastic leukemia, 5 had myelodysplastic syndrome, 3 had non-Hodgkin's lymphoma, and 2 had aplastic anemia. (bvsalud.org)
- Differential effects of metalloporphyrins on messenger RNA levels of delta-aminolevulinate synthase and heme oxygenase. (umassmed.edu)
- D) A total of 4 δ-aminolevulinate molecules are used to synthesize 1 heme molecule. (foodelphi.com)
- These data indicate that the Cyp2a-4/5 complex is regulated in a different way in DBA/2 and C57BL/6 mice and that some association exists between the development of liver damage and COH induction. (labome.org)
- The structure consists of a γ-rubromycin core possessing a C 5 N unit as an amide substituent of the carboxyl functionality. (biomedcentral.com)
- GSS (glutathione synthetase) was not differentially expressed, but higher levels were linked to poor progression free survival. (beds.ac.uk)
- Groups of 2-5 cats ingesting fruit juice containing 730-2000 ppm (0.073-0.2%) tin (3.65-20 mg tin/kg bw) did not excrete any tin in their urine (Benoy et al. (inchem.org)
- The most common chemotherapeutic agent used in superficial basal cell carcinoma is topical 5-fluorouracil. (medscape.com)
- Compounds did not present thiol oxidase-like activity and effect on the δ-aminolevulinate dehydratase. (bvsalud.org)