Hemoglobins: The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.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.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.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Hemoglobin A: Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.Hemoglobins, Abnormal: Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains.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.Fetal Hemoglobin: The major component of hemoglobin in the fetus. This HEMOGLOBIN has two alpha and two gamma polypeptide subunits in comparison to normal adult hemoglobin, which has two alpha and two beta polypeptide subunits. Fetal hemoglobin concentrations can be elevated (usually above 0.5%) in children and adults affected by LEUKEMIA and several types of ANEMIA.Hemoglobin, Sickle: An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia.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.Carbon-Carbon Double Bond Isomerases: Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Amidine-Lyases: These enzymes catalyze the elimination of ammonia from amidines with the formation of a double bond. EC 4.3.2.Steroids: A group of polycyclic compounds closely related biochemically to TERPENES. They include cholesterol, numerous hormones, precursors of certain vitamins, bile acids, alcohols (STEROLS), and certain natural drugs and poisons. Steroids have a common nucleus, a fused, reduced 17-carbon atom ring system, cyclopentanoperhydrophenanthrene. Most steroids also have two methyl groups and an aliphatic side-chain attached to the nucleus. (From Hawley's Condensed Chemical Dictionary, 11th ed)Ketosteroids: Steroid derivatives formed by oxidation of a methyl group on the side chain or a methylene group in the ring skeleton to form a ketone.Bile Acids and Salts: Steroid acids and salts. The primary bile acids are derived from cholesterol in the liver and usually conjugated with glycine or taurine. The secondary bile acids are further modified by bacteria in the intestine. They play an important role in the digestion and absorption of fat. They have also been used pharmacologically, especially in the treatment of gallstones.Dronabinol: A psychoactive compound extracted from the resin of Cannabis sativa (marihuana, hashish). The isomer delta-9-tetrahydrocannabinol (THC) is considered the most active form, producing characteristic mood and perceptual changes associated with this compound.Pregnanes: Saturated derivatives of the steroid pregnane. The 5-beta series includes PROGESTERONE and related hormones; the 5-alpha series includes forms generally excreted in the urine.17-alpha-Hydroxyprogesterone: A metabolite of PROGESTERONE with a hydroxyl group at the 17-alpha position. It serves as an intermediate in the biosynthesis of HYDROCORTISONE and GONADAL STEROID HORMONES.Immunoglobulin Class Switching: Gene rearrangement of the B-lymphocyte which results in a substitution in the type of heavy-chain constant region that is expressed. This allows the effector response to change while the antigen binding specificity (variable region) remains the same. The majority of class switching occurs by a DNA recombination event but it also can take place at the level of RNA processing.Heme Oxygenase-1: A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Plasma Cells: Specialized forms of antibody-producing B-LYMPHOCYTES. They synthesize and secrete immunoglobulin. They are found only in lymphoid organs and at sites of immune responses and normally do not circulate in the blood or lymph. (Rosen et al., Dictionary of Immunology, 1989, p169 & Abbas et al., Cellular and Molecular Immunology, 2d ed, p20)Heme Oxygenase (Decyclizing): A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC 1.14.99.3.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.B-Lymphocytes: Lymphoid cells concerned with humoral immunity. They are short-lived cells resembling bursa-derived lymphocytes of birds in their production of immunoglobulin upon appropriate stimulation.Toxicodendron: A genus (formerly part of Rhus genus) of shrubs, vines, or trees that yields a highly allergenic oleoresin which causes a severe contact dermatitis (DERMATITIS, TOXICODENDRON). The most toxic species are Toxicodendron vernix (poison sumac), T. diversilobum (poison oak), and T. radicans (poison ivy). T. vernicifera yields a useful varnish from which certain enzymes (laccases) are obtained.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
(1/369) delta-Aminolevulinate synthetases in the liver cytosol fraction and mitochondria of mice treated with allylisopropylacetamide and 3,5-dicarbethoxyl-1,4-dihydrocollidine.

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)

(2/369) 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.

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)

(3/369) Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania).

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)

(4/369) Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release.

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)

(5/369) Phylogenetic analysis of the 5-aminolevulinate synthase gene.

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)

(6/369) Respiratory uncoupling induces delta-aminolevulinate synthase expression through a nuclear respiratory factor-1-dependent mechanism in HeLa cells.

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)

(7/369) Characterization of the rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes, HemA and HemT, isolated from recombinant Escherichia coli.

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)

(8/369) A photosensitising adenovirus for photodynamic therapy.

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)

*  List of MeSH codes (D08)
... 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 --- ...
*  Ferrochelatase
... 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- ...
*  SUCLA2
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- ...
*  Chromosome 9 (human)
... 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 ...
*  ALAS2
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) ...
*  Chromosome 3 (human)
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: ...
*  Porphyria cutanea tarda
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.; ...
*  Actinic keratosis
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 ...
*  Amino acid synthesis
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 ...
Erythroid 5-aminolevulinate synthetase deficiency | Article about Erythroid 5-aminolevulinate synthetase deficiency by The Free...  Erythroid 5-aminolevulinate synthetase deficiency | Article about Erythroid 5-aminolevulinate synthetase deficiency by The Free...
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. [ ...
more infohttps://encyclopedia2.thefreedictionary.com/Erythroid+5-aminolevulinate+synthetase+deficiency
Differential effects of metalloporphyrins on messenger RNA levels of d by Edward Earl Cable, Joyce A. Pepe et al.  "Differential effects of metalloporphyrins on messenger RNA levels of d" by Edward Earl Cable, Joyce A. Pepe et al.
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; ...
more infohttps://escholarship.umassmed.edu/gsbs_sp/164/
Effects of mifepristone (RU-486) on heme metabolism and cytochromes P- by Edward Earl Cable, Joyce A. Pepe et al.  "Effects of mifepristone (RU-486) on heme metabolism and cytochromes P-" by Edward Earl Cable, Joyce A. Pepe et al.
5-Aminolevulinate Synthetase; Animals; Cells, Cultured; Chick Embryo; Cytochrome P-450 Enzyme System; Deferoxamine; Heme; Liver ...
more infohttps://escholarship.umassmed.edu/gsbs_sp/163/
List of MeSH codes (D08) - Wikipedia  List of MeSH codes (D08) - Wikipedia
... 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 --- ...
more infohttps://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
NAVER 학술정보 >...  NAVER 학술정보 >...
Regulation of haem biosynthesis in normoblastic erythropoiesis: role of 5-aminolaevulinic acid synthase and ferrochelatase.. ... 5-Aminolevulinate Synthetase, metabolism, Bone Marrow, enzymology, Cell Differentiation, Erythroblasts, Erythropoiesis, ...
more infohttps://academic.naver.com/search.naver?field=3&query=Biochimica+et+Biophysica+Acta+1201%EA%B6%8C+1%ED%98%B8
Hemoglobin | definition of Hemoglobin by Medical …  Hemoglobin | definition of Hemoglobin by Medical …
Research Proceedings 5: 29, 1957.3. Shemin, D., Abramsky, T., and Russell, C. S.: The synthesis of protoporphyrinfrom delta- ... ALAS2 is a specific erythroid isoform of 5-aminolevulinate synthetase (ALAS) and is essential for synthesis of hemoglobin in ...
more infohttp://spaceshipsla.com/protoporphyrin-hemoglobin-synthesis.html
Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1alpha.  - PubMed - NCBI  Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1alpha. - PubMed - NCBI
We show that the rate-limiting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/16122419?dopt=Abstract
Experts and Doctors on humans in Sendai, Miyagi, Japan  Experts and Doctors on humans in Sendai, Miyagi, Japan
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 ...
more infohttp://www.labome.org/locale/japan/miyagi/experts-and-doctors-on-humans-in-sendai--miyagi--japan-35209.html
Erythrogenic | definition of erythrogenic by Medical dictionary  Erythrogenic | definition of erythrogenic by Medical dictionary
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?
more infohttp://medical-dictionary.thefreedictionary.com/erythrogenic
Erythrogenesis imperfecta | definition of erythrogenesis imperfecta by Medical dictionary  Erythrogenesis imperfecta | definition of erythrogenesis imperfecta by Medical dictionary
Looking for online definition of erythrogenesis imperfecta in the Medical Dictionary? erythrogenesis imperfecta explanation free. What is erythrogenesis imperfecta? Meaning of erythrogenesis imperfecta medical term. What does erythrogenesis imperfecta mean?
more infohttp://medical-dictionary.thefreedictionary.com/erythrogenesis+imperfecta
topic:Hydrogen Peroxide - pharmacology found 13 records • Arctic Health  topic:"Hydrogen Peroxide - pharmacology" found 13 records • Arctic Health
Experiments with inhibitors of gamma-glutamylcysteine synthetase and catalase supported our conclusion that mechanisms ... 5-Aminolevulinate Synthetase - metabolism Animals Cycloheximide - pharmacology Enzyme Induction - drug effects Glutathione - ... Inoculated whole melons stored at 5 degrees C for up to 7 days were washed with water, 2.5% and 5% hydrogen peroxide at day 0 ... Lettuce was artificially inoculated by dipping it in a suspension of the studied pathogens at 10(8), 10(7) or 10(5) cfu ml(-1 ...
more infohttps://arctichealth.org/en/list?q=topic%3A%22Hydrogen+Peroxide+-+pharmacology%22&p=1&ps=&sort=title_sort+asc
anti-ALAS1 Primary Antibodies  anti-ALAS1 Primary Antibodies
... 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 ...
more infohttps://www.antikoerper-online.de/regulation-of-lipid-metabolism-by-pparalpha-pathway-66/alas1-antibody-1846/
KEGG BRITE: KEGG Orthology (KO) - Mus musculus (mouse)  KEGG BRITE: KEGG Orthology (KO) - Mus musculus (mouse)
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- ...
more infohttp://www.genome.jp/kegg-bin/get_htext?mmu00001+394435
Ferrochelatase - Wikipedia  Ferrochelatase - Wikipedia
... 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- ...
more infohttps://en.wikipedia.org/wiki/Ferrochelatase
Search Articles | University of Toronto Libraries  Search Articles | University of Toronto Libraries
5,10,15,20-tetrakis(1-methylpyridinium-4-yl)-porphyrin tetra-iodide (TMPyP), a potent water-soluble photosensitizer (PS) used ...
more infohttps://query.library.utoronto.ca/index.php/search/q?kw=SubjectTerms:Porphyrins%20-%20administration%20&%20dosage&page=2
Draft genome sequence of Streptomyces hyaluromycini MB-PO13T, a hyaluromycin producer | Standards in Genomic Sciences | Full...  Draft genome sequence of Streptomyces hyaluromycini MB-PO13T, a hyaluromycin producer | Standards in Genomic Sciences | Full...
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 ...
more infohttps://standardsingenomics.biomedcentral.com/articles/10.1186/s40793-017-0286-7
Zeitschrift für Naturforschung C  Zeitschrift für Naturforschung C
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 ...
more infohttps://www.degruyter.com/view/j/znc.1981.36.issue-1-2/issue-files/znc.1981.36.issue-1-2.xml
The American Porphyria Foundation             | Genetic and Rare Diseases Information Center (GARD) - an NCATS Program  The American Porphyria Foundation | Genetic and Rare Diseases Information Center (GARD) - an NCATS Program
Aminolevulinate dehydratase deficiency porphyria Synonyms: 5-Aminolevulinic acid dehydratase deficiency porphyria, ALA ... Synonyms: Erythrohepatic protoporphyria, EPP, Heme synthetase deficiency, Ferrochelatase deficiency Hepatoerythropoietic ...
more infohttps://rarediseases.info.nih.gov/organizations/69
The rhizome of Reclinomonas americana, Homo sapiens, Pediculus humanus and Saccharomyces cerevisiae mitochondria | Biology...  The rhizome of Reclinomonas americana, Homo sapiens, Pediculus humanus and Saccharomyces cerevisiae mitochondria | Biology...
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 ...
more infohttps://biologydirect.biomedcentral.com/articles/10.1186/1745-6150-6-55
Erythroid cells | Article about erythroid cells by The Free Dictionary  Erythroid cells | Article about erythroid cells by The Free Dictionary
Although the rate-limiting step in non-erythroid cells is the delta-aminolevulinate formation, in erythroid cells, the rate- ... to ATP by the enzyme ATP synthetase. See Mitochondria ... 5. a small religious house dependent upon a larger one 6. a ... Without carefully designed support over the whole rear face the mirror of the 5-meter Hale telescope would sag by 0.0625 mm, ... 5. In electrical systems, a single raceway of a cellular or underfloor duct system. ...
more infohttp://encyclopedia2.thefreedictionary.com/erythroid+cells
  • 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)
  • DL significantly increased only the EROD and NADPH-cytochrome c reductase activities and shortened HB sleeping time to a lesser extent, suggesting a weaker enzyme-inducing effect as compared to NF and V. The three drugs increased the delta-aminolevulinic acid (ALA) synthetase activity and decreased heme oxygenase (HO) activity. (nih.gov)
  • Decreased heme production de-represses ALA synthetase and further increases ALA levels. (medscape.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)