Coproporphyrinogen Oxidase: An enzyme that catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX by the conversion of two propionate groups to two vinyl groups. It is the sixth enzyme in the 8-enzyme biosynthetic pathway of HEME, and is encoded by CPO gene. Mutations of CPO gene result in HEREDITARY COPROPORPHYRIA.Coproporphyrinogens: Porphyrinogens which are intermediates in the heme biosynthesis. They have four methyl and four propionic acid side chains attached to the pyrrole rings. Coproporphyrinogens I and III are formed in the presence of uroporphyrinogen decarboxylase from the corresponding uroporphyrinogen. They can yield coproporphyrins by autooxidation or protoporphyrin by oxidative decarboxylation.Porphyrinogens: Colorless reduced precursors of porphyrins in which the pyrrole rings are linked by methylene (-CH2-) bridges.Coproporphyria, Hereditary: An autosomal dominant porphyria that is due to a deficiency of COPROPORPHYRINOGEN OXIDASE in the LIVER, the sixth enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features include both neurological symptoms and cutaneous lesions. Patients excrete increased levels of porphyrin precursors, 5-AMINOLEVULINATE and COPROPORPHYRINS.Protoporphyrinogen Oxidase: A membrane-bound flavoenzyme that catalyzes the oxygen-dependent aromatization of protoporphyrinogen IX (Protogen) to protoporphyrin IX (Proto IX). It is the last enzyme of the common branch of the HEME and CHLOROPHYLL pathways in plants, and is the molecular target of diphenyl ether-type herbicides. VARIEGATE PORPHYRIA is an autosomal dominant disorder associated with deficiency of protoporphyrinogen oxidase.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.Coproporphyrins: Porphyrins with four methyl and four propionic acid side chains attached to the pyrrole rings. Elevated levels of Coproporphyrin III in the urine and feces are major findings in patients with HEREDITARY COPROPORPHYRIA.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.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Decarboxylation: The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.Porphyrias: A diverse group of metabolic diseases characterized by errors in the biosynthetic pathway of HEME in the LIVER, the BONE MARROW, or both. They are classified by the deficiency of specific enzymes, the tissue site of enzyme defect, or the clinical features that include neurological (acute) or cutaneous (skin lesions). Porphyrias can be hereditary or acquired as a result of toxicity to the hepatic or erythropoietic marrow tissues.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.Uroporphyrinogen Decarboxylase: An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA.Uroporphyrinogens: Porphyrinogens which are intermediates in heme biosynthesis. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation.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.NADPH Oxidase: A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.Porphyrias, Hepatic: A group of metabolic diseases due to deficiency of one of a number of LIVER enzymes in the biosynthetic pathway of HEME. They are characterized by the accumulation and increased excretion of PORPHYRINS or its precursors. Clinical features include neurological symptoms (PORPHYRIA, ACUTE INTERMITTENT), cutaneous lesions due to photosensitivity (PORPHYRIA CUTANEA TARDA), or both (HEREDITARY COPROPORPHYRIA). Hepatic porphyrias can be hereditary or acquired as a result of toxicity to the hepatic tissues.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.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.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Electron Transport Complex IV: A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.Cyanobacteria: A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.Plasmodium falciparum: A species of protozoa that is the causal agent of falciparum malaria (MALARIA, FALCIPARUM). It is most prevalent in the tropics and subtropics.ChalconeMalaria, Falciparum: Malaria caused by PLASMODIUM FALCIPARUM. This is the severest form of malaria and is associated with the highest levels of parasites in the blood. This disease is characterized by irregularly recurring febrile paroxysms that in extreme cases occur with acute cerebral, renal, or gastrointestinal manifestations.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Chromosome Mapping: Any method used for determining the location of and relative distances between genes on a chromosome.Chromosomes: In a prokaryotic cell or in the nucleus of a eukaryotic cell, a structure consisting of or containing DNA which carries the genetic information essential to the cell. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Molecular Sequence Annotation: The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.Chromosome Banding: Staining of bands, or chromosome segments, allowing the precise identification of individual chromosomes or parts of chromosomes. Applications include the determination of chromosome rearrangements in malformation syndromes and cancer, the chemistry of chromosome segments, chromosome changes during evolution, and, in conjunction with cell hybridization studies, chromosome mapping.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Diketopiperazines: Piperazines with two keto oxygens.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Ferrichrome: A cyclic peptide consisting of three residues of delta-N-hydroxy-delta-N-acetylornithine. It acts as an iron transport agent in Ustilago sphaerogena.Hemeproteins: Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)Electrons: Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Gases: The vapor state of matter; nonelastic fluids in which the molecules are in free movement and their mean positions far apart. Gases tend to expand indefinitely, to diffuse and mix readily with other gases, to have definite relations of volume, temperature, and pressure, and to condense or liquefy at low temperatures or under sufficient pressure. (Grant & Hackh's Chemical Dictionary, 5th ed)Porphyria, Erythropoietic: An autosomal recessive porphyria that is due to a deficiency of UROPORPHYRINOGEN III SYNTHASE in the BONE MARROW; also known as congenital erythropoietic porphyria. This disease is characterized by SPLENOMEGALY; ANEMIA; photosensitivity; cutaneous lesions; accumulation of hydroxymethylbilane; and increased excretion of UROPORPHYRINS and COPROPORPHYRINS.Levulinic Acids: Keto acids that are derivatives of 4-oxopentanoic acids (levulinic acid).Porphyria, Acute Intermittent: An autosomal dominant porphyria that is due to a deficiency of HYDROXYMETHYLBILANE SYNTHASE in the LIVER, the third enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features are recurrent and life-threatening neurologic disturbances, ABDOMINAL PAIN, and elevated level of AMINOLEVULINIC ACID and PORPHOBILINOGEN in the urine.Porphyria, Variegate: An autosomal dominant porphyria that is due to a deficiency of protoporphyrinogen oxidase (EC 1.3.3.4) in the LIVER, the seventh enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features include both neurological symptoms and cutaneous lesions. Patients excrete increased levels of porphyrin precursors, COPROPORPHYRINS and protoporphyrinogen.Uroporphyrinogen III Synthetase: An enzyme that catalyzes the cyclization of hydroxymethylbilane to yield UROPORPHYRINOGEN III and water. It is the fourth enzyme in the 8-enzyme biosynthetic pathway of HEME, and is encoded by UROS gene. Mutations of UROS gene result in CONGENITAL ERYTHROPOIETIC PORPHYRIA.Information Centers: Facilities for collecting and organizing information. They may be specialized by subject field, type of source material, persons served, location, or type of services.Pseudomonas aeruginosa: A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Pseudomonas Infections: Infections with bacteria of the genus PSEUDOMONAS.Bacterial Proteins: Proteins found in any species of bacterium.Pyocyanine: Antibiotic pigment produced by Pseudomonas aeruginosa.Pseudomonas fluorescens: A species of nonpathogenic fluorescent bacteria found in feces, sewage, soil, and water, and which liquefy gelatin.

Induction of coproporphyrinogen oxidase in Chlamydomonas chloroplasts occurs via transcriptional regulation of Cpx1 mediated by copper response elements and increased translation from a copper deficiency-specific form of the transcript. (1/92)

Coproporphyrinogen III oxidase, encoded by a single nuclear gene in Chlamydomonas reinhardtii, produces three distinct transcripts. One of these transcripts is greatly induced in copper-deficient cells by transcriptional activation, whereas the other forms are copper-insensitive. The induced form of the transcript was expressed coordinately with the cytochrome c6-encoding (Cyc6) gene, which is known to be transcriptionally regulated in copper-deficient cells. The sequence GTAC, which forms the core of a copper response element associated with the Cyc6 gene, is also essential for induction of the Cpx1 gene, suggesting that both are targets of the same signal transduction pathway. The constitutive and induced Cpx1 transcripts have the same half-lives in vivo, and all encode the same polypeptide with a chloroplast-targeting transit sequence, but the shortest one representing the induced form is a 2-4-fold better template for translation than are either of the constitutive forms. The enzyme remains localized to a soluble compartment in the chloroplast even in induced cells, and its abundance is not affected when the tetrapyrrole pathway is manipulated either genetically or by gabaculine treatment.  (+info)

Transcriptional control of Bacillus subtilis hemN and hemZ. (2/92)

Previous characterization of Bacillus subtilis hemN, encoding a protein involved in oxygen-independent coproporphyrinogen III decarboxylation, indicated the presence of a second hemN-like gene (B. Hippler, G. Homuth, T. Hoffmann, C. Hungerer, W. Schumann, and D. Jahn, J. Bacteriol. 179:7181-7185, 1997). The corresponding hemZ gene was found to be split into the two potential open reading frames yhaV and yhaW by a sequencing error of the genome sequencing project. The hemZ gene, encoding a 501-amino-acid protein with a calculated molecular mass of 57,533 Da, complemented a Salmonella typhimurium hemF hemN double mutant under aerobic and anaerobic growth conditions. A B. subtilis hemZ mutant accumulated coproporphyrinogen III under anaerobic growth conditions. A hemN hemZ double mutant exhibited normal aerobic and anaerobic growth, indicating the presence of a third alternative oxygen-independent enzymatic system for coproporphyrinogen III oxidation. The hemY gene, encoding oxygen-dependent protoporphyrinogen IX oxidase with coproporphyrinogen III oxidase side activity, did not significantly contribute to this newly identified system. Growth behavior of hemY mutants revealed the presence of an oxygen-independent protoporphyrinogen IX oxidase in B. subtilis. A monocistronic hemZ mRNA, starting 31 bp upstream of the translational start codon, was detected. Reporter gene fusions of hemZ and hemN demonstrated a fivefold anaerobic induction of both genes under nitrate ammonifying growth conditions. No anaerobic induction was observed for fermentatively growing B. subtilis. The B. subtilis redox regulatory systems encoded by resDE, fnr, and ywiD were indispensable for the observed transcriptional induction. A redox regulation cascade proceeding from an unknown sensor via resDE, through fnr and ywiD to hemN/hemZ, is suggested for the observed coregulation of heme biosynthesis and the anaerobic respiratory energy metabolism. Finally, only hemZ was found to be fivefold induced by the presence of H(2)O(2), indicating further coregulation of heme biosynthesis with the formation of the tetrapyrrole enzyme catalase.  (+info)

Coordinate copper- and oxygen-responsive Cyc6 and Cpx1 expression in Chlamydomonas is mediated by the same element. (3/92)

Chlamydomonas reinhardtii activates the transcription of the Cyc6 and the Cpx1 genes (encoding cytochrome c(6) and coprogen oxidase) in response to copper deficiency. Mutational analysis of promoter regions of the Cyc6 and Cpx1 genes revealed a four nucleotide sequence, GTAC, which was absolutely essential for copper responsiveness. The Cyc6 promoter contains two copper response elements, each with a functionally important GTAC sequence, whereas the Cpx1 promoter contains only one. This may contribute to the stronger and more tightly regulated expression of the Cyc6 gene. Mutation or deletion of sequences flanking the GTACs implicates additional nucleotides contributing to copper-responsive expression, but none are absolutely essential. Metal ion selectivity of Cpx1 expression is identical to that described previously for Cyc6 and is restricted to the copper deficiency-induced Cpx1 transcript. The Cyc6 and Cpx1 genes are also induced by oxygen deficiency. Reporter gene constructs indicate that the induction occurs at the level of transcription and requires the same GTAC sequence that is critical for copper responsiveness. We suggest that components of the copper-responsive signal transduction pathway are used for some of the changes in gene expression in hypoxic cells.  (+info)

Alcohol and porphyrin metabolism. (4/92)

Alcohol is a porphyrinogenic agent which may cause disturbances in porphyrin metabolism in healthy persons as well as biochemical and clinical manifestations of acute and chronic hepatic porphyrias. After excessive consumption of alcohol, a temporary, clinically asymptomatic secondary hepatic coproporphyrinuria is observable, which can become persistent in cases of alcohol-induced liver damage. Nowadays, the alcohol-liver-porphyrinuria syndrome is the first to be mentioned in secondary hepatic disturbances of porphyrin metabolism. Acute hepatic porphyrias (acute intermittent porphyria, variegate porphyria and hereditary coproporphyria) are considered to be molecular regulatory diseases, in contrast to non-acute, chronic hepatic porphyria, clinically appearing as porphyria cutanea tarda (PCT). Porphyrins do not accumulate in the liver in acute porphyrias, whereas in chronic hepatic porphyrias they do. Thus, chronic hepatic porphyria is a porphyrin-accumulation disease, whereas acute hepatic porphyrias are haem-pathway-dysregulation diseases, characterized in general by induction of delta-aminolevulinic acid synthase in the liver and excessive stimulation of the pathway without storage of porphyrins in the liver. The clinical expression of acute hepatic porphyrias can be triggered by alcohol, because alcohol augments the inducibility of delta-aminolevulinic acid synthase. In chronic hepatic porphyrias, however, which are already associated with liver damage, alcohol potentiates the disturbance of the decarboxylation of uro- and heptacarboxyporphyrinogen, which is followed by a hepatic accumulation of uro- and heptacarboxyporphyrin and their sometimes extreme urinary excretion. Especially in persons with a genetic deficiency of uroporphyrinogen decarboxylase, but also in patients with the so-called sporadic variety of PCT, alcohol is able to transform an asymptomatic coproporphyrinuria into PCT. Alcohol has many biochemical and clinical effects on porphyrin and haem synthesis both in humans and laboratory animals. Ethanol suppresses the activity of porphobilinogen synthase (synonym: delta-aminolevulinic acid dehydratase), uroporphyrinogen decarboxylase, coproporphyrinogen oxidase and ferrochelatase, whereas it induces the first and rate-limiting enzyme in the pathway, delta-aminolevulinic acid synthase and also porphobilinogen deaminase. Therefore, teetotalism is a therapeutically and prophylactically important measure in all types of hepatic porphyrias.  (+info)

Interacting regulatory circuits involved in orderly control of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. (5/92)

FnrL, the homolog of the global anaerobic regulator Fnr, is required for the induction of the photosynthetic apparatus in Rhodobacter sphaeroides 2.4.1. Thus, the precise role of FnrL in photosynthesis (PS) gene expression and its interaction(s) with other regulators of PS gene expression are of considerable importance to our understanding of the regulatory circuitry governing spectral complex formation. Using a CcoP and FnrL double mutant strain, we obtained results which suggested that FnrL is not involved in the transduction of the inhibitory signal, by which PS gene expression is "silenced," emanating from the cbb(3) oxidase encoded by the ccoNOQP operon under aerobic conditions. The dominant effect of the ccoP mutation in the FnrL mutant strain with respect to spectral complex formation under aerobic conditions and restoration of a PS-positive phenotype suggested that inactivation of the cbb(3) oxidase to some extent bypasses the requirement for FnrL in the formation of spectral complexes. Additional analyses revealed that anaerobic induction of the bchE, hemN, and hemZ genes, which are involved in the tetrapyrrole biosynthetic pathways, requires FnrL. Thus, FnrL appears to be involved at multiple loci involved in the regulation of PS gene expression. Additionally, bchE was also shown to be regulated by the PrrBA two-component system, in conjunction with hemN and hemZ. These and other results to be discussed permit us to more accurately describe the role of FnrL as well as the interactions between the FnrL, PrrBA, and other regulatory circuits in the regulation of PS gene expression.  (+info)

The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. (6/92)

Chlamydomonas reinhardtii adapts to copper deficiency by degrading apoplastocyanin and inducing Cyc6 and Cpx1 encoding cytochrome c(6) and coproporphyrinogen oxidase, respectively. To identify other components in this pathway, colonies resulting from insertional mutagenesis were screened for copper- conditional phenotypes. Twelve crd (copper response defect) strains were identified. In copper-deficient conditions, the crd strains fail to accumulate photosystem I and light-harvesting complex I, and they contain reduced amounts of light-harvesting complex II. Cyc6, Cpx1 expression and plastocyanin accumulation remain copper responsive. The crd phenotype is rescued by a similar amount of copper as is required for repression of Cyc6 and Cpx1 and for maintenance of plastocyanin at its usual stoichiometry, suggesting that the affected gene is a target of the same signal transduction pathway. The crd strains represent alleles at a single locus, CRD1, which encodes a 47 kDa, hydrophilic protein with a consensus carboxylate-bridged di-iron binding site. Crd1 homologs are present in the genomes of photosynthetic organisms. In Chlamydomonas, Crd1 expression is activated in copper- or oxygen-deficient cells, and Crd1 function is required for adaptation to these conditions.  (+info)

Regulation of the expression of human ferrochelatase by intracellular iron levels. (7/92)

Mammalian ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of a ferrous ion into protoporphyrin and contains a labile [2Fe-2S] cluster center at the C-terminus. To clarify the roles of the iron-sulfur cluster in the expression of mammalian ferrochelatase, enzyme activity in human erythroleukemia K562 cells under iron-depleted conditions was examined. Treatment of cells with an iron chelator, desferrioxamine, resulted in a decrease in enzyme activity, in a dose- and time-dependent manner. Heme content decreased during desferrioxamine treatment of the cells. Addition of ferric ion-nitrilotriacetate [Fe (III)NTA] to desferrioxamine-containing cultures led to restoration of the reduction in the enzyme activity. While RNA blots showed that the amount of ferrochelatase mRNA remained unchanged during these treatments, the amount of ferrochelatase decreased with a concomitant decrease in enzyme activity. When full-length human ferrochelatase was expressed in Cos7 cells, the activity was found mainly in the mitochondria and was decreased markedly by treatment with desferrioxamine. The activity in Cos7 cells expressing human ferrochelatase in cytoplasm decreased with desferrioxamine, but to a lesser extent. When Escherichia coli ferrochelatase, which lacks the iron-sulfur cluster, was expressed in Cos7 cells, the activity did not change following any treatment. Conversely, the addition of Fe (III)NTA to the culture of K562 and Cos7 cells led to an increase in ferrochelatase activity. These results indicate that the expression of mammalian ferrochelatase is regulated by intracellular iron levels, via the iron-sulfur cluster center at the C-terminus, and this contributes to the regulation of the biosynthesis of heme at the terminal step.  (+info)

One of two hemN genes in Bradyrhizobium japonicum is functional during anaerobic growth and in symbiosis. (8/92)

Previously, we screened the symbiotic gene region of the Bradyrhizobium japonicum chromosome for new NifA-dependent genes by competitive DNA-RNA hybridization (A. Nienaber, A. Huber, M. Gottfert, H. Hennecke, and H. M. Fischer, J. Bacteriol. 182:1472-1480, 2000). Here we report more details on one of the genes identified, a hemN-like gene (now called hemN(1)) whose product exhibits significant similarity to oxygen-independent coproporphyrinogen III dehydrogenases involved in heme biosynthesis in facultatively anaerobic bacteria. In the course of these studies, we discovered that B. japonicum possesses a second hemN-like gene (hemN(2)), which was then cloned by using hemN(1) as a probe. The hemN(2) gene maps outside of the symbiotic gene region; it is located 1.5 kb upstream of nirK, the gene for a Cu-containing nitrite reductase. The two deduced HemN proteins are similar in size (445 and 450 amino acids for HemN(1) and HemN(2), respectively) and share 53% identical (68% similar) amino acids. Expression of both hemN genes was monitored with the help of chromosomally integrated translational lacZ fusions. No significant expression of either gene was detected in aerobically grown cells, whereas both genes were strongly induced (> or = 20-fold) under microaerobic or anaerobic conditions. Induction was in both cases dependent on the transcriptional activator protein FixK(2). In addition, maximal anaerobic hemN(1) expression was partially dependent on NifA, which explains why this gene had been identified by the competitive DNA-RNA hybridization approach. Strains were constructed carrying null mutations either in individual hemN genes or simultaneously in both genes. All mutants showed normal growth in rich medium under aerobic conditions. Unlike the hemN(1) mutant, strains lacking a functional hemN(2) gene were unable to grow anaerobically under nitrate-respiring conditions and largely failed to fix nitrogen in symbiosis with the soybean host plant. Moreover, these mutants lacked several c-type cytochromes which are normally detectable by heme staining of proteins from anaerobically grown wild-type cells. Taken together, our results revealed that B. japonicum hemN(2), but not hemN(1), encodes a protein that is functional under the conditions tested, and this conclusion was further corroborated by the successful complementation of a Salmonella enterica serovar Typhimurium hemF hemN mutant with hemN(2) only.  (+info)

A unique hybrid pathway has been proposed for de novo heme biosynthesis in Plasmodium falciparum involving three different compartments of the parasite, namely mitochondrion, apicoplast and cytosol. While parasite mitochondrion and apicoplast have been shown to harbor key enzymes of the pathway, there has been no experimental evidence for the involvement of parasite cytosol in heme biosynthesis. In this study, a recombinant P. falciparum coproporphyrinogen III oxidase (rPfCPO) was produced in E. coli and confirmed to be active under aerobic conditions. rPfCPO behaved as a monomer of 61 kDa molecular mass in gel filtration analysis. Immunofluorescence studies using antibodies to rPfCPO suggested that the enzyme was present in the parasite cytosol. These results were confirmed by detection of enzyme activity only in the parasite soluble fraction. Western blot analysis with anti-rPfCPO antibodies also revealed a 58 kDa protein only in this fraction and not in the membrane fraction. The cytosolic ...
Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersHeme, porphyrin, and cobalaminputative oxygen-independent coproporphyrinogen III oxidase (TIGR00539; EC 1.3.99.22; HMM-score: 12.3) ...
... is an autosomal dominant form of liver (hepatic) porphyria that is very similar to acute intermittent porphyria, although it is usually a less severe disease. It results from low levels of the enzyme responsible for the sixth step in heme production - coproporphyrinogen oxidase. This enzyme speeds the conversion of coproporphyrinogen to protoporphyrinogen. In coproporphyria, the porphyrin precursors porphobilinogen and amino-levulinic acid (ALA) accumulate, as well as the formed porphyrin coproporphyrin. This leads to abdominal pain, neuropathies, constipation, and skin changes. Treatment is dependent on the symptoms ...
Hereditary coproporphyria is one of the porphyrias, a group of diseases that involves defects in heme metabolism and that results in excessive secretion of porphyrins and porphyrin precursors. Inheritance is autosomal (usually autosomal dominant, but sometimes autosomal recessive).
A collection of disease information resources and questions answered by our Genetic and Rare Diseases Information Specialists for Hereditary coproporphyria
Porphyrins are organic aromatic compounds composed of four pyrrole rings interconnected to each other and to the Fe2+ ion. Porphyrins are essential cofactors of many proteins including cytochrome proteins and haemoglobin and myoglobin in humans. The first step in the production of porphyrin in animals is the mitochondrial formation of delta-aminolevulinate from glycine and succinyl-CoA. In humans, this aminolevulinate is then transported to cytosol where the 4-step conversion into Coproporphyrinogen III occurs. The remaining processing of this intermediate to protoporphyrin IX and then to heme takes place in mitochondrion.. The cytochrome proteins in Plasmodium and Coccidian species such as Toxoplasma and Neospora require de novo synthesis of porphyrin. Although P. falciparum obtains heme from host haemoglobin digestion, it cannot utilise them for biosynthesis of its own porphyrin-containing proteins [1] and converts them to hemozoin [2]. The enzymes of de novo heme biosynthesis in P. falciparum ...
As for the hem, a) I wouldnt do a wide hem on a knit. Using a narrow hem will largely eliminate the need to ease anyway. I have no idea what the patterns suggested hem is, so this is just me babbling. b) Theres a product called Steam-a-Seam 2 lite that comes in long, narrow rolls (I got mine, predictably, at Fabricland, but it seems to be widely available). Its basically a (barely) double-sided tape of extremely light fusing. You place it, peel the top off, fold it over, iron it into place (which is more or less permanent, and then twin-needle or whatever. It adds a tiny bit of body to the hem (not noticeable in most knits), keeps it in place while stitching, and is at least as stretchy as your twin-needle stitch. Although it doesnt solve every problem, it makes knit hems much more fun ...
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If you have used this database, please ensure that you acknowledge this most recent Pseudomonas Genome Database publication rather than just the website URL. Thank you!. Winsor GL, Griffiths EJ, Lo R, Dhillon BK, Shay JA, Brinkman FS (2016 ...
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Depression (HCP) Symptom Checker: Possible causes include Hereditary Coproporphyria & Hantavirus Pulmonary Syndrome & Erythropoietic Coproporphyria. Check the full list of possible causes and conditions now! Talk to our Chatbot to narrow down your search.
If you have used this database, please ensure that you acknowledge this most recent Pseudomonas Genome Database publication rather than just the website URL. Thank you!. Winsor GL, Griffiths EJ, Lo R, Dhillon BK, Shay JA, Brinkman FS (2016 ...
Protoporphyrinogen oxidases have some domain similarities to N-6 Adenine-specific DNA methylases, however we believe the correct/primary EC number has been assigned to UU004 and UU005. These enzymes are typically constituted of 425-455 residues in bacteria; UU004 appears to represent only the first 272-390 of the residues whereas UU005 may represent the C-terminal residues (false internal stop?). UU005 may be itself a member of the SUA5/yciO/yrdC family (see Prosite PDOC00883). Protoporphyrinogen oxidase is the enzyme that catalyzes in the penultimate step in the heme biosynthetic pathway ...
Most types are inherited but the most common type, porphyria cutanea tarda is acquired, associated with liver disease and iron overload. Of 4 types, any may present with neurovisceral presentation esp colicky abdominal pain, and hereditary coproporphyria and variegate porphyria can also present with cutaneous features. Attacks are likely precipitated by adverse effects of excess ALA which is structurally similar to GABA. Starvation, poor CH2O/ energy intake, drugs, alcohol, smoking, infections and stress can ppt. In this case the negative energy balance with surgery caused up regulation of hepatic ALA synthase 1, due to loss of CH2O repression of rate controlling enzyme for heme synthesis in the liver. Other "bad " drugs in this case were phenytoin, tramadol and bactrim. Sulfonamides and barbiturates are also "bad." So is progesterone (which is why postpubertal women are more susceptible). The treatment is i-v heme. It can prevent reversible axonal death. Prognosis is slow and incomplete ...
Bikramjit Raychaudhury*, R. Jyoti, Kakuli Chakraborty, Anindita Chakraborty, Moushree Palroy and Rajen Haldar. ABSTRACT. Leishmaniasis is a parasitic disease which infects as many as 400,000 people per year. Because the infective agent- a protozoan-inhabits phagolysosomes in host macrophages, the parasites are partially protected from chemotherapeutic agents. Thus, treated patients often relapse or experience toxic reactions to the drugs. In order to develop new leishmanicidal agents, studies have been conducted to understand the interactions of the parasite with the macrophage. Ordinarily, microorganisms which are taken up by macrophages are destroyed by oxygen-dependent and oxygen-independent antimicrobial systems. The oxygen-dependent antimicrobial activity of macrophages is dependent on the generation of superoxide (O2-) by the one-electron reduction of molecular oxygen. This O2- can then undergo a series of reactions to produce hydrogen peroxide (H2O2), hydroxyl radicals (.OH), and perhaps, ...
This protein is identical to GenBank accession AAD18267 (genome position accession AE001598). This methylase is thought to promote the oxidation of protoporphyrinogen. (May have DNA methylating activity ...
Underwater kinetics eLed CPO AT Tail Switch I. When our customers demanded a flashlight with superior LED technology that was also lightweig, dive
17. Ulusal Çocuk Cerrahisi Hemşireliği Kongresi 30 Ekim - 2 Kasım October - 2 November 2013 Eskişehir Ulusal Çocuk Cerrahisi Hemşireliği Kongresi Kurulları KONGRE ONURSAL ÜYELERİ Prof.
PBGU : First-order test for evaluation of a suspected acute porphyria: acute intermittent porphyria, hereditary coproporphyria, and variegate porphyria
AS07 227, HemY antibody, NP_681164, Anti-HemY | protoporphyrinogen oxidase antibodyHemY is an uncharacterized enzyme of heme biosynthesis. Immunogen: Overexpressed Thermosynechococcus elongatus HemY
FIG. 7. Reversibility of Ni-induced gene expression. Expression of target genes in strain CC125 at 3 × 106 cells/ml is shown in lane 1 (t = 0). The culture was treated with either 25 μM NiCl2 for 5 h (lane 2) or 50 μM EDTA for 5 or 19 h (lanes 7 and 8) The reversibility of the 5 h Ni2+ treatment was ascertained either by addition of excess EDTA (50 μM) to chelate the Ni2+ ions or by transfer to fresh medium and then sampled 5 or 19 h later to assess gene expression (lanes 5 and 6 and lanes 9 and 10, respectively). Ni-treated cultures were maintained in parallel for another 5 or 19 h as a control for the EDTA treatment (lanes 3 and 4, respectively), or in the case of the washed cells, NiCl2 was added back, and the culture sampled 5 or 19 h later (lanes 11 and 12). The total time of exposure to Ni2+ was, therefore, 10 or 24 h. Total RNA was isolated and analyzed by RNA blot hybridization for Cyc6 and Cpx1 expression. Cβlp expression was used as a loading control. The circular arrow indicates ...
Startsida för Europaparlamentets utskott för sysselsättning och sociala frågor (EMPL). Senaste nyheter, länkar till dokument och videoinspelningar av sammanträden.
ID W8WYL2_CASDE Unreviewed; 561 AA. AC W8WYL2; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 25-OCT-2017, entry version 19. DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313,EMBL:CDM24848.1}; DE EC=1.1.5.3 {ECO:0000313,EMBL:CDM24848.1}; GN ORFNames=BN940_11951 {ECO:0000313,EMBL:CDM24848.1}; OS Castellaniella defragrans 65Phen. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Castellaniella. OX NCBI_TaxID=1437824 {ECO:0000313,EMBL:CDM24848.1, ECO:0000313,Proteomes:UP000019805}; RN [1] {ECO:0000313,EMBL:CDM24848.1, ECO:0000313,Proteomes:UP000019805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=65Phen {ECO:0000313,EMBL:CDM24848.1}; RX PubMed=24952578; DOI=10.1186/1471-2180-14-164; RA Petasch J., Disch E.M., Markert S., Becher D., Schweder T., Huttel B., RA Reinhardt R., Harder J.; RT "The oxygen-independent metabolism of cyclic monoterpenes in RT Castellaniella defragrans 65Phen."; RL BMC ...
Hemö local information and maps. Hemö is a section of island in Stockholms Län, Sweden, Europe. Hemo is also known as Hemon, Hemön.
PPOX antibody [N3C3] (protoporphyrinogen oxidase) for WB. Anti-PPOX pAb (GTX106163) is tested in Human samples. 100% Ab-Assurance.
Omstreeks die tijd legde koning Herodes de hand op enkele leden van de Kerk om hen te mishandelen. Jakobus, de broer van Johannes, liet hij met het zwaard ter dood brengen. Omdat hij bemerkte dat dit de Joden aangenaam was, liet hij ook nog Petrus gevangen nemen. Het was juist in de dagen van het ongedesemde brood. Toen hij hem in handen had gekregen, wierp hij hem in de gevangenis en liet hem bewaken door vier groepen soldaten, elk van vier man. Het was zijn bedoeling Petrus na het paasfeest voor het volk te leiden. Terwijl Petrus in de gevangenis zat, werd door de Kerk vurig voor hem tot God gebeden. In de nacht voordat Herodes hem wilde laten voorleiden, lag Petrus met twee kettingen vastgebonden te slapen tussen twee soldaten, terwijl ook voor de poort van de gevangenis wacht werd gehouden. Opeens stond een engel des Heren bij hem en was de cel hel verlicht. Hij stootte Petrus in de zij, wekte hem en sprak: Sta vlug op. Meteen vielen de kettingen van zijn handen. Vervolgens zei de engel: ...
Gavin Collins is a microbiologist with interests in microbial ecology; environmental microbiology; and environmental biotechnology. He is an ERC Laureate at NUI Galway; a Fulbright Scholar University of California Berkeley); an Alexander von Humboldt Fellow at Helmholtz-Zentrum für Umweltforschung - UFZ - Leipzig, Germany 2017-2019; a Royal Irish Academy Charlemount Scholar; an Ireland-Canada University Scholar (University of British Columbia, Vancouver); Marie Curie Fellow (Max Planck Institute for Marine Microbiology, Bremen); Irish Research Council Fellow; and British Science Association Media Fellow at The Irish Times ...
CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental pluripotency associated 2. *DZIP3 ...
"Four novel mutations of the coproporphyrinogen III oxidase gene". Cellular and Molecular Biology. 55 (1): 8-15.. ... Thus cytochrome oxidase, which has two A hemes (heme a and heme a3) in its structure, contains two moles of heme A per mole ... Cytochrome a refers to the heme A in specific combination with membrane protein forming a portion of cytochrome c oxidase.[13] ... PPOX: protoporphyrinogen oxidase (deficiency causes variegate porphyria)[42]. *UROD: uroporphyrinogen decarboxylase (deficiency ...
"Four novel mutations of the coproporphyrinogen III oxidase gene". Cellular and Molecular Biology. 55 (1): 8-15. Bustad, H. J.; ... coproporphyrinogen oxidase (deficiency causes hereditary coproporphyria) FECH: ferrochelatase (protoporphyria) HMBS: ... Caughey, W. S.; Smythe, G. E.; O'Keeffe, D. H.; Maskasky, J. E.; Smith, M. L. (1975). "Heme A of Cytochrome c Oxidase: ... Cytochrome a refers to the heme A in specific combination with membrane protein forming a portion of cytochrome c oxidase. The ...
"Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol". Parasitology International. 59 (2): 121- ...
The enzyme coproporphyrinogen oxidase converts coproporphyrinogen III into protoporphyrinogen IX. The process entails ... In coproporphyrinogen III, the pyrrole substituents have the arrangement MeP-MeP-MeP-PMe, where Me and P are methyl and ... By the action of protoporphyrinogen oxidase, protoporphyrinogen IX is converted into protoporphyrin IX, the first colored ...
HCP is caused by a deficiency of the enzyme coproporphyrinogen oxidase, coded for by the CPOX gene, and is inherited in an ... There is no cure for HCP caused by the deficient activity of coproporphyrinogen oxidase. Treatment of the acute symptoms of HCP ... HCP is caused by mutations in the CPOX gene, which codes for the enzyme coproporphyrinogen oxidase. This enzyme is responsible ... ISBN 978-3-642-15719-6. "Homo sapiens coproporphyrinogen oxidase, mRNA (cDNA clone MGC:19736 IMAGE:3607724), complete cds". US ...
Enzyme tests show markedly reduced activity of coproporphyrinogen oxidase, compared to both unaffected individuals and those ...
Genes encoding coproporphyrinogen oxidase, an essential enzyme in the heme biosynthetic pathway were found as well as genes ...
... and it is converted into protoporphyrinogen IX by coproporphyrinogen III oxidase. Coproporphyrinogens at the US National ... Coproporphyrinogen III is the most common variance. In the metabolism of porphyrin, it is formed from uroporphyrinogen III by ... Library of Medicine Medical Subject Headings (MeSH) PubChem - Coproporphyrinogen III. ...
... coproporphyrinogen oxidase (coproporphyria, harderoporphyria) DPPA2: Developmental pluripotency associated 2 DZIP3 encoding ... homogentisate oxidase) IFT122: intraflagellar transport gene 122 KIAA1257: KIAA1257 LMLN: encoding protein Leishmanolysin-like ...
... oxygen-independent coproporphyrinogen III oxidase (cofactor biosynthesis - heme) HmdB - 5,10-methenyltetrahydromethanopterin ...
... coproporphyrinogen oxidase EC 1.3.3.4: protoporphyrinogen oxidase EC 1.3.3.5: bilirubin oxidase EC 1.3.3.6: acyl-CoA oxidase EC ... D-aspartate oxidase EC 1.4.3.2: L-amino-acid oxidase EC 1.4.3.3: D-amino-acid oxidase EC 1.4.3.4: amine oxidase (flavin- ... glycine oxidase EC 1.4.3.20: L-lysine 6-oxidase EC 1.4.3.21: primary-amine oxidase EC 1.4.3.22: diamine oxidase EC 1.4.3.23: 7- ... malate oxidase EC 1.1.3.4: glucose oxidase EC 1.1.3.5: hexose oxidase EC 1.1.3.6: cholesterol oxidase EC 1.1.3.7: aryl-alcohol ...
Layer G, Moser J, Heinz DW, Jahn D, Schubert WD (2003). "Crystal structure of coproporphyrinogen III oxidase reveals cofactor ... Layer G, Verfurth K, Mahlitz E, Jahn D (2002). "Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli". ... Importantly, only HemN utilizes S-adenosyl Methionine (SAM). Human variants of Coproporphyrinogen oxidase are cofactor- ... HemN is the Oxygen-independent oxidase produced in E. coli. HemF is the oxygen-dependent oxidase within E. coli. ...
... coproporphyrinogen oxidase FECH: ferrochelatase (protoporphyria) HMBS: hydroxymethylbilane synthase PPOX: protoporphyrinogen ... Protoporphyrinogen oxidase is an enzyme that in humans is encoded by the PPOX gene. Protoporphyrinogen oxidase is responsible ... Nishimura K, Taketani S, Inokuchi H (Apr 1995). "Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in ... Dailey TA, Meissner P, Dailey HA (Jan 1994). "Expression of a cloned protoporphyrinogen oxidase". The Journal of Biological ...
Coproporphyrinogen-III oxidase, mitochondrial (abbreviated as CPOX) is an enzyme that in humans is encoded by the CPOX gene. A ... Coproporphyrinogen III Oxidases at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Guo R, Lim CK, Peters TJ (October 1988). "Accurate and specific HPLC assay of coproporphyrinogen III oxidase activity in human ... Madsen O, Sandal L, Sandal NN, Marcker KA (October 1993). "A soybean coproporphyrinogen oxidase gene is highly expressed in ...
Coproporphyrinogen III oxidase. *Protoporphyrinogen oxidase. *Bilirubin oxidase. *Acyl-CoA oxidase. *Dihydrouracil oxidase ...
... coproporphyrinogen oxidase MeSH D08.811.682.660.275 --- dihydrodipicolinate reductase MeSH D08.811.682.660.300 --- ... sarcosine oxidase MeSH D08.811.682.662.640 --- proline oxidase MeSH D08.811.682.662.680 --- pyridoxamine-phosphate oxidase MeSH ... d-amino-acid oxidase MeSH D08.811.682.664.500.261 --- d-aspartate oxidase MeSH D08.811.682.664.500.398 --- glutamate ... proline oxidase MeSH D08.811.682.664.500.848 --- protein-lysine 6-oxidase MeSH D08.811.682.664.500.924 --- valine dehydrogenase ...
Naturally occurring porphyrinogens Uroporphyrinogen III, precursor to coproporphyrinogen III. coproporphyrinogen III, precursor ... In the biosynthesis of porphyrins protoporphyrinogen is dehydrogenated by protoporphyrinogen oxidase. Because of their limited ...
Coproporphyrinogen III oxidase. *Protoporphyrinogen oxidase. *Bilirubin oxidase. *Acyl-CoA oxidase. *Dihydrouracil oxidase ...
Its biosynthesis is mediated by the enzyme protoporphyrinogen oxidase. The simplified biosynthetic sequence is acyclic ...
Oxygen-dependent coproporphyrinogen III oxidase superfamily (IPR036406). Short name: Coprogen_oxidase_aer_sf ... A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules.. Plant Mol. Biol. 23 35-43 1993 ... Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation.. J. Biol. ... Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae.. Eur. J. Biochem. 156 579-87 ...
Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the ... IPR004558 Coprogen_oxidase_HemN. IPR034505 Coproporphyrinogen-III_oxidase. IPR006638 Elp3/MiaB/NifB. IPR010723 HemN_C. ... IPR004558 Coprogen_oxidase_HemN. IPR034505 Coproporphyrinogen-III_oxidase. IPR006638 Elp3/MiaB/NifB. IPR010723 HemN_C. ... Oxygen-independent coproporphyrinogen III oxidase (EC:1.3.98.3*Search proteins in UniProtKB for this EC number. ...
Coproporphyrinogen III oxidase; Plasmodium falciparum; Heme. Department/Centre:. Division of Biological Sciences , Biochemistry ... In this study, a recombinant P. falciparum coproporphyrinogen III oxidase (rPfCPO) was produced in E. coli and confirmed to be ... Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol. In: Parasitology International, 59 (2). pp ...
The coproporphyrinogen oxidase enzyme speeds the conversion of coproporphyrinogen to protoporphyrinogen. In subsequent steps, ... coproporphyrinogen oxidase, which is responsible for the sixth step in heme production. Heme is an essential component of iron- ... In HCP, the the function of coproporphyrinogen oxidase is only 40-60% of normal. This reduced function leads to a build up of ... Coproporphyrinogen oxidase deficiency; CPO deficiency; CPRO deficiency; CPX deficiency See More ...
... coproporphyrinogen oxidase. This enzyme speeds the conversion of coproporphyrinogen to protoporphyrinogen. In coproporphyria, ... coproporphyria is an autosomal dominant disorder resulting from the half-normal activity of coproporphyrinogen oxidase (CPO), a ...
Coproporphyrinogen-III oxidase, mitochondrial (abbreviated as CPOX) is an enzyme that in humans is encoded by the CPOX gene. A ... Coproporphyrinogen III Oxidases at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Guo R, Lim CK, Peters TJ (October 1988). "Accurate and specific HPLC assay of coproporphyrinogen III oxidase activity in human ... Madsen O, Sandal L, Sandal NN, Marcker KA (October 1993). "A soybean coproporphyrinogen oxidase gene is highly expressed in ...
Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the ... IPR001260 Coprogen_oxidase_aer. IPR036406 Coprogen_oxidase_aer_sf. IPR018375 Coprogen_oxidase_CS. ... IPR001260 Coprogen_oxidase_aer. IPR036406 Coprogen_oxidase_aer_sf. IPR018375 Coprogen_oxidase_CS. ... "Leishmania major coproporphyrinogen III oxidase with bound ligand.". Merritt E.A., Le Trong I., Larson E.T., Shibata S., Zhang ...
Coproporphyrinogen III oxidase is an enzyme involved in the sixth step of porphyrin metabolism, converting coproporphyrinogen ... Coproporphyrinogen-III oxidase, mitochondrial is an enzyme that in humans is encoded by the CPOX gene.[1][2][3] ... Lamoril J, Deybach JC, Puy H, et al. (1997). "Three novel mutations in the coproporphyrinogen oxidase gene.". Hum. Mutat. 9 (1 ... Daimon M, Gojyou E, Sugawara M, et al. (1997). "A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase ...
An autosomal dominant porphyria that is due to a deficiency of COPROPORPHYRINOGEN OXIDASE in the LIVER, the sixth enzyme in the ... Coproporphyrinogen Oxidase (Coproporphyrinogen III Oxidases)IBA 10/01/2000 - "The present study describes a simple method for ... An autosomal dominant porphyria that is due to a deficiency of COPROPORPHYRINOGEN OXIDASE in the LIVER, the sixth enzyme in the ... Hereditary Coproporphyria (Coproporphyrinogen Oxidase Deficiency). Subscribe to New Research on Hereditary Coproporphyria ...
Involved in coproporphyrinogen oxidase activity. Specific Function. Key enzyme in heme biosynthesis. Catalyzes the oxidative ... Susa S, Daimon M, Ono H, Li S, Yoshida T, Kato T: The long, but not the short, presequence of human coproporphyrinogen oxidase ... Showing Protein Coproporphyrinogen-III oxidase, mitochondrial (HMDBP00251). IdentificationBiological propertiesGene properties ... Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y: A molecular defect in coproporphyrinogen oxidase gene ...
Learn more about Anti-Coproporphyrinogen oxidase Rabbit Polyclonal Antibody. We enable science by offering product choice, ... Home , Antibodies , Anti-Coproporphyrinogen oxidase Rabbit Polyclonal Antibody. Anti-Coproporphyrinogen oxidase Rabbit ... CPOX(Coproporphyrinogen-III oxidase, mitochondrial) is also named as CPO and CPX. Human CPO is a 76 kDa protein that is active ... Antigen: Coproporphyrinogen oxidase. Clonality: Polyclonal. Clone: Conjugation: Unconjugated. Epitope: Host: Rabbit. Isotype: ...
Coproporphyrinogen oxidase. CPOX is the sixth enzyme of the heme biosynthetic pathway. The enzyme is soluble and found in the ... The association between a genetic polymorphism of coproporphyrinogen oxidase, dental mercury exposure and neurobehavioral ...
HCP is caused by a deficiency of coproporphyrinogen oxidase due to mutations in a gene by the same name at 3q12. The greatest ... HCP is caused by a deficiency of coproporphyrinogen oxidase due to mutations in a gene by the same name at 3q12. The greatest ... HCP is caused by a deficiency of coproporphyrinogen oxidase due to mutations in a gene by the same name at 3q12. The greatest ... the disorder is caused by a deficiency in coproporphyrinogen oxidase. The greatest difference between HCP and AIP is that ...
CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental pluripotency associated 2. *DZIP3 ...
We examined the hypothesis that CPOX4, a genetic variant of the heme pathway enzyme coproporphyrinogen oxidase (CPOX) that ... Modification of neurobehavioral effects of mercury by a genetic polymorphism of coproporphyrinogen oxidase in children.. Woods ...
The expression of coproporphyrinogen oxidase, thiazole biosynthetic enzyme, glutamine synthetase, ATP citrate lyase, and ... cytochrome C oxidase were only observed in library C1, while those of fatty acid biosynthesis (path 2), styrene degradation, ...
Coproporphyrinogen oxidase removes a carboxyl group from the propionic groups on 2 of the pyrrole rings to yield ... Protoporphyrinogen oxidase forms protoporphyrin by removing 6 hydrogen atoms from protoporphyrinogen IX. This enzyme has been ... Identification of a recurrent mutation in the protoporphyrinogen oxidase gene in Swiss patients with variegate porphyria: ... sequentially removes a carboxylic group from the acetic side chains of each of the pyrrole rings to yield coproporphyrinogen. ...
Oxygen-dependent coproporphyrinogen-III oxidase. Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081). ... Oxygen-dependent coproporphyrinogen-III oxidase. Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). Loading... ... Oxygen-dependent coproporphyrinogen-III oxidase. Shewanella baltica (strain OS155 / ATCC BAA-1091). Loading... ... Oxygen-dependent coproporphyrinogen-III oxidase. Francisella tularensis subsp. tularensis (strain WY96-3418). Loading... ...
coproporphyrinogen oxidase activity IEA Inferred from Electronic Annotation. more info. metal ion binding IEA Inferred from ...
Ex vivo, expression of various heme biosynthetic enzymes including coproporphyrinogen oxidase (CPOX) was measured, and ... Ex vivo, expression of various heme biosynthetic enzymes including coproporphyrinogen oxidase (CPOX) was measured, and ... Ex vivo, expression of various heme biosynthetic enzymes including coproporphyrinogen oxidase (CPOX) was measured, and ... Ex vivo, expression of various heme biosynthetic enzymes including coproporphyrinogen oxidase (CPOX) was measured, and ...
Oxygen-independent coproporphyrinogen III oxidase. Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / ... Oxygen-independent coproporphyrinogen III oxidase UniProtKBInterProInteractive Modelling. 460 aa; Sequence (Fasta) Identical ...
Coproporphyrinogen III oxidase, aerobic (IPR001260) Pfam signature: PF01218 DAGK family (IPR000829) Pfam signature: PF01219 ... Cytochrome c oxidase subunit I (IPR000883) Pfam signature: PF00115 Cytochrome c oxidase subunit II-like C-terminal (IPR002429) ... Cytochrome c oxidase subunit III-like (IPR000298) Pfam signature: PF00510 Papillomavirus E2, C-terminal (IPR000427) Pfam ... Acyl-CoA dehydrogenase/oxidase C-terminal (IPR009075) Pfam signature: PF00441 Peptidase C19, ubiquitin carboxyl-terminal ...
"Four novel mutations of the coproporphyrinogen III oxidase gene". Cellular and Molecular Biology. 55 (1): 8-15.. ... Thus cytochrome oxidase, which has two A hemes (heme a and heme a3) in its structure, contains two moles of heme A per mole ... Cytochrome a refers to the heme A in specific combination with membrane protein forming a portion of cytochrome c oxidase.[13] ... PPOX: protoporphyrinogen oxidase (deficiency causes variegate porphyria)[42]. *UROD: uroporphyrinogen decarboxylase (deficiency ...
coproporphyrinogen oxidase MGI:104841 .yui-skin-sam .yui-dt th{ background:url(http://www.informatics.jax.org/webshare/images/ ...
coproporphyrinogen (COPRO) oxidase. Hereditary coproporphyria (HCP). Hepatic. Autosomal dominant [7]. Photosensitivity, ... Variegate porphyria (also porphyria variegata or mixed porphyria), which results from a partial deficiency in PROTO oxidase, ... protoporphyrinogen (PROTO) oxidase. Variegate porphyria (VP). Mixed. Autosomal dominant [7]. Photosensitivity, neurologic ...
  • LOCUS CRU26344 427 bp mRNA PLN 01-JUN-1995 DEFINITION Chlamydomonas reinhardtii coproporphyrinogen oxidase (CPX) mRNA, partial cds. (bio.net)
  • Modification of neurobehavioral effects of mercury by a genetic polymorphism of coproporphyrinogen oxidase in children. (cdc.gov)
  • Chlamydomonas reinhardtii activates Cpx1 , Cyc6 , and Crd1 , encoding, respectively, coproporphyrinogen oxidase, cytochrome c 6 , and a novel di-iron enzyme when transferred to oxygen-deficient growth conditions. (plantphysiol.org)