chembox verifiedrevid 444060219 ImageFile Porphobilinogen.png ImageSize 200px IUPACName 3 5 Aminomethyl 4 carboxymethyl 1H pyrrol 3 yl propanoic acid OtherNames Section1 Chembox Identifiers CASNo 487 90 1 PubChem 1021 DrugBank Ref drugbankcite correct drugbank DrugBank DB02272 SMILES C1 C C C N1 CN CC O O CCC O O EINECS 207 666 3 MeSHName Porphobilinogen Section2 Chembox Properties Formula C sub 10 sub H sub 14 sub N sub 2 sub O sub 4 sub MolarMass 226.229 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Porphobilinogen PBG is a pyrrole involved in porphyrin metabolism. It is generated by aminolevulinate ALA and the enzyme ALA dehydratase . PBG is then converted into hydroxymethyl bilane by the enzyme porphobilinogen deaminase , also known as hydroxymethylbilane synthase . Acute intermittent porphyria causes an increase in urinary porphobilinogen. ref cite journal last Aarsand first AK coauthors Petersen PH, Sandberg S title Estimation and application of biological variation of urinary delta aminolevulinic acid and porphobilinogen in healthy individuals and in patients with acute intermittent porphyria journal Clinical Chemistry volume 52 issue 4 pages 650 656 month April year 2006 url http www.clinchem.org cgi content full 52 4 650 pmid 16595824 doi 10.1373 clinchem.2005.060772 ref References references Heme metabolism intermediates Category Metabolism Category Pyrroles Category Carboxylic acids Category Amines biochemistry stub de Porphobilinogen it Porfobilinogeno ja ... more details
enzyme Name porphobilinogen synthase EC number 4.2.1.24 CAS number 9036 37 7 IUBMB EC number 4 2 1 24 GO code 0004655 image width caption protein Name ALAD Delta aminolevulinic acid dehydratase caption image width HGNCid 395 Symbol ALAD AltSymbols EntrezGene 210 OMIM 125270 RefSeq NM 001003945 UniProt P13716 PDB ECnumber 4.2.1.24 Chromosome 9 Arm q Band 32 LocusSupplementaryData Infobox protein family Symbol ALAD Name ALAD image PDB 1b4k EBI.jpg width caption high resolution crystal structure of a mg2 dependent 5 aminolevulinic acid dehydratase Pfam PF00490 Pfam clan CL0036 InterPro IPR001731 SMART PROSITE PDOC00153 MEROPS SCOP 1aw5 TCDB OPM family OPM protein CAZy CDD Porphobilinogen synthase or ALA dehydratase , or aminolevulinate dehydratase synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid . All natural tetrapyrroles , including heme s, chlorophyll s and vitamin B12 vitamin B sub 12 sub , share porphobilinogen as a common precursor. It is involved in the second step of the metabolism of porphyrin . Deficiency ALA dehydratase deficiency redirects here A deficiency of porphobilinogen synthase is usually acquired rather than hereditary and and can be caused by heavy metal poisoning , especially lead poisoning , as the enzyme is very susceptible to inhibition by heavy metals. ref http library.med.utah.edu NetBiochem hi32.htm ALA dehydratase reaction , from NetBiochem at the University of Utah. Last modified 1 5 95 ref Hereditary insufficiency of porphobilinogen synthase is called Aminolevulinic acid dehydratase deficiency porphyria porphobilinogen synthase or ALA dehydratase deficiency poprhyria . It is an extremely rare cause of porphyria , ref name pmid17236137 cite journal author Jaffe EK, Stith L title ALAD porphyria is a conformational disease journal Am. J. Hum. Genet. volume 80 issue 2 pages 329 37 year 2007 month February pmid 17236137 pmc 1785348 doi 10.1086 511444 url accessdate 2008 12 10 ref with less ... more details
PBB geneid 3145 Porphobilinogen deaminase also known as hydroxymethylbilane synthase or uroporphyrinogen I synthase is an enzyme involved in the third step of the metabolism of porphyrin , converting porphobilinogen into hydroxymethylbilane . The enzyme has the unique cofactor dipyrromethane . Defective activity of this enzyme can lead to the disorder acute intermittent porphyria . The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text This gene encodes a member of the hydroxymethylbilane synthase superfamily. The encoded protein is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane ... refbegin 2 PBB Further reading citations cite journal author Deybach JC, Puy H title Porphobilinogen ... in porphobilinogen deaminase gene polymorphisms and mutations causing acute intermittent porphyria ... of seven point mutations in the porphobilinogen deaminase gene in patients with acute intermittent ... G, et al. title High frequency of mutations in exon 10 of the porphobilinogen deaminase gene ... Namba H, Narahara K, Tsuji K, et al. title Assignment of human porphobilinogen deaminase to 11q24.1 ... M title Identification of the most common mutation within the porphobilinogen deaminase gene in Swedish ... intermittent porphyria caused by a C T mutation that produces a stop codon in the porphobilinogen ... to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent ... JCI114869 pmc 296897 cite journal author Lannfelt L, Wetterberg L, Lilius L, et al. title Porphobilinogen ... al. title A point mutation G A in exon 12 of the porphobilinogen deaminase gene results in exon skipping ... porphobilinogen deaminase journal Nucleic Acids Res. volume 14 issue 15 pages 5955 68 year ... yes update citations yes de Porphobilinogen Desaminase es HMBS it Porfobilinogeno deaminasi ja ... more details
PBG is a three letter acronym three letter abbreviation which may represent Palm Beach Gardens, Florida , a US city Parallel Blade with Ground, a term used in theater lighting to designate an ordinary NEMA connector NEMA 5 15 electrical power connector The Pepsi Bottling Group NYSE PBG , a US company Porphobilinogen Plattsburgh International Airport in Plattsburgh, New York IATA Code PBG Photonic band gap, a property of Photonic crystals Paintball marker Paintball gun marker disambig de PBG Begriffskl rung it PBG ... more details
Aminolevulinic acid dehydratase deficiency porphyria also known as Doss porphyria, ref name Bolognia and Plumboporphyria ref name Bolognia is a cutaneous condition, disease can present during early childhood as well as in adulthood with acute neurologic symptoms that resemble those encountered in acute intermittent porphyria. ref name Bolognia cite book author Rapini, Ronald P. Bolognia, Jean L. Jorizzo, Joseph L. title Dermatology 2 Volume Set publisher Mosby location St. Louis year 2007 pages isbn 1 4160 2999 0 oclc doi accessdate ref The condition is extremely rare, with less than 10 cases ever reported. ref http rarediseasesnetwork.epi.usf.edu porphyrias patients ADP Overview of the Porphyrias at The Porphyrias Consortium a part of NIH Rare Diseases Clinical Research Network RDCRN Retrieved June 2011 ref ALA dehydratase deficiency is a rare cause of hepatic porphyria . ref name jaffe cite journal author Jaffe EK, Stith L title ALAD porphyria is a conformational disease journal American Journal of Human Genetics volume 80 issue 2 pages 329 37 year 2007 month February pmid 17236137 pmc 1785348 doi 10.1086 511444 url http linkinghub.elsevier.com retrieve pii S0002 9297 07 62690 1 ref ref name pmid513604 cite journal author Doss M, von Tiepermann R, Schneider J, Schmid H title New type of hepatic porphyria with porphobilinogen synthase defect and intermittent acute clinical manifestation journal Klinische Wochenschrift volume 57 issue 20 pages 1123 7 year 1979 month October pmid 513604 doi url ref It is an autosomal recessive disorder that results from inappropriately low levels of the enzyme porphobilinogen synthase ALA dehydratase ALAD, also called porphobilinogen synthase , which is required for normal heme synthesis. ref name jaffe Genetics Image Autorecessive.svg thumb right ALA dehydratase deficiency has an autosomal recessive pattern of heredity inheritance . ALA dehydratase deficiency is inherited in an autosomal recessive manner. ref name jaffe This means a ... more details
Bilins , bilanes or bile pigments are biological pigments formed in many organisms as a metabolic product of certain porphyrin s. Bilin also called bilichrome was named as a bile pigment of mammal s, but can also be found in lower vertebrate s, invertebrate s, as well as red algae , green plant s and cyanobacteria . Bilins can range in color from red, orange, yellow or brown to blue or green. In chemical terms, bilins are linear arrangements of four pyrrole rings tetrapyrrole s . In human metabolism, bilirubin is a breakdown product of heme . Hydroxymethyl bilane is a major anabolic product, from the biosynthetic reaction of porphobilinogen PBG and uroporphyrinogen I synthase known as porphobilinogen deaminase . Examples of bilins are found in animals, and phycocyanobilin , the chromophore of the photosynthetic pigment phycocyanin in algae and plants. In plants, bilins also serve as the photopigment s of the photoreceptor protein phytochrome . An example of an invertebrate bilin is micromatabilin , which is responsible for the green color of the Green Huntsman Spider, Micrommata virescens . ref name OxfordGillespie1998 Oxford, G.S. & Gillespie, R.G. 1998 . Evolution and Ecology of Spider Coloration. Annual Review of Entomology 43 619 643. DOI 10.1146 annurev.ento.43.1.619 ref See also Bilirubin Biliverdin Phycobilin Phycobiliprotein Phycoerythrobilin Stercobilin Urobilin References references External links MeshName Bilin biochem stub Tetrapyrroles Category Pigments Category Organic pigments Category Tetrapyrroles Category Biomolecules de Gallenfarbstoffe ja ru sl ol no barvilo ... more details
3327436 doi 10.1111 j.1749 6632.1987.tb48759.x cite journal author Jaffe EK title The porphobilinogen ... R, Schneider J title Acute hepatic porphyria syndrome with porphobilinogen synthase defect. journal ..., Jaffe EK, Stauffer F, et al. title Mechanistic basis for suicide inactivation of porphobilinogen synthase ... more details
to a tetramer or a pentamer. The one protein that is established to function as a morpheein is porphobilinogen ... forms. An inhibitor of porphobilinogen synthase with this mechanism of action has been documented ... disease is ALAD porphyria , which results from a mutation of porphobilinogen synthase ... more details
into the cytoplasm , and finishes back in the mitochondrion. However, without porphobilinogen deaminase , a necessary cytoplasmic enzyme, heme synthesis cannot finish, and the metabolite porphobilinogen ... and porphobilinogen in healthy individuals and in patients with acute intermittent porphyria journal ... more details
Unreferenced stub auto yes date December 2009 Chembox verifiedrevid 443862987 ImageFile Ref chemboximage correct ?? ImageFile Hydroxymethylbilane.svg ImageSize IUPACName OtherNames Section1 Chembox Identifiers InChI 1 C40H46N4O17 c45 17 32 25 12 40 60 61 21 4 8 36 52 53 29 44 32 15 31 24 11 39 58 59 20 3 7 35 50 51 28 43 31 14 30 23 10 38 56 57 19 2 6 34 48 49 27 42 30 13 26 22 9 37 54 55 18 16 41 26 1 5 33 46 47 h16,41 45H,1 15,17H2, H,46,47 H,48,49 H,50,51 H,52,53 H,54,55 H,56,57 H,58,59 H,60,61 InChIKey WDFJYRZCZIUBPR UHFFFAOYAI ChEMBL Ref ebicite correct EBI ChEMBL 273676 StdInChI Ref stdinchicite correct chemspider StdInChI 1S C40H46N4O17 c45 17 32 25 12 40 60 61 21 4 8 36 52 53 29 44 32 15 31 24 11 39 58 59 20 3 7 35 50 51 28 43 31 14 30 23 10 38 56 57 19 2 6 34 48 49 27 42 30 13 26 22 9 37 54 55 18 16 41 26 1 5 33 46 47 h16,41 45H,1 15,17H2, H,46,47 H,48,49 H,50,51 H,52,53 H,54,55 H,56,57 H,58,59 H,60,61 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey WDFJYRZCZIUBPR UHFFFAOYSA N CASNo 73023 76 4 PubChem 788 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 767 ChEBI Ref ebicite correct EBI ChEBI 16645 SMILES O C O Cc1c cnc1Cc2c c c n2 Cc3nc c c3CCC O O CC O O Cc4c c c n4 CO CC O O CCC O O CC O O CCC O O CCC O O MeSHName hydroxymethylbilane Section2 Chembox Properties Formula C sub 40 sub H sub 46 sub N sub 4 sub O sub 17 sub MolarMass 854.81 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Hydroxymethylbilane HMB , also known as preuroporphyrinogen , is a molecule involved in the metabolism of porphyrin . In the third step, it is generated by the enzyme porphobilinogen deaminase , and in the next step the enzyme uroporphyrinogen III synthase converts it into uroporphyrinogen III . In general, defects of heme synthesis after formation of HMB lead to photosensitivity . Heme metabolism intermediates Category Tetrapyrroles Biochem stub it Idrossimetilbilano ja ... more details
in several key proteins, for example zinc cations in the ALAD protein, which is also known as Porphobilinogen ... pair effect becomes dramatic for zinc binding proteins, such as the above mentioned porphobilinogen ... more details
condense to give aminolevulinate. Two molecules of this intermediate become linked to form porphobilinogen . Four molecules of porphobilinogen combine to form a linear tetrapyrrole , which cyclizes ... more details
PBB geneid 7975 Transcription factor MafK is a protein that in humans is encoded by the MAFK gene . ref name pmid9763667 cite journal author Iwata T, Kogame K, Toki T, Yokoyama M, Yamamoto M, Ito E title Structure and chromosome mapping of the human small maf genes MAFG and MAFK journal Cytogenet Cell Genet volume 82 issue 1 2 pages 88 90 year 1998 month Nov pmid 9763667 pmc doi 10.1159 000015071 ref ref name entrez cite web title Entrez Gene MAFK v maf musculoaponeurotic fibrosarcoma oncogene homolog K avian url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 7975 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text The developmentally regulated expression of the globin genes depends on upstream regulatory elements termed locus control regions LCRs . LCRs are associated with powerful enhancer activity that is mediated by the transcription factor NFE2 nuclear factor erythroid 2 . NFE2 recognition sites are also present in the gene promoters of 2 heme biosynthetic enzymes, porphobilinogen deaminase PBGD MIM 609806 and ferrochelatase FECH MIM 177000 . NFE2 DNA binding activity consists of a heterodimer containing an 18 kD Maf protein MafF, MafG MIM 602020 , or MafK and p45 MIM 601490 . Both subunits are members of the activator protein 1 superfamily of basic leucine zipper bZIP proteins see MIM 165160 . Maf homodimers suppress transcription at NFE2 sites. supplied by OMIM ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Ney PA, Andrews NC, Jane SM, et al. title Purification of the human NF E2 complex cDNA cloning of the hematopoietic cell specific subunit and evidence for an associated partner journal Mol. Cell. Biol. volume 13 issue 9 pages 5604 12 year 1993 pmid 8355703 doi pmc 360284 cite journal author Oyake T, Itoh K, Motohashi H, et al. title Bach protein ... more details
estimation of porphobilinogen PBG is the first step if acute porphyria is suspected. As a result of feedback ... Network RDCRN Retrieved June 2011 ref Porphobilinogen deaminase hydroxymethylbilane HMB synthase or Porphobilinogen ... more details
of lead poisoning In the human body, lead inhibits porphobilinogen synthase and ferrochelatase , preventing both porphobilinogen formation and the incorporation of iron into protoporphyrin IX , the final ... more details
For other categories, see List of MeSH codes . This is the fourth part of the list of the D codes for MeSH . It is a product of the United States National Library of Medicine . Source for content is http www.nlm.nih.gov mesh filelist.html here . File 2006 MeSH Trees . MeshNumber D08 Enzymes and Coenzymes enzymes and coenzymes MeshNumber D08.211 Coenzymes coenzymes MeshNumber D08.211.090 Biopterin biopterin MeshNumber D08.211.090.500 Neopterin neopterin MeshNumber D08.211.096 Biotin biotin MeshNumber D08.211.175 Cobamides cobamides MeshNumber D08.211.211 Coenzyme A coenzyme a MeshNumber D08.211.211.300 Acyl Coenzyme A acyl coenzyme a MeshNumber D08.211.211.300.075 Acetyl Coenzyme A acetyl coenzyme a MeshNumber D08.211.211.300.500 Malonyl Coenzyme A malonyl coenzyme a MeshNumber D08.211.211.300.700 Palmitoyl Coenzyme A palmitoyl coenzyme a MeshNumber D08.211.474 Flavins flavins MeshNumber D08.211.474.650 Riboflavin riboflavin MeshNumber D08.211.474.650.249 Flavin Adenine Dinucleotide flavin adenine dinucleotide MeshNumber D08.211.474.650.500 Flavin Mononucleotide flavin mononucleotide MeshNumber D08.211.589 NAD nad MeshNumber D08.211.625 NADP nadp MeshNumber D08.211.682 PQQ Cofactor pqq cofactor MeshNumber D08.211.740 Pyridoxal Phosphate pyridoxal phosphate MeshNumber D08.211.790 Sphingolipid Activator Proteins sphingolipid activator proteins MeshNumber D08.211.790.249 G M2 Activator Protein g m2 activator protein MeshNumber D08.211.790.500 Saposins saposins MeshNumber D08.211.840 Tetrahydrofolates tetrahydrofolates MeshNumber D08.211.840.300 Formyltetrahydrofolates formyltetrahydrofolates MeshNumber D08.211.840.300.500 Leucovorin leucovorin MeshNumber D08.211.878 Thiamine Pyrophosphate thiamine pyrophosphate MeshNumber D08.211.906 Thioctic Acid thioctic acid MeshNumber D08.211.935 Ubiquinone ubiquinone MeshNumber D08.244 Cytochromes cytochromes MeshNumber D08.244.175 Cytochrome a Group cytochrome a group MeshNumber D08.244.175.249 Cytochromes a cytochromes a MeshNumb ... more details
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