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 fa it Idrossimetil ... more details
HMBS may refer to Her Majesty s Ship , aka Her Majesty s Burmese Ship or Her majesty s Britannic Ship HMBS gene , hydroxymethylbilane synthase gene, involved in heme biosynthesis disambig ... 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. Mutations in this gene are associated with the autosomal dominant disease acute intermittent porphyria. Alternatively spliced transcript variants encoding different isoforms have been described. ref cite web title Entrez Gene HMBS hydroxymethylbilane synthase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 3145 accessdate ref Image Heme synthesis.png center framed Heme synthesis&mdash note that some reactions occur in the cytoplasm and some in the mitochondrion yellow Older sources categorize it under EC number 4.3.1.8 . References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Deybach JC, Puy H title Porphobilinogen deaminase gene structure and molecular defects. journal J. Bioenerg. Biomembr. volume 27 issue 2 pages ... title Molecular basis of acute intermittent porphyria mutations and polymorphisms in the human hydroxymethylbilane ... resolved and static ensemble structural chemistry of hydroxymethylbilane synthase. journal Faraday ..., et al. title Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine ... http www.ncbi.nlm.nih.gov books NBK1193 GeneReviews NCBI NIH UW entry on Hydroxymethylbilane Synthase ... more details
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 fa it Porfobilinogeno ja zh ... more details
Infobox disease Name Gunther disease Image Hydroxymethylbilane.svg Caption Hydroxymethylbilane , precursor to uroporphyrinogen III . DiseasesDB 3048 ICD10 ICD10 E 80 0 e 70 ICD9 ICD9 277.1 ICDO OMIM 263700 MedlinePlus eMedicineSubj derm eMedicineTopic 145 MeshID D017092 Gunther disease , also known as congenital erythropoietic porphyria CEP , uroporphyrinogen III synthase deficiency and UROS deficiency , ref name omim OMIM 263700 ref ref name Andrews cite book author James, William D. Berger, Timothy G. et al. title Andrews Diseases of the Skin clinical Dermatology publisher Saunders Elsevier location year 2006 pages 526 isbn 0 7216 2921 0 ref is a congenital form of erythropoietic porphyria . It is a rare, autosome autosomal dominance genetics recessive ref name gdar cite journal pmid 2331520 year 1990 author Deybach JC, De Verneuil H, Boulechfar S, Grandchamp B, Nordmann Y title Point mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria Gunther s disease volume 75 issue 9 pages 1763 5 issn 0006 4971 journal Blood ref inborn errors of metabolism metabolic disorder affecting heme , caused by deficiency of the enzyme uroporphyrinogen cosynthetase . ref name pmid18179890 cite journal author Robert Richard E, Moreau Gaudry F, Lalanne M, et al. title Effective gene therapy of mice with congenital erythropoietic porphyria is facilitated by a survival advantage of corrected erythroid cells journal Am. J. Hum. Genet. volume 82 issue 1 pages 113 24 year 2008 month January pmid 18179890 pmc 2253957 doi 10.1016 j.ajhg.2007.09.007 url ref It is extremely rare, with a prevalence estimated at 1 in 1,000,000 or less. ref cite doi 10.1136 bmj.320.7250.1647 ref Genetics Image Autorecessive.jpg thumb left Gunther disease has an autosomal recessive pattern of heredity inheritance . Gunther disease is caused by mutations in the gene that encodes the enzyme uroporphyrinogen III synthase UROS , located at human chromosome chromosome 10 human 10q25.2 ... 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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