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Human Metabolome Database Version 2.5

 

Showing metabocard for Hydroxymethylbilane (HMDB01137)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:31
Accession Number HMDB01137
Secondary Accession Numbers Not Available
Common Name Hydroxymethylbilane
Description Hydroxymethylbilane 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. -- Wikipedia
Synonyms
  1. 3,8,13,18-tetrakis(carboxymethyl)-19-(hydroxymethyl)bilane-2,7,12,17-tetrapropanoate
  2. 3,8,13,18-tetrakis(carboxymethyl)-19-(hydroxymethyl)bilane-2,7,12,17-tetrapropanoic acid
  3. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,22,23,24-hexahydro-19-(hydroxymethyl)-21H-Biline-2,7,12,17-tetrapropanoate
  4. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,22,23,24-hexahydro-19-(hydroxymethyl)-21H-Biline-2,7,12,17-tetrapropanoic acid
  5. 3-[2-[[4-(2-carboxyethyl)-5-[[4-(2-carboxyethyl)-5-[[4-(2-carboxyethyl)-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-4-(carboxymethyl)-5-(hydroxymethyl)-1H-pyrrol-3-yl]propanoate
  6. 3-[2-[[4-(2-carboxyethyl)-5-[[4-(2-carboxyethyl)-5-[[4-(2-carboxyethyl)-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-4-(carboxymethyl)-5-(hydroxymethyl)-1H-pyrrol-3-yl]propanoic acid
  7. Preuroporphyrinogen
  8. hydroxymethylbilane
Chemical IUPAC Name 3-[2-[[4-(2-carboxyethyl)-5-[[4-(2-carboxyethyl)-5-[[4-(2-carboxyethyl)-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-3-(carboxymethyl)-1H-pyrrol-2-yl]methyl]-4-(carboxymethyl)-5-(hydroxymethyl)-1H-pyrrol-3-yl]propanoic acid
Chemical Formula C40H46N4O17
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Porphyrins
Sub Class
  • Bilirubins
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Porphyrin and chlorophyll metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 854.810
Monoisotopic Molecular Weight 854.285767
Isomeric SMILES OCC1=C(CC(O)=O)C(CCC(O)=O)=C(CC2=C(CC(O)=O)C(CCC(O)=O)=C(CC3=C(CC(O)=O)C(CCC(O)=O)=C(CC4=C(CC(O)=O)C(CCC(O)=O)=CN4)N3)N2)N1
Canonical SMILES OCC1=C(CC(O)=O)C(CCC(O)=O)=C(CC2=C(CC(O)=O)C(CCC(O)=O)=C(CC3=C(CC(O)=O)C(CCC(O)=O)=C(CC4=C(CC(O)=O)C(CCC(O)=O)=CN4)N3)N2)N1
KEGG Compound ID C01024 Link Image
BioCyc ID HYDROXYMETHYLBILANE Link Image
BiGG ID 36648 Link Image
Wikipedia Link Hydroxymethylbilane Link Image
NuGOwiki Link HMDB01137 Link Image
Metagene Link HMDB01137 Link Image
METLIN ID 3699 Link Image
PubChem Compound 788 Link Image
PubChem Substance 2811 Link Image
ChEBI ID 16645 Link Image
CAS Registry Number 73023-76-4
InChI Identifier 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)
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0323 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -8
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.53 [Predicted by ALOGPS]; -2.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Uroporphyrinogen-III synthase
  2. Porphobilinogen deaminase
  3. cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase
  4. cDNA, FLJ95799, Homo sapiens uroporphyrinogen III synthase (congenitalerythropoietic porphyria) (UROS), mRNA (Uroporphyrinogen III synthase (Congenital erythropoietic porphyria), isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5593
Enzyme 1 Name Uroporphyrinogen-III synthase
Enzyme 1 Synonyms
  1. UROS
  2. Uroporphyrinogen- III cosynthetase
  3. Hydroxymethylbilane hydrolyase [cyclizing]
  4. UROIIIS
Enzyme 1 Gene Name UROS
Enzyme 1 Protein Sequence >Uroporphyrinogen-III synthase 
MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLI
FTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCG
NAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNL
NSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVS
CTAESPTPQALATGIRKALQPHGCC
Enzyme 1 Number of Residues 265
Enzyme 1 Molecular Weight 28628
Enzyme 1 Theoretical pI 5.16
Enzyme 1 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Hydroxymethylbilane = uroporphyrinogen III + H(2)O
Enzyme 1 Pathways
Enzyme 1 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 337463 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P10746 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HEM4_HUMAN Link Image
Enzyme 1 PDB ID 1JR2 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >798 bp 
ATGAAGGTTCTTTTACTGAAGGATGCGAAGGAAGATGACTGTGGCCAGGATCCGTATATC
AGGGAATTAGGATTATATGGACTTGAAGCCACTTTGATCCCTGTTTTATCGTTTGAGTTT
TTGTCTCTTCCCAGTTTCTCTGAGAAGCTTTCTCATCCTGAAGATTACGGGGGACTCATT
TTTACCAGCCCCAGAGCAGTGGAAGCAGCAGAGTTATGTTTGGAGCAAAACAATAAAACT
GAAGTCTGGGAAAGGTCTCTGAAAGAAAAATGGAATGCCAAGTCAGTGTATGTGGTTGGA
AATGCTACTGCTTCTCTAGTGAGTAAAATTGGCCTGGATACAGAAGGAGAAACCTGTGGA
AATGCAGAAAAGCTTGCAGAATATATTTGTTCCAGGGAGTCCTCAGCACTGCCTCTTCTA
TTTCCCTGTGGAAACCTCAAAAGAGAAATCCTGCCAAAAGCGCTCAAGGACAAAGGGATT
GCCATGGAAAGCATAACTGTGTATCAGACAGTTGCACACCCAGGAATCCAAGGGAACCTG
AACAGCTACTATTCCCAGCAGGGGGTTCCAGCCAGCATCACATTTTTTAGTCCCTCTGGC
CTCACATACAGTCTCAAGCACATTCAGGAGTTATCTGGTGACAATATCGATCAAATTAAG
TTTGCAGCCATCGGCCCCACTACGGCTCGCGCGCTGGCCGCCCAGGGCCTTCCTGTAAGC
TGCACTGCAGAGAGCCCCACGCCACAAGCCCTGGCCACTGGCATCAGGAAGGCTCTCCAG
CCCCATGGCTGCTGCTGA
Enzyme 1 GenBank Gene ID J03824 Link Image
Enzyme 1 GeneCard ID UROS Link Image
Enzyme 1 GenAtlas ID UROS Link Image
Enzyme 1 HGNC ID HGNC:12592 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10q25.2-q26.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Tsai SF, Bishop DF, Desnick RJ: Human uroporphyrinogen III synthase: molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7049-53. [PubMed Link Image]
  2. Xu W, Astrin KH, Desnick RJ: Molecular basis of congenital erythropoietic porphyria: mutations in the human uroporphyrinogen III synthase gene. Hum Mutat. 1996;7(3):187-92. [PubMed Link Image]
  3. Deybach JC, de Verneuil H, Boulechfar S, Grandchamp B, Nordmann Y: Point mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria (Gunther's disease). Blood. 1990 May 1;75(9):1763-5. [PubMed Link Image]
  4. Boulechfar S, Da Silva V, Deybach JC, Nordmann Y, Grandchamp B, de Verneuil H: Heterogeneity of mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria. Hum Genet. 1992 Jan;88(3):320-4. [PubMed Link Image]
  5. Warner CA, Yoo HW, Roberts AG, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of exonic mutations in the uroporphyrinogen III synthase gene. J Clin Invest. 1992 Feb;89(2):693-700. [PubMed Link Image]
  6. Xu W, Warner CA, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of 10 mutations in the uroporphyrinogen III synthase gene. J Clin Invest. 1995 Feb;95(2):905-12. [PubMed Link Image]
  7. Tanigawa K, Bensidhoum M, Takamura N, Namba H, Yamashita S, de Verneuil H, Ged C: A novel point mutation in congenital erythropoietic porphyria in two members of Japanese family. Hum Genet. 1996 May;97(5):557-60. [PubMed Link Image]
  8. Tezcan I, Xu W, Gurgey A, Tuncer M, Cetin M, Oner C, Yetgin S, Ersoy F, Aizencang G, Astrin KH, Desnick RJ: Congenital erythropoietic porphyria successfully treated by allogeneic bone marrow transplantation. Blood. 1998 Dec 1;92(11):4053-8. [PubMed Link Image]
  9. Frank J, Wang X, Lam HM, Aita VM, Jugert FK, Goerz G, Merk HF, Poh-Fitzpatrick MB, Christiano AM: C73R is a hotspot mutation in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria. Ann Hum Genet. 1998 May;62(Pt 3):225-30. [PubMed Link Image]
  10. Rogounovitch T, Takamura N, Hombrados I, Morel C, Tanaka T, Kameyoshi Y, Shimizu-Yoshida Y, de Verneuil H, Yamashita S: Congenital erythropoietic porphyria: a novel homozygous mutation in a Japanese patient. J Invest Dermatol. 2000 Dec;115(6):1156. [PubMed Link Image]
  11. Shady AA, Colby BR, Cunha LF, Astrin KH, Bishop DF, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of eight novel mutations in the uroporphyrinogen III synthase gene. Br J Haematol. 2002 Jun;117(4):980-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5594
Enzyme 2 Name Porphobilinogen deaminase
Enzyme 2 Synonyms
  1. Hydroxymethylbilane synthase
  2. HMBS
  3. Pre-uroporphyrinogen synthase
  4. PBG-D
Enzyme 2 Gene Name HMBS
Enzyme 2 Protein Sequence >Porphobilinogen deaminase 
MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG
DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH
DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQ
QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH
VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA
H
Enzyme 2 Number of Residues 361
Enzyme 2 Molecular Weight 39331
Enzyme 2 Theoretical pI 7.19
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydroxymethylbilane synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 35307 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P08397 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HEM3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1035 bp 
ATGAGAGTGATTCGCGTGGGTACCCGCAAGAGCCAGCTTGCTCGCATACAGACGGACAGT
GTGGTGGCAACATTGAAAGCCTCGTACCCTGGCCTGCAGTTTGAAATCATTGCTATGTCC
ACCACAGGGGACAAGATTCTTGATACTGCACTCTCTAAGATTGGAGAGAAAAGCCTGTTT
ACCAAGGAGCTTGAACATGCCCTGGAGAAGAATGAAGTGGACCTGGTTGTTCACTCCTTG
AAGGACCTGCCCACTGTGCTTCCTCCTGGCTTCACCATCGGAGCCATCTGCAAGCGGGAA
AACCCTCATGATGCTGTTGTCTTTCACCCAAAATTTGTTGGGAAGACCCTAGAAACCCTG
CCAGAGAAGAGTGTGGTGGGAACCAGCTCCCTGCGAAGAGCAGCCCAGCTGCAGAGAAAG
TTCCCGCATCTGGAGTTCAGGAGTATTCGGGGAAACCTCAACACCCGGCTTCGGAAGCTG
GACGAGCAGCAGGAGTTCAGTGCCATCATCCTAGCAACAGCTGGCCTGCAGCGCATGGGC
TGGCACAACCGGGTTGGGCAGATCCTGCACCCTGAGGAATGCATGTATGCTGTGGGCCAG
GGGGCCTTGGGCGTGGAAGTGCGAGCCAAGGACCAGGACATCTTGGATCTGGTGGGTGTG
CTGCACGATCCCGAGACTCTGCTTCGCTGCATCGCTGAAAGGGCCTTCCTGAGGCACCTG
GAAGGAGGCTGCAGTGTGCCAGTAGCCGTGCATACAGCTATGAAGGATGGGCAACTGTAC
CTGACTGGAGGAGTCTGGAGTCTAGACGGCTCAGATAGCATACAAGAGACCATGCAGGCT
ACCATCCATGTCCCTGCCCAGCATGAAGATGGCCCTGAGGATGACCCACAGTTGGTAGGC
ATCACTGCTCGTAACATTCCACGAGGGCCCCAGTTGGCTGCCCAGAACTTGGGCATCAGC
CTGGCCAACTTGTTGCTGAGCAAAGGAGCCAAAACCATCCTGGATGTTGCACGGCAGCTT
AACGATGCCCATTAA
Enzyme 2 GenBank Gene ID X04217 Link Image
Enzyme 2 GeneCard ID HMBS Link Image
Enzyme 2 GenAtlas ID HMBS Link Image
Enzyme 2 HGNC ID HGNC:4982 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11q23.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Raich N, Romeo PH, Dubart A, Beaupain D, Cohen-Solal M, Goossens M: Molecular cloning and complete primary sequence of human erythrocyte porphobilinogen deaminase. Nucleic Acids Res. 1986 Aug 11;14(15):5955-68. [PubMed Link Image]
  2. Grandchamp B, De Verneuil H, Beaumont C, Chretien S, Walter O, Nordmann Y: Tissue-specific expression of porphobilinogen deaminase. Two isoenzymes from a single gene. Eur J Biochem. 1987 Jan 2;162(1):105-10. [PubMed Link Image]
  3. Yoo HW, Warner CA, Chen CH, Desnick RJ: Hydroxymethylbilane synthase: complete genomic sequence and amplifiable polymorphisms in the human gene. Genomics. 1993 Jan;15(1):21-9. [PubMed Link Image]
  4. Chretien S, Dubart A, Beaupain D, Raich N, Grandchamp B, Rosa J, Goossens M, Romeo PH: Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. Proc Natl Acad Sci U S A. 1988 Jan;85(1):6-10. [PubMed Link Image]
  5. Lannfelt L, Wetterberg L, Lilius L, Thunell S, Jornvall H, Pavlu B, Wielburski A, Gellerfors P: Porphobilinogen deaminase in human erythrocytes: purification of two forms with apparent molecular weights of 40 kDa and 42 kDa. Scand J Clin Lab Invest. 1989 Nov;49(7):677-84. [PubMed Link Image]
  6. Astrin KH, Desnick RJ: Molecular basis of acute intermittent porphyria: mutations and polymorphisms in the human hydroxymethylbilane synthase gene. Hum Mutat. 1994;4(4):243-52. [PubMed Link Image]
  7. Delfau MH, Picat C, de Rooij FW, Hamer K, Bogard M, Wilson JH, Deybach JC, Nordmann Y, Grandchamp B: Two different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyria. J Clin Invest. 1990 Nov;86(5):1511-6. [PubMed Link Image]
  8. Delfau MH, Picat C, De Rooij F, Voortman G, Deybach JC, Nordmann Y, Grandchamp B: Molecular heterogeneity of acute intermittent porphyria: identification of four additional mutations resulting in the CRIM-negative subtype of the disease. Am J Hum Genet. 1991 Aug;49(2):421-8. [PubMed Link Image]
  9. Gu XF, de Rooij F, Voortman G, Te Velde K, Nordmann Y, Grandchamp B: High frequency of mutations in exon 10 of the porphobilinogen deaminase gene in patients with a CRIM-positive subtype of acute intermittent porphyria. Am J Hum Genet. 1992 Sep;51(3):660-5. [PubMed Link Image]
  10. Mgone CS, Lanyon WG, Moore MR, Connor JM: Detection of seven point mutations in the porphobilinogen deaminase gene in patients with acute intermittent porphyria, by direct sequencing of in vitro amplified cDNA. Hum Genet. 1992 Sep-Oct;90(1-2):12-6. [PubMed Link Image]
  11. Kauppinen R, Peltonen L, Pihlaja H, Mustajoki P: CRIM-positive mutations of acute intermittent porphyria in Finland. Hum Mutat. 1992;1(5):392-6. [PubMed Link Image]
  12. Mgone CS, Lanyon WG, Moore MR, Louie GV, Connor JM: Detection of a high mutation frequency in exon 12 of the porphobilinogen deaminase gene in patients with acute intermittent porphyria. Hum Genet. 1993 Dec;92(6):619-22. [PubMed Link Image]
  13. Llewellyn DH, Whatley S, Elder GH: Acute intermittent porphyria caused by an arginine to histidine substitution (R26H) in the cofactor-binding cleft of porphobilinogen deaminase. Hum Mol Genet. 1993 Aug;2(8):1315-6. [PubMed Link Image]
  14. Gu XF, de Rooij F, de Baar E, Bruyland M, Lissens W, Nordmann Y, Grandchamp B: Two novel mutations of the porphobilinogen deaminase gene in acute intermittent porphyria. Hum Mol Genet. 1993 Oct;2(10):1735-6. [PubMed Link Image]
  15. Gu XF, de Rooij F, Voortman G, Te Velde K, Deybach JC, Nordmann Y, Grandchamp B: Detection of eleven mutations causing acute intermittent porphyria using denaturing gradient gel electrophoresis. Hum Genet. 1994 Jan;93(1):47-52. [PubMed Link Image]
  16. Lundin G, Wedell A, Thunell S, Anvret M: Two new mutations in the porphobilinogen deaminase gene and a screening method using PCR amplification of specific alleles. Hum Genet. 1994 Jan;93(1):59-62. [PubMed Link Image]
  17. Mgone CS, Lanyon WG, Moore MR, Louie GV, Connor JM: Identification of five novel mutations in the porphobilinogen deaminase gene. Hum Mol Genet. 1994 May;3(5):809-11. [PubMed Link Image]
  18. Chen CH, Astrin KH, Lee G, Anderson KE, Desnick RJ: Acute intermittent porphyria: identification and expression of exonic mutations in the hydroxymethylbilane synthase gene. An initiation codon missense mutation in the housekeeping transcript causes "variant acute intermittent porphyria" with normal expression of the erythroid-specific enzyme. J Clin Invest. 1994 Nov;94(5):1927-37. [PubMed Link Image]
  19. Kauppinen R, Mustajoki S, Pihlaja H, Peltonen L, Mustajoki P: Acute intermittent porphyria in Finland: 19 mutations in the porphobilinogen deaminase gene. Hum Mol Genet. 1995 Feb;4(2):215-22. [PubMed Link Image]
  20. Lundin G, Hashemi J, Floderus Y, Thunell S, Sagen E, Laegreid A, Wassif W, Peters T, Anvret M: Four mutations in the porphobilinogen deaminase gene in patients with acute intermittent porphyria. J Med Genet. 1995 Dec;32(12):979-81. [PubMed Link Image]
  21. Puy H, Deybach JC, Lamoril J, Robreau AM, Da Silva V, Gouya L, Grandchamp B, Nordmann Y: Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria. Am J Hum Genet. 1997 Jun;60(6):1373-83. [PubMed Link Image]
  22. Lundin G, Lee JS, Thunell S, Anvret M: Genetic investigation of the porphobilinogen deaminase gene in Swedish acute intermittent porphyria families. Hum Genet. 1997 Jul;100(1):63-6. [PubMed Link Image]
  23. Mustajoki S, Pihlaja H, Ahola H, Petersen NE, Mustajoki P, Kauppinen R: Three splicing defects, an insertion, and two missense mutations responsible for acute intermittent porphyria. Hum Genet. 1998 May;102(5):541-8. [PubMed Link Image]
  24. Ong PM, Lanyon WG, Hift RJ, Halkett J, Cramp CE, Moore MR, Connor JM: Identification of two novel mutations in the hydroxymethylbilane synthase gene in three patients from two unrelated families with acute intermittent porphyria. Hum Hered. 1998 Jan-Feb;48(1):24-9. [PubMed Link Image]
  25. De Siervi A, Rossetti MV, Parera VE, Astrin KH, Aizencang GI, Glass IA, Batlle AM, Desnick RJ: Identification and characterization of hydroxymethylbilane synthase mutations causing acute intermittent porphyria: evidence for an ancestral founder of the common G111R mutation. Am J Med Genet. 1999 Oct 8;86(4):366-75. [PubMed Link Image]
  26. Whatley SD, Woolf JR, Elder GH: Comparison of complementary and genomic DNA sequencing for the detection of mutations in the HMBS gene in British patients with acute intermittent porphyria: identification of 25 novel mutations. Hum Genet. 1999 Jun;104(6):505-10. [PubMed Link Image]
  27. De Siervi A, Mendez M, Parera VE, Varela L, Batlle AM, Rossetti MV: Acute intermittent porphyria: characterization of two novel mutations in the porphobilinogen deaminase gene, one amino acid deletion (453-455delAGC) and one splicing aceptor site mutation (IVS8-1G>T). Hum Mutat. 1999 Oct;14(4):355. [PubMed Link Image]
  28. Gross U, Puy H, Doss M, Robreau AM, Nordmann Y, Doss MO, Deybach JC: New mutations of the hydroxymethylbilane synthase gene in German patients with acute intermittent porphyria. Mol Cell Probes. 1999 Dec;13(6):443-7. [PubMed Link Image]
  29. Robreau-Fraolini AM, Puy H, Aquaron C, Bogard C, Traore M, Nordmann Y, Aquaron R, Deybach JC: Porphobilinogen deaminase gene in African and Afro-Caribbean ethnic groups: mutations causing acute intermittent porphyria and specific intragenic polymorphisms. Hum Genet. 2000 Aug;107(2):150-9. [PubMed Link Image]
  30. Schneider-Yin X, Bogard C, Rufenacht UB, Puy H, Nordmann Y, Minder EI, Deybach J: Identification of a prevalent nonsense mutation (W283X) and two novel mutations in the porphobilinogen deaminase gene of Swiss patients with acute intermittent porphyria. Hum Hered. 2000 Jul-Aug;50(4):247-50. [PubMed Link Image]
  31. De Siervi A, Weiss Cadiz DE, Parera VE, del C Batlle AM, Rossetti MV: Identification and characterization of two novel mutations that produce acute intermittent porphyria: A 3-base deletion (841-843delGGA) and a missense mutation (T35M). Hum Mutat. 2000 Oct;16(4):373. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13087
Enzyme 3 Name cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase
Enzyme 3 Synonyms
  1. HMBS, mRNA
  2. Hydroxymethylbilane synthase, isoform CRA_a
Enzyme 3 Gene Name HMBS
Enzyme 3 Protein Sequence >cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase 
MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG
DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH
DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQ
QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH
VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA
H
Enzyme 3 Number of Residues 361
Enzyme 3 Molecular Weight 39331
Enzyme 3 Theoretical pI 7.19
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158261573 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A8K2L0 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A8K2L0_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AK290275 Link Image
Enzyme 3 GeneCard ID A8K2L0 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16714
Enzyme 4 Name cDNA, FLJ95799, Homo sapiens uroporphyrinogen III synthase (congenitalerythropoietic porphyria) (UROS), mRNA (Uroporphyrinogen III synthase (Congenital erythropoietic porphyria), isoform CRA_a)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name UROS
Enzyme 4 Protein Sequence >cDNA, FLJ95799, Homo sapiens uroporphyrinogen III synthase (congenitalerythropoietic porphyria) (UROS), mRNA (Uroporphyrinogen III synthase (Congenital erythropoietic porphyria), isoform CRA_a) 
MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLI
FTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCG
NAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNL
NSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVS
CTAESPTPQALATGIRKALQPHGCC
Enzyme 4 Number of Residues 265
Enzyme 4 Molecular Weight 28628
Enzyme 4 Theoretical pI 5.16
Enzyme 4 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B2RC13 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B2RC13_HUMAN Link Image
Enzyme 4 PDB ID 1JR2 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK314896 Link Image
Enzyme 4 GeneCard ID B2RC13 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location 10
Enzyme 4 Locus 10q25.2-q26.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available