| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-11-25 11:09:26 |
| Accession Number |
HMDB00245 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Porphobilinogen |
| Description |
Porphobilinogen is a pyrrole involved in porphyrin metabolism. -- Wikipedia; It consists of a pyrrole ring with acetyl, propionyl, and aminomethyl side chains; It is a key monopyrrolic intermediate in porphyrin, chlorophyll and vitamin B12 biosynthesis. Porphobilinogen is generated by the enzyme ALA dehydratase by combining two molecules of dALA together, and converted into hydroxymethyl bilane by the enzyme porphobilinogen deaminase. 4 molecules of porphobilinogen are condensed to form one molecule of uroporphyrinogen III, which is then converted successively to coproporphyrinogen III, protoporphyrin IX, and heme. Porphobilinogen is produced in excess and excreted in the urine in acute intermittent porphyria and several other porphyrias. |
| Synonyms |
- 5-(aminomethyl)-4-(carboxymethyl)-Pyrrole-3-propionate
- 5-(aminomethyl)-4-(carboxymethyl)-Pyrrole-3-propionic acid
- PBG
- Porphobilinogen
|
| Chemical IUPAC Name |
3-[5-(aminomethyl)-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid |
| Chemical Formula |
C10H14N2O4 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- primary amine
- primary aliphatic amine (alkylamine)
- carboxylic acid
- aromatic compound
- heterocyclic compound
|
| Biofunction |
- Component of Porphyrin and chlorophyll metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
226.229 |
| Monoisotopic Molecular Weight |
226.095352 |
| Isomeric SMILES |
NCC1=C(CC(O)=O)C(CCC(O)=O)=CN1 |
| Canonical SMILES |
NCC1=C(CC(O)=O)C(CCC(O)=O)=CN1 |
| KEGG Compound ID |
C00931  |
| BioCyc ID |
PORPHOBILINOGEN  |
| BiGG ID |
36404  |
| Wikipedia Link |
Porphobilinogen  |
| NuGOwiki Link |
HMDB00245  |
| Metagene Link |
HMDB00245  |
| METLIN ID |
76  |
| PubChem Compound |
1021  |
| PubChem Substance |
153515  |
| ChEBI ID |
17381  |
| CAS Registry Number |
487-90-1 |
| InChI Identifier |
InChI=1/C10H14N2O4/c11-4-8-7(3-10(15)16)6(5-12-8)1-2-9(13)14/h5,12H,1-4,11H2,(H,13,14)(H,15,16) |
| Synthesis Reference |
Frydman, Benjamin; Despuy, Maria E.; Rapoport, Henry. Pyrroles from azaindoles. A synthesis of porphobilinogen. Journal of the American Chemical Society (1965), 87(15), 3530-1. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
1000.0 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 2.72 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.40 [Predicted by ALOGPS]; -1.2 [Predicted by PubChem via XLOGP]; -4.46 [MEYLAN,WM & HOWARD,PH (1995)]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| 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 |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
|
| Biofluid Location |
|
| Tissue Location |
| Tissue |
References |
| Erythrocyte |
— |
| Liver |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
0.066 +/- 0.067 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
Blood |
| Value |
0.06 (0.00-0.12) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Healthy individuals |
| Comments |
Not Available |
| References |
- Floderus Y, Sardh E, Moller C, Andersson C, Rejkjaer L, Andersson DE, Harper P: Variations in porphobilinogen and 5-aminolevulinic acid concentrations in plasma and urine from asymptomatic carriers of the acute intermittent porphyria gene with increased porphyrin precursor excretion. Clin Chem. 2006 Apr;52(4):701-7. Epub 2006 Feb 23. [PubMed
]
|
| Biofluid |
Urine |
| Value |
<=0.579 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
|
| Biofluid |
Urine |
| Value |
0.31 +/- 0.13 umol/mmol creatinine |
| Age |
Children:1-13 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
- West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
- Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
0.29 +/- 0.14 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
- West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
- Basel, Switzerland c1981-1992.
|
|
| Concentrations (Abnormal) |
| Biofluid |
Blood |
| Value |
3.1 +/- 1.0 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Porphyria |
| Comments |
Acute intermittent porphyria gene carriers
n=10 (5 men and 5 women) |
| References |
- Floderus Y, Sardh E, Moller C, Andersson C, Rejkjaer L, Andersson DE, Harper P: Variations in porphobilinogen and 5-aminolevulinic acid concentrations in plasma and urine from asymptomatic carriers of the acute intermittent porphyria gene with increased porphyrin precursor excretion. Clin Chem. 2006 Apr;52(4):701-7. Epub 2006 Feb 23. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Porphyria |
- Floderus Y, Sardh E, Moller C, Andersson C, Rejkjaer L, Andersson DE, Harper P: Variations in porphobilinogen and 5-aminolevulinic acid concentrations in plasma and urine from asymptomatic carriers of the acute intermittent porphyria gene with increased porphyrin precursor excretion. Clin Chem. 2006 Apr;52(4):701-7. Epub 2006 Feb 23. [PubMed
]
|
|
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Dhar GJ, Bossenmaier I, Petryka ZJ, Cardinal R, Watson CJ: Effects of hematin in hepatic porphyria. Further studies. Ann Intern Med. 1975 Jul;83(1):20-30. [PubMed
]
- Ivanov E, Pisanets M: Studies on the biosynthesis of porphyrins in erythrocytes after incubation with delta-aminolevulinic acid: an attempt to investigate the pathogenesis of nephrogenic anemia. Acta Biol Med Ger. 1982;41(4):307-13. [PubMed
]
- Ellencweig N, Schoenfeld N, Zemishlany Z: Acute intermittent porphyria: psychosis as the only clinical manifestation. Isr J Psychiatry Relat Sci. 2006;43(1):52-6. [PubMed
]
- Buchet JP, Lauwerys R, Hassoun A, Dratwa M, Wens R, Collart F, Tielemans C: Effect of aluminum on porphyrin metabolism in hemodialyzed patients. Nephron. 1987;46(4):360-3. [PubMed
]
- Tishler PV, Woodward B, O'Connor J, Holbrook DA, Seidman LJ, Hallett M, Knighton DJ: High prevalence of intermittent acute porphyria in a psychiatric patient population. Am J Psychiatry. 1985 Dec;142(12):1430-6. [PubMed
]
- Hsiao KJ, Lee FY, Wu SJ, Chang WJ: Determination of erythrocyte porphobilinogen deaminase activity using porphobilinogen as substrate. Clin Chim Acta. 1987 Sep 30;168(2):257-8. [PubMed
]
- Evans J, Lefkowitch J, Lim CK, Billing B: Fecal porphyrin abnormalities in a patient with features of Rotor's syndrome. Gastroenterology. 1981 Dec;81(6):1125-30. [PubMed
]
- Sassa S, Solish G, Levere RD, Kappas A: Studies in porphyria. IV. Expression of the gene defect of acute intermittent porphyria in cultured human skin fibroblasts and amniotic cells: prenatal diagnosis of the porphyric trait. J Exp Med. 1975 Sep 1;142(3):722-31. [PubMed
]
- Ford RE, Ou CN, Ellefson RD: Assay for erythrocyte uroporphyrinogen I synthase activity, with porphobilinogen as substrate. Clin Chem. 1980 Jul;26(8):1182-5. [PubMed
]
- Shiue JW, Lee FY, Hsiao KJ, Tsai YT, Lee SD, Wu SJ: Abnormal thyroid function and hypercholesterolemia in a case of acute intermittent porphyria. Taiwan Yi Xue Hui Za Zhi. 1989 Jul;88(7):729-31. [PubMed
]
- Mustajoki P: Normal erythrocyte uroporphyrinogen I synthase in a kindred with acute intermittent porphyria. Ann Intern Med. 1981 Aug;95(2):162-6. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Porphobilinogen deaminase
- Delta-aminolevulinic acid dehydratase
- CDNA FLJ16678 fis, clone TLIVE2002046, highly similar to DELTA- AMINOLEVULINIC ACID DEHYDRATASE
- cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase
- cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5594 |
| Enzyme 1 Name |
Porphobilinogen deaminase |
| Enzyme 1 Synonyms |
- Hydroxymethylbilane synthase
- HMBS
- Pre-uroporphyrinogen synthase
- PBG-D
|
| Enzyme 1 Gene Name |
HMBS |
| Enzyme 1 Protein Sequence |
>Porphobilinogen deaminase
MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG
DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH
DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQ
QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH
VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA
H
|
| Enzyme 1 Number of Residues |
361 |
| Enzyme 1 Molecular Weight |
39331 |
| Enzyme 1 Theoretical pI |
7.19 |
| Enzyme 1 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 1 General Function |
Coenzyme transport and metabolism |
| Enzyme 1 Specific Function |
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- 4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
35307  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P08397  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
HEM3_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1035 bp
ATGAGAGTGATTCGCGTGGGTACCCGCAAGAGCCAGCTTGCTCGCATACAGACGGACAGT
GTGGTGGCAACATTGAAAGCCTCGTACCCTGGCCTGCAGTTTGAAATCATTGCTATGTCC
ACCACAGGGGACAAGATTCTTGATACTGCACTCTCTAAGATTGGAGAGAAAAGCCTGTTT
ACCAAGGAGCTTGAACATGCCCTGGAGAAGAATGAAGTGGACCTGGTTGTTCACTCCTTG
AAGGACCTGCCCACTGTGCTTCCTCCTGGCTTCACCATCGGAGCCATCTGCAAGCGGGAA
AACCCTCATGATGCTGTTGTCTTTCACCCAAAATTTGTTGGGAAGACCCTAGAAACCCTG
CCAGAGAAGAGTGTGGTGGGAACCAGCTCCCTGCGAAGAGCAGCCCAGCTGCAGAGAAAG
TTCCCGCATCTGGAGTTCAGGAGTATTCGGGGAAACCTCAACACCCGGCTTCGGAAGCTG
GACGAGCAGCAGGAGTTCAGTGCCATCATCCTAGCAACAGCTGGCCTGCAGCGCATGGGC
TGGCACAACCGGGTTGGGCAGATCCTGCACCCTGAGGAATGCATGTATGCTGTGGGCCAG
GGGGCCTTGGGCGTGGAAGTGCGAGCCAAGGACCAGGACATCTTGGATCTGGTGGGTGTG
CTGCACGATCCCGAGACTCTGCTTCGCTGCATCGCTGAAAGGGCCTTCCTGAGGCACCTG
GAAGGAGGCTGCAGTGTGCCAGTAGCCGTGCATACAGCTATGAAGGATGGGCAACTGTAC
CTGACTGGAGGAGTCTGGAGTCTAGACGGCTCAGATAGCATACAAGAGACCATGCAGGCT
ACCATCCATGTCCCTGCCCAGCATGAAGATGGCCCTGAGGATGACCCACAGTTGGTAGGC
ATCACTGCTCGTAACATTCCACGAGGGCCCCAGTTGGCTGCCCAGAACTTGGGCATCAGC
CTGGCCAACTTGTTGCTGAGCAAAGGAGCCAAAACCATCCTGGATGTTGCACGGCAGCTT
AACGATGCCCATTAA
|
| Enzyme 1 GenBank Gene ID |
X04217  |
| Enzyme 1 GeneCard ID |
HMBS  |
| Enzyme 1 GenAtlas ID |
HMBS  |
| Enzyme 1 HGNC ID |
HGNC:4982  |
| Enzyme 1 Chromosome Location |
11 |
| Enzyme 1 Locus |
11q23.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6349 |
| Enzyme 2 Name |
Delta-aminolevulinic acid dehydratase |
| Enzyme 2 Synonyms |
- Porphobilinogen synthase
- ALADH
|
| Enzyme 2 Gene Name |
ALAD |
| Enzyme 2 Protein Sequence |
>Delta-aminolevulinic acid dehydratase
MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKR
LEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACD
VCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKE
ALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDR
DVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAV
LEAMTAFRRAGADIIITYYTPQLLQWLKEE
|
| Enzyme 2 Number of Residues |
330 |
| Enzyme 2 Molecular Weight |
36295 |
| Enzyme 2 Theoretical pI |
6.78 |
| Enzyme 2 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- hydro-lyase activity
- lyase activity
- porphobilinogen synthase activity
|
| Process |
- cellular metabolism
- heme biosynthesis
- heterocycle metabolism
- metabolism
- physiological process
- porphyrin biosynthesis
- porphyrin metabolism
|
| Component |
| — |
|
| Enzyme 2 General Function |
Coenzyme transport and metabolism |
| Enzyme 2 Specific Function |
2 5-aminolevulinate = porphobilinogen + 2 H(2)O |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 2 5-aminolevulinate = porphobilinogen + 2 H2O
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
178329  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P13716  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
HEM2_HUMAN  |
| Enzyme 2 PDB ID |
1E51  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>993 bp
ATGCAGCCCCAGTCCGTTCTGCACAGCGGCTACTTCCACCCACTACTTCGGGCCTGGCAG
ACAGCCACCACCACCCTCAATGCCTCCAACCTCATCTACCCCATCTTTGTCACGGATGTT
CCTGATGACATACAGCCTATCACCAGCCTCCCAGGAGTGGCCAGGTATGGTGTGAAGCGG
CTGGAAGAGATGCTGAGGCCCTTGGTGGAAGAGGGCCTACGCTGTGTCTTGATCTTTGGC
GTCCCCAGCAGAGTTCCCAAGGACGAGCGGGGTTCCGCAGCTGACTCCGAGGAGTCCCCA
GCTATTGAGGCAATCCATCTGTTGAGGAAGACCTTCCCCAACCTCCTGGTGGCCTGTGAT
GTCTGCCTGTGTCCCTACACCTCCCATGGTCACTGCGGGCTCCTGAGTGAAAACGGAGCA
TTCCGGGCTGAGGAGAGCCGCCAGCGGCTGGCTGAGGTGGCATTGGCGTATGCCAAGGCA
GGATGTCAGGTGGTAGCCCCGTCGGACATGATGGATGGACGCGTGGAAGCCATCAAAGAG
GCCCTGATGGCACATGGACTTGGCAACAGGGTATCGGTGATGAGCTACAGTGCCAAATTT
GCTTCCTGTTTCTATGGCCCTTTCCGGGATGCAGCTAAGTCAAGCCCAGCTTTTGGGGAC
CGCCGCTGCTACCAGCTGCCCCCTGGAGCACGAGGCCTGGCTCTCCGAGCTGTGGACCGG
GATGTACGGGAAGGAGCTGACATGCTCATGGTGAAGCCGGGAATGCCCTACCTGGACATC
GTGCGGGAGGTAAAGGACAAGCACCCTGACCTCCCTCTCGCCGTGTACCACGTCTCTGGA
GAGTTTGCCATGCTGTGGCATGGAGCCCAGGCCGGGGCATTTGATCTCAAGGCTGCCGTA
CTGGAGGCCATGACTGCCTTCCGCAGAGCAGGTGCTGACATCATCATCACCTACTACACA
CCGCAGCTGCTGCAGTGGCTGAAGGAGGAATGA
|
| Enzyme 2 GenBank Gene ID |
M13928  |
| Enzyme 2 GeneCard ID |
ALAD  |
| Enzyme 2 GenAtlas ID |
ALAD  |
| Enzyme 2 HGNC ID |
HGNC:395  |
| Enzyme 2 Chromosome Location |
9 |
| Enzyme 2 Locus |
9q33.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Wetmur JG, Bishop DF, Cantelmo C, Desnick RJ: Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7703-7. [PubMed
]
- Astrin KH, Kaya AH, Wetmur JG, Desnick RJ: RsaI polymorphism in the human delta-aminolevulinate dehydratase gene at 9q34. Nucleic Acids Res. 1991 Aug 11;19(15):4307. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Gibbs PN, Jordan PM: Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. Biochem J. 1986 Jun 1;236(2):447-51. [PubMed
]
- Wetmur JG, Kaya AH, Plewinska M, Desnick RJ: Molecular characterization of the human delta-aminolevulinate dehydratase 2 (ALAD2) allele: implications for molecular screening of individuals for genetic susceptibility to lead poisoning. Am J Hum Genet. 1991 Oct;49(4):757-63. [PubMed
]
- Plewinska M, Thunell S, Holmberg L, Wetmur JG, Desnick RJ: delta-Aminolevulinate dehydratase deficient porphyria: identification of the molecular lesions in a severely affected homozygote. Am J Hum Genet. 1991 Jul;49(1):167-74. [PubMed
]
- Ishida N, Fujita H, Fukuda Y, Noguchi T, Doss M, Kappas A, Sassa S: Cloning and expression of the defective genes from a patient with delta-aminolevulinate dehydratase porphyria. J Clin Invest. 1992 May;89(5):1431-7. [PubMed
]
- Akagi R, Yasui Y, Harper P, Sassa S: A novel mutation of delta-aminolaevulinate dehydratase in a healthy child with 12% erythrocyte enzyme activity. Br J Haematol. 1999 Sep;106(4):931-7. [PubMed
]
- Akagi R, Shimizu R, Furuyama K, Doss MO, Sassa S: Novel molecular defects of the delta-aminolevulinate dehydratase gene in a patient with inherited acute hepatic porphyria. Hepatology. 2000 Mar;31(3):704-8. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
13082 |
| Enzyme 3 Name |
CDNA FLJ16678 fis, clone TLIVE2002046, highly similar to DELTA- AMINOLEVULINIC ACID DEHYDRATASE |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
Not Available |
| Enzyme 3 Protein Sequence |
>CDNA FLJ16678 fis, clone TLIVE2002046, highly similar to DELTA- AMINOLEVULINIC ACID DEHYDRATASE
MPPTSSTPSLSRPGLGQAGKPDTGSHPPPTISTSIFLSCFPTIPLSRPRTTGPSHSYQSI
SHPRSCRDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERG
SAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLA
EVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDA
AKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMLYLDIVREVKDKHPDL
PLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE
|
| Enzyme 3 Number of Residues |
359 |
| Enzyme 3 Molecular Weight |
39050 |
| Enzyme 3 Theoretical pI |
7.72 |
| Enzyme 3 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- hydro-lyase activity
- lyase activity
- porphobilinogen synthase activity
|
| Process |
- cellular metabolism
- heme biosynthesis
- heterocycle metabolism
- metabolism
- physiological process
- porphyrin biosynthesis
- porphyrin metabolism
|
| Component |
| — |
|
| Enzyme 3 General Function |
Coenzyme transport and metabolism |
| Enzyme 3 Specific Function |
2 5-aminolevulinate = porphobilinogen + 2 H(2)O |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- 2 5-aminolevulinate = porphobilinogen + 2 H2O [RN:R00036] ALL_REAC R00036
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
47077495  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q6ZMU0  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
Q6ZMU0_HUMAN  |
| Enzyme 3 PDB ID |
1E51  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
AK131490  |
| Enzyme 3 GeneCard ID |
Q6ZMU0  |
| Enzyme 3 GenAtlas ID |
Not Available |
| Enzyme 3 HGNC ID |
HGNC:395  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
Not Available |
| Enzyme 3 General References |
Not Available |
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
13087 |
| Enzyme 4 Name |
cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase |
| Enzyme 4 Synonyms |
- HMBS, mRNA
- Hydroxymethylbilane synthase, isoform CRA_a
|
| Enzyme 4 Gene Name |
HMBS |
| Enzyme 4 Protein Sequence |
>cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase
MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG
DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH
DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQ
QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH
VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA
H
|
| Enzyme 4 Number of Residues |
361 |
| Enzyme 4 Molecular Weight |
39331 |
| Enzyme 4 Theoretical pI |
7.19 |
| Enzyme 4 GO Classification |
Not Available |
| 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 |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158261573  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A8K2L0  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A8K2L0_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK290275  |
| Enzyme 4 GeneCard ID |
A8K2L0  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
15248 |
| Enzyme 5 Name |
cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
Not Available |
| Enzyme 5 Protein Sequence |
>cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA
MPPTSSTPSLSRPGLGQAGKPDTGSHPPPTISTSIFLSCFPTIPLSRPRTTGPSHSYQSI
SHPRSCRDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERG
SAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLA
EVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDA
AKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDL
PLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE
|
| Enzyme 5 Number of Residues |
359 |
| Enzyme 5 Molecular Weight |
39034 |
| Enzyme 5 Theoretical pI |
7.72 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Coenzyme transport and metabolism |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
Not Available |
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
158254412  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
A8K375  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
A8K375_HUMAN  |
| Enzyme 5 PDB ID |
1E51  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1080 bp
ATGCCTCCAACCTCATCTACCCCATCTTTGTCACGCCCTGGGCTTGGCCAGGCAGGGAAG
CCAGACACTGGATCCCATCCTCCTCCCACCATCTCCACTTCCATATTTCTTTCCTGCTTC
CCAACCATCCCTCTCAGTCGCCCCCGCACCACTGGCCCTTCCCACAGCTACCAATCCATA
TCCCACCCCCGCTCTTGCAGGGATGTTCCTGATGACATACAGCCTATCACCAGCCTCCCA
GGAGTGGCCAGGTATGGTGTGAAGCGGCTGGAAGAGATGCTGAGGCCCTTGGTGGAAGAG
GGCCTACGCTGTGTCTTGATCTTTGGCGTCCCCAGCAGAGTTCCCAAGGACGAGCGGGGT
TCCGCAGCTGACTCCGAGGAGTCCCCAGCTATTGAGGCAATCCATCTGTTGAGGAAGACC
TTCCCCAACCTCCTGGTGGCCTGTGATGTCTGCCTGTGTCCCTACACCTCCCATGGTCAC
TGCGGGCTCCTGAGTGAAAACGGAGCATTCCGGGCTGAGGAGAGCCGCCAGCGGCTGGCT
GAGGTGGCATTGGCGTATGCCAAGGCAGGATGTCAGGTGGTAGCCCCGTCGGACATGATG
GATGGACGCGTGGAAGCCATCAAAGAGGCCCTGATGGCACATGGACTTGGCAACAGGGTA
TCGGTGATGAGCTACAGTGCCAAATTTGCTTCCTGTTTCTATGGCCCTTTCCGGGATGCA
GCTAAGTCAAGCCCAGCTTTTGGGGACCGCCGCTGCTACCAGCTGCCCCCTGGAGCACGA
GGCCTGGCTCTCCGAGCTGTGGACCGGGATGTACGGGAAGGAGCTGACATGCTCATGGTG
AAGCCGGGAATGCCCTACCTGGACATCGTGCGGGAGGTAAAGGACAAGCACCCTGACCTC
CCTCTCGCCGTGTACCACGTCTCTGGAGAGTTTGCCATGCTGTGGCATGGAGCCCAGGCC
GGGGCATTTGATCTCAAGGCTGCCGTACTGGAGGCCATGACTGCCTTCCGCAGAGCAGGT
GCTGACATCATCATCACCTACTACACACCGCAGCTGCTGCAGTGGCTGAAGGAGGAATGA
|
| Enzyme 5 GenBank Gene ID |
AK290490  |
| Enzyme 5 GeneCard ID |
A8K375  |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
Not Available |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
Not Available |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |