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==References==
==References==
{{reflist}}
{{reflist|2}}
==Further reading==
==Further reading==
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{{refbegin | 2}}

Revision as of 13:56, 4 September 2012



Aminolevulinate, delta-, dehydratase
PDB rendering based on 1e51.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols ALAD ; ALADH; MGC5057; PBGS
External IDs Template:OMIM5 Template:MGI HomoloGene: 16
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Aminolevulinate, delta-, dehydratase, also known as ALAD, is a human gene.

The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Alternatively spliced transcript variants encoding different isoforms have been identified.[1]

References

  1. ↑ "Entrez Gene: ALAD aminolevulinate, delta-, dehydratase".

Further reading

  • Bernard A, Lauwerys R (1988). "Metal-induced alterations of delta-aminolevulinic acid dehydratase". Ann. N. Y. Acad. Sci. 514: 41–7. PMID 3327436.
  • Jaffe EK (2005). "The porphobilinogen synthase catalyzed reaction mechanism". Bioorg. Chem. 32 (5): 316–25. doi:10.1016/j.bioorg.2004.05.010. PMID 15381398.
  • Roels HA, Buchet JP, Lauwerys RR, Sonnet J (1975). "Comparison of in vivo effect of inorganic lead and cadmium on glutathione reductase system and delta-aminolevulinate dehydratase in human erythrocytes". British journal of industrial medicine. 32 (3): 181–92. PMID 1156566.
  • Ishida N, Fujita H, Fukuda Y; et al. (1992). "Cloning and expression of the defective genes from a patient with delta-aminolevulinate dehydratase porphyria". J. Clin. Invest. 89 (5): 1431–7. PMID 1569184.
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. PMID 1602151.
  • Astrin KH, Kaya AH, Wetmur JG, Desnick RJ (1991). "RsaI polymorphism in the human delta-aminolevulinate dehydratase gene at 9q34". Nucleic Acids Res. 19 (15): 4307. PMID 1678509.
  • Wetmur JG, Kaya AH, Plewinska M, Desnick RJ (1991). "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. 49 (4): 757–63. PMID 1716854.
  • Plewinska M, Thunell S, Holmberg L; et al. (1991). "delta-Aminolevulinate dehydratase deficient porphyria: identification of the molecular lesions in a severely affected homozygote". Am. J. Hum. Genet. 49 (1): 167–74. PMID 2063868.
  • Potluri VR, Astrin KH, Wetmur JG; et al. (1987). "Human delta-aminolevulinate dehydratase: chromosomal localization to 9q34 by in situ hybridization". Hum. Genet. 76 (3): 236–9. PMID 3036687.
  • Gibbs PN, Jordan PM (1986). "Identification of lysine at the active site of human 5-aminolaevulinate dehydratase". Biochem. J. 236 (2): 447–51. PMID 3092810.
  • Wetmur JG, Bishop DF, Cantelmo C, Desnick RJ (1986). "Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone". Proc. Natl. Acad. Sci. U.S.A. 83 (20): 7703–7. PMID 3463993.
  • Wetmur JG, Bishop DF, Ostasiewicz L, Desnick RJ (1986). "Molecular cloning of a cDNA for human delta-aminolevulinate dehydratase". Gene. 43 (1–2): 123–30. PMID 3758678.
  • Beaumont C, Foubert C, Grandchamp B; et al. (1984). "Assignment of the human gene for delta aminolevulinate dehydrase to chromosome 9 by somatic cell hybridization and specific enzyme immunoassay". Ann. Hum. Genet. 48 (Pt 2): 153–9. PMID 6378062.
  • Eiberg H, Mohr J, Nielsen LS (1983). "delta-Aminolevulinatedehydrase: synteny with ABO-AK1-ORM (and assignment to chromosome 9)". Clin. Genet. 23 (2): 150–4. PMID 6839527.
  • Doss M, von Tiepermann R, Schneider J (1981). "Acute hepatic porphyria syndrome with porphobilinogen synthase defect". Int. J. Biochem. 12 (5–6): 823–6. PMID 7450139.
  • Kaya AH, Plewinska M, Wong DM; et al. (1994). "Human delta-aminolevulinate dehydratase (ALAD) gene: structure and alternative splicing of the erythroid and housekeeping mRNAs". Genomics. 19 (2): 242–8. PMID 8188255.
  • Akagi R, Yasui Y, Harper P, Sassa S (1999). "A novel mutation of delta-aminolaevulinate dehydratase in a healthy child with 12% erythrocyte enzyme activity". Br. J. Haematol. 106 (4): 931–7. PMID 10519994.
  • Akagi R, Shimizu R, Furuyama K; et al. (2000). "Novel molecular defects of the delta-aminolevulinate dehydratase gene in a patient with inherited acute hepatic porphyria". Hepatology. 31 (3): 704–8. doi:10.1002/hep.510310321. PMID 10706561.
  • Kervinen J, Jaffe EK, Stauffer F; et al. (2001). "Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity". Biochemistry. 40 (28): 8227–36. PMID 11444968.


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