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| <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
| | #REDIRECT [[Delta-aminolevulinic acid dehydratase]] |
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| <!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
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| {{GNF_Protein_box
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| | image = PBB_Protein_ALAD_image.jpg
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| | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e51.
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| | PDB = {{PDB2|1e51}}, {{PDB2|1pv8}}
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| | Name = Aminolevulinate, delta-, dehydratase
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| | HGNCid = 395
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| | Symbol = ALAD
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| | AltSymbols =; ALADH; MGC5057; PBGS
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| | OMIM = 125270
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| | ECnumber =
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| | Homologene = 16
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| | MGIid = 96853
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| | GeneAtlas_image1 = PBB_GE_ALAD_218487_at_tn.png
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| | GeneAtlas_image2 = PBB_GE_ALAD_218489_s_at_tn.png
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| | Function = {{GNF_GO|id=GO:0004655 |text = porphobilinogen synthase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
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| | Component =
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| | Process = {{GNF_GO|id=GO:0006783 |text = heme biosynthetic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
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| | Orthologs = {{GNF_Ortholog_box
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| | Hs_EntrezGene = 210
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| | Hs_Ensembl = ENSG00000148218
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| | Hs_RefseqProtein = NP_000022
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| | Hs_RefseqmRNA = NM_000031
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| | Hs_GenLoc_db =
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| | Hs_GenLoc_chr = 9
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| | Hs_GenLoc_start = 115188418
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| | Hs_GenLoc_end = 115203412
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| | Hs_Uniprot = P13716
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| | Mm_EntrezGene = 17025
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| | Mm_Ensembl = ENSMUSG00000028393
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| | Mm_RefseqmRNA = XM_982322
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| | Mm_RefseqProtein = XP_987416
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| | Mm_GenLoc_db =
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| | Mm_GenLoc_chr = 4
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| | Mm_GenLoc_start = 61995531
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| | Mm_GenLoc_end = 62006424
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| | Mm_Uniprot = O89061
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| }}
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| }}
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| '''Aminolevulinate, delta-, dehydratase''', also known as '''ALAD''', is a human [[gene]].
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| <!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
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| {{PBB_Summary
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| | section_title =
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| | summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ALAD aminolevulinate, delta-, dehydratase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=210| accessdate = }}</ref>
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| ==References==
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| {{reflist|2}}
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| ==Further reading==
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| {{refbegin | 2}}
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| {{PBB_Further_reading | |
| | citations =
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| *{{cite journal | author=Bernard A, Lauwerys R |title=Metal-induced alterations of delta-aminolevulinic acid dehydratase. |journal=Ann. N. Y. Acad. Sci. |volume=514 |issue= |pages= 41–7 |year= 1988 |pmid= 3327436 |doi= }}
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| *{{cite journal | author=Jaffe EK |title=The porphobilinogen synthase catalyzed reaction mechanism. |journal=Bioorg. Chem. |volume=32 |issue= 5 |pages= 316–25 |year= 2005 |pmid= 15381398 |doi= 10.1016/j.bioorg.2004.05.010 }}
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| *{{cite journal | author=Roels HA, Buchet JP, Lauwerys RR, Sonnet J |title=Comparison of in vivo effect of inorganic lead and cadmium on glutathione reductase system and delta-aminolevulinate dehydratase in human erythrocytes. |journal=British journal of industrial medicine |volume=32 |issue= 3 |pages= 181–92 |year= 1975 |pmid= 1156566 |doi= }}
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| *{{cite journal | author=Ishida N, Fujita H, Fukuda Y, ''et al.'' |title=Cloning and expression of the defective genes from a patient with delta-aminolevulinate dehydratase porphyria. |journal=J. Clin. Invest. |volume=89 |issue= 5 |pages= 1431–7 |year= 1992 |pmid= 1569184 |doi= }}
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| *{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi= }}
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| *{{cite journal | author=Astrin KH, Kaya AH, Wetmur JG, Desnick RJ |title=RsaI polymorphism in the human delta-aminolevulinate dehydratase gene at 9q34. |journal=Nucleic Acids Res. |volume=19 |issue= 15 |pages= 4307 |year= 1991 |pmid= 1678509 |doi= }}
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| *{{cite journal | author=Wetmur JG, Kaya AH, Plewinska M, Desnick RJ |title=Molecular characterization of the human delta-aminolevulinate dehydratase 2 (ALAD2) allele: implications for molecular screening of individuals for genetic susceptibility to lead poisoning. |journal=Am. J. Hum. Genet. |volume=49 |issue= 4 |pages= 757–63 |year= 1991 |pmid= 1716854 |doi= }}
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| *{{cite journal | author=Plewinska M, Thunell S, Holmberg L, ''et al.'' |title=delta-Aminolevulinate dehydratase deficient porphyria: identification of the molecular lesions in a severely affected homozygote. |journal=Am. J. Hum. Genet. |volume=49 |issue= 1 |pages= 167–74 |year= 1991 |pmid= 2063868 |doi= }}
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| *{{cite journal | author=Potluri VR, Astrin KH, Wetmur JG, ''et al.'' |title=Human delta-aminolevulinate dehydratase: chromosomal localization to 9q34 by in situ hybridization. |journal=Hum. Genet. |volume=76 |issue= 3 |pages= 236–9 |year= 1987 |pmid= 3036687 |doi= }}
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| *{{cite journal | author=Gibbs PN, Jordan PM |title=Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. |journal=Biochem. J. |volume=236 |issue= 2 |pages= 447–51 |year= 1986 |pmid= 3092810 |doi= }}
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| *{{cite journal | author=Wetmur JG, Bishop DF, Cantelmo C, Desnick RJ |title=Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 20 |pages= 7703–7 |year= 1986 |pmid= 3463993 |doi= }}
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| *{{cite journal | author=Wetmur JG, Bishop DF, Ostasiewicz L, Desnick RJ |title=Molecular cloning of a cDNA for human delta-aminolevulinate dehydratase. |journal=Gene |volume=43 |issue= 1-2 |pages= 123–30 |year= 1986 |pmid= 3758678 |doi= }}
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| *{{cite journal | author=Beaumont C, Foubert C, Grandchamp B, ''et al.'' |title=Assignment of the human gene for delta aminolevulinate dehydrase to chromosome 9 by somatic cell hybridization and specific enzyme immunoassay. |journal=Ann. Hum. Genet. |volume=48 |issue= Pt 2 |pages= 153–9 |year= 1984 |pmid= 6378062 |doi= }}
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| *{{cite journal | author=Eiberg H, Mohr J, Nielsen LS |title=delta-Aminolevulinatedehydrase: synteny with ABO-AK1-ORM (and assignment to chromosome 9). |journal=Clin. Genet. |volume=23 |issue= 2 |pages= 150–4 |year= 1983 |pmid= 6839527 |doi= }}
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| *{{cite journal | author=Doss M, von Tiepermann R, Schneider J |title=Acute hepatic porphyria syndrome with porphobilinogen synthase defect. |journal=Int. J. Biochem. |volume=12 |issue= 5-6 |pages= 823–6 |year= 1981 |pmid= 7450139 |doi= }}
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| *{{cite journal | author=Kaya AH, Plewinska M, Wong DM, ''et al.'' |title=Human delta-aminolevulinate dehydratase (ALAD) gene: structure and alternative splicing of the erythroid and housekeeping mRNAs. |journal=Genomics |volume=19 |issue= 2 |pages= 242–8 |year= 1994 |pmid= 8188255 |doi= }}
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| *{{cite journal | author=Akagi R, Yasui Y, Harper P, Sassa S |title=A novel mutation of delta-aminolaevulinate dehydratase in a healthy child with 12% erythrocyte enzyme activity. |journal=Br. J. Haematol. |volume=106 |issue= 4 |pages= 931–7 |year= 1999 |pmid= 10519994 |doi= }}
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| *{{cite journal | author=Akagi R, Shimizu R, Furuyama K, ''et al.'' |title=Novel molecular defects of the delta-aminolevulinate dehydratase gene in a patient with inherited acute hepatic porphyria. |journal=Hepatology |volume=31 |issue= 3 |pages= 704–8 |year= 2000 |pmid= 10706561 |doi= 10.1002/hep.510310321 }}
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| *{{cite journal | author=Kervinen J, Jaffe EK, Stauffer F, ''et al.'' |title=Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity. |journal=Biochemistry |volume=40 |issue= 28 |pages= 8227–36 |year= 2001 |pmid= 11444968 |doi= }}
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| {{refend}}
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