Human δ-aminolevulinate dehydratase: chromosomal localization to 9q34 by in situ hybridization

  title={Human $\delta$-aminolevulinate dehydratase: chromosomal localization to 9q34 by in situ hybridization},
  author={Venkateswara R. Potluri and Kenneth H. Astrin and James G. Wetmur and David F. Bishop and Robert J. Desnick},
  journal={Human Genetics},
SummaryThe structural gene for human δ-aminolevulinate dehydratase (ALA-D) has been localized to chromosomal region 9q34 by in situ hybridization using a [125I]-labeled human δ-aminolevulinate dehydratase cDNA. Of the 150 silver grains analyzed, 25% were localized to chromosome 9q, while 12% and 8% were on chromosomes 1p and 13q, respectively. The single chromosomal region q34 had over 90% of the total grains observed on chromosome 9. In contrast, the grains on chromosomes 1p and 13q were… 

Regional assignment of the human uroporphyrinogen III synthase (UROS) gene to chromosome 10q25.2→q26.3

Using human-rodent hybrids containing different portions of human chromosome 10, the UROS gene was assigned to the region 10q25.2→ q26.3 by Southern hybridization analysis of DNA from somatic cell hybrids with the full-length UROS cDNA.

Erythrocyte delta-aminolevulinic acid dehydratase genotype and other mechanisms affecting workers' susceptibility to lead.

The depletion in erythrocyte ALAD activity was not found to be caused by the ALAD allele, and the entire ALAD gene analysis failed to indicate other variants, except for the Rsa I site.

Lack of association of δ-aminolevulinic acid dehydratase genotype with cytogenetic damage in lead workers

A significant association existed between both SCE and HFC levels and lead exposure, however, different ALAD genotypes were not found to be associated with levels of blood lead and ZPP in the three groups.

Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.

A number of X-ray analyses of an enzyme involved in a key early stage of tetrapyrrole biosynthesis are reported, showing that the enzyme adopts an octameric quaternary structure in accord with previously published analyses of the enzyme from a range of other species.

Delta-aminolevulinate dehydratase polymorphism and blood lead levels in Chinese children.

Results indicate that individuals carrying the ALAD2 allele are more likely to have sustained increases in blood lead levels when exposed to a lead-contaminated environment.

Polymorphism of Delta-Aminolevulinic Acid Dehydratase and Its Effect on Blood Lead Levels in Thai Workers

The frequency of ALAD2 in Thai workers was low; the authors found that ALAD polymorphism had a small or only modest effect on BLLs.

Erythrocyte aminolevulinic acid dehydratase inhibition by cis-platin.

Delta-Aminolevulinic acid dehydratase enzyme activity and susceptibility to lead toxicity in Uganda’s urban children

Majority of children in Uganda code for the ALAD1 allele, which is important for blood lead ions hoarding during lead toxicity, and expounding susceptibility to lead toxicity by relating blood lead levels, delta-aminolevulinic acid dehydratase (ALAD) enzyme activity, and genetic variations of proteins that code for ALAD in urban children of Uganda.

Biosynthesis of heme in mammals.



δ-Aminolevulinate dehydratase: Induced expression and regional assignment of the human gene to chromosome 9q13»qter

Examination of secondary, tertiary, and quaternary XX-8 subclones revealed that the expression of the human isozyme segregated with human chromosome 9q, confirming the provisional regional assignment made by classical linkage studies.

Assignment of the human gene for δ aminolevulinate dehydrase to chromosome 9 by somatic cell hybridization and specific enzyme immunoassay

A non‐competitive enzyme immunoassay specific for δ aminolevulinate dehydrase has been devised and applied to rodent–human hybrid cell lines and the gene for ALA dehydrase is assigned to chromosome 9.

Regional gene assignment of human porphobilinogen deaminase and esterase A4 to chromosome 11q23 leads to 11qter.

Results confirm the location of the gene for human PBGD on chromosome 11 and establish the assignment of the loci for PBGD and ESA4 in the region 11q23 leads to 11qter.


  • Biology
  • 2003
A genetic analysis of the factors involved in the control and development of this enzyme and with attempts to induce this enzyme in two inbred strains of mice are dealt with.

Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone.

Two cDNAs encoding human delta-aminolevulinate dehydratase (ALA-D) were identified, recloned into bacteriophage M13, and sequenced by primer extension, finding a cysteine- and histidine-rich binding site for zinc and an unusual region of charge complementarity surrounding the active lysine residue in the catalytic site.

Inherited deficiency of delta-aminolevulinic acid dehydratase.

Intial experiments support the hypothesis that the mutation in this family with an inherited deficiency of red cell ALA-D activity occurring over three generations may affect a regulatory gene, but enzyme purification and further study are required.

Isolation of a rat liver delta-aminolevulinate dehydrase (ALAD) cDNA clone: evidence for unequal ALAD gene dosage among inbred mouse strains.

We have isolated several cDNA clones encoding delta-aminolevulinate dehydrase [ALAD; porphobilinogen synthase; 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing), EC],

Linkage analyses using biochemical variants in mice. II. Levulinate dehydratase and autosomal glucose 6-phosphate dehydrogenase

The level of hepatic δ-aminolevulinate dehydratase varies among inbred strains of mice and is regulated by codominant alleles at the Lv locus, which is 5±2 recombination units from brown, b, in linkage group VIII.

Δ‐Aminolevulinatedehydrase: synteny with ABO‐AK1‐ORM (and assignment to chromosome 9)

A material comprising 846 normal families from the Copenhagen area was tested for δ‐aminolevulinatedehydrogenase and the most likely sequence, as judged from male θ values, was found to be ABO‐AK1 ‐ALADH‐ORM.