High impact information on DAL1

• The chain of enzymes necessary to convert uric acid to its metabolic products urea and glyoxylic acid in vertebrates is truncated through the successive loss of allantoicase, allantoinase, and urate oxidase during phylogenetic evolution [1].
• The hepatic- and renal-specific expression of allantoinase coincides with the distribution of urate oxidase in these tissues in the frog [1].
• This study reports the cloning of a cDNA encoding bullfrog (Rana catesbeiana) allantoinase, an enzyme that converts allantoin to allantoic acid [1].
• Amphibian allantoinase. Molecular cloning, tissue distribution, and functional expression [1].
• Immunocytochemical analysis revealed that allantoinase is localized to mitochondria and not to peroxisomes [1].

Biological context of DAL1

• Missing from the DAL1 5' flanking region were any sequences with significant homology to the DAL7 UIS element required for response to inducer [2].
• Correlated with these expression characteristics, the upstream region of DAL1 contained five copies of a sequence that is homologous to the DAL UASNTR element previously shown to be required for transcriptional activation and NCR sensitivity of the DAL5 and DAL7 genes [2].
• This report describes genetic data indicating that the DAL80 and DAL81 loci are situated approximately 13 cM from the centromere on the right arm of chromosome XI and 9 cM proximal to the DAL1 locus on chromosome IX, respectively [3].
• Their functions were confirmed by genetic complementation of a yeast mutant (dal1) deficient in allantoin hydrolysis [4].
• Allantoinase is a key enzyme for biogenesis and degradation of these ureide compounds [4].

Anatomical context of DAL1

• The proteins encoded by those genes were predicted to have a signal peptide for the secretory pathway, which is consistent with earlier biochemical work that localized allantoinase activity to microbodies and endoplasmic reticulum (Hanks et al., 1981) [4].
• These cell organelles probably were the site of urate oxidase, an enzyme that, after growth on purine substrates, together with allantoinase was present at high activities [5].

Associations of DAL1 with chemical compounds

• 1. Allantoinase [EC 3.5.2.5] was isolated from cells of Candida utilis and unpurified by chromatography on columns of DEAE-cellulose and Sephadex G-200 after treatment with urea to remove urate oxidase [EC 1.7.3.3.]. 2. The purified allantoinase catalyzed the hydrolysis of allantoin into allantoic acid [6].

Regulatory relationships of DAL1

• DAL1 is expressed in an inducer-independent manner in strain M970 (sigma 1278b genetic background) and modestly responds to mutation of the dal80 locus [2].

Other interactions of DAL1

• Cis-acting sites contributing to expression of divergently transcribed DAL1 and DAL4 genes in S. cerevisiae: a word of caution when correlating cis-acting sequences with genome-wide expression analyses [7].

References