High impact information on DAL2

• Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea [1].
• 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 [2].
• This sequence, which we term Arabidopsis thaliana Allantoate Amidohydrolase (AtAAH), was shown to be functional by complementation of Saccharomyces cerevisiae dal2 mutants, blocked in allantoate degradation [3].
• Sequences of two adjacent genes, one (DAL2) encoding allantoicase and another (DCG1) sensitive to nitrogen-catabolite repression in Saccharomyces cerevisiae [4].
• Also present upstream from DAL2 is a mutant form of the upstream induction sequence required for response of DAL7 to induction [4].

Biological context of DAL2

• Reported are the nucleotide sequences of the yeast allantoicase-encoding gene (DAL2) and that of an unknown gene adjacent to it [4].
• Deletion of sequences containing ORC-binding sites near the DAL2 and DAL4 genes in the DAL gene cluster, which are induced by either the orc2-1 mutation or by starvation, constitutively activates these genes and abolishes their activation by the orc2-1 mutation [5].

Associations of DAL2 with chemical compounds

• Uninduced cultures of Saccharomyces cerevisiae exhibit high basal levels of allantoinase, allantoicase, and ureidoglycolate hydrolase, the enzymes responsible for degrading allantoin to urea [6].

Other interactions of DAL2

• Genes coding for Dur1.2p, Dal2p, and Sps19p were down-regulated [7].

References