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Allantoicase

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Giovanni Bernardini – 1st expert on this subject based on the ideXlab platform

  • Selective Pressure on the Allantoicase Gene During Vertebrate Evolution
    Journal of Molecular Evolution, 2003
    Co-Authors: Davide Vigetti, Giovanni Bernardini, Claudio Monetti, Mariangela Prati, Giorgio Binelli, Rosalba Gornati

    Abstract:

    During vertebrate evolution, the uric acid degradation pathway has been modified and several enzymes have been lost. Consequently, the end product of purine catabolism varies from species to species. In the past few years, we have focused our attention on vertebrate Allantoicase (an uricolytic pathway enzyme), whose activity is present in certain fish and amphibians only, but whose mRNA we detected also in mammals. As Allantoicase activity disappeared in amniotes, we wonder why these sequences not only remain present in the mammalian genome, but are still transcribed. To elucidate this issue, we have cloned and analyzed comparable cDNA sequences of different organisms from ascidians to mammals. The analysis of the nonsynonymous–synonymous substitution rate that we performed on the coding region comprising exons 3 to 8 by means of maximum likelihood suggested that a certain amount of purifying selection is acting on the Allantoicase sequences. Some implications of the preservation of an apparently unnecessary gene in higher vertebrates are discussed.

  • genomic organization and chromosome localization of the murine and human Allantoicase gene
    Gene, 2002
    Co-Authors: Davide Vigetti, Claudio Monetti, Mariangela Prati, Rosalba Gornati, Giovanni Bernardini

    Abstract:

    Abstract Allantoicase is one of the enzymes involved in uricolysis. The enzymes of this catabolic pathway (i.e. allantoinase, Allantoicase, ureidoglycolate lyase and urease) were lost during vertebrate evolution and the causes for this loss are still unclear. In mammals, as well as in birds and reptiles, the activity of Allantoicase is absent; notwithstanding, we recently cloned human and mouse cDNA sequences with high similarity with previously characterized Allantoicases. In the present paper, we report the genomic organization of the Allantoicase gene in mouse and in man. Both genes are constituted by 11 exons that appear to be very conserved; introns are more variable in length while maintain the same phase but for intron 4. We have also detected a second transcript of the human Allantoicase gene in which exon 1 is absent. Moreover, the mouse gene maps in chromosome 12 at 13.0 cM from the centromere.

  • Property comparison of recombinant amphibian and mammalian Allantoicases.
    FEBS Letters, 2002
    Co-Authors: Davide Vigetti, Giovanni Bernardini, Claudio Monetti, Mariangela Prati, Loredano Pollegioni, Rosalba Gornati

    Abstract:

    Allantoicase is an enzyme involved in uric acid degradation. Although it is commonly accepted that Allantoicase is lost in mammals, birds and reptiles, we have recently identified its transcripts in mice and humans. The mouse mRNA seems capable of encoding a functional Allantoicase, therefore we expressed the Xenopus and mouse Allantoicases (MAlc and XAlc, respectively) in Escherichia coli and characterized the recombinant enzymes. The two recombinant Allantoicases show a similar temperature and pH stability but, although XAlc and MAlc share a 54% amino acid identity, they differ in sensitivity to bivalent cations, in substrate affinity and in the level of expression in tissues (as revealed by means of Western blot analysis). We propose that the loss of Allantoicase activity in mouse is due to a low substrate affinity and to a reduced expression level of the enzyme.

Davide Vigetti – 2nd expert on this subject based on the ideXlab platform

  • Selective Pressure on the Allantoicase Gene During Vertebrate Evolution
    Journal of Molecular Evolution, 2003
    Co-Authors: Davide Vigetti, Giovanni Bernardini, Claudio Monetti, Mariangela Prati, Giorgio Binelli, Rosalba Gornati

    Abstract:

    During vertebrate evolution, the uric acid degradation pathway has been modified and several enzymes have been lost. Consequently, the end product of purine catabolism varies from species to species. In the past few years, we have focused our attention on vertebrate Allantoicase (an uricolytic pathway enzyme), whose activity is present in certain fish and amphibians only, but whose mRNA we detected also in mammals. As Allantoicase activity disappeared in amniotes, we wonder why these sequences not only remain present in the mammalian genome, but are still transcribed. To elucidate this issue, we have cloned and analyzed comparable cDNA sequences of different organisms from ascidians to mammals. The analysis of the nonsynonymous–synonymous substitution rate that we performed on the coding region comprising exons 3 to 8 by means of maximum likelihood suggested that a certain amount of purifying selection is acting on the Allantoicase sequences. Some implications of the preservation of an apparently unnecessary gene in higher vertebrates are discussed.

  • genomic organization and chromosome localization of the murine and human Allantoicase gene
    Gene, 2002
    Co-Authors: Davide Vigetti, Claudio Monetti, Mariangela Prati, Rosalba Gornati, Giovanni Bernardini

    Abstract:

    Abstract Allantoicase is one of the enzymes involved in uricolysis. The enzymes of this catabolic pathway (i.e. allantoinase, Allantoicase, ureidoglycolate lyase and urease) were lost during vertebrate evolution and the causes for this loss are still unclear. In mammals, as well as in birds and reptiles, the activity of Allantoicase is absent; notwithstanding, we recently cloned human and mouse cDNA sequences with high similarity with previously characterized Allantoicases. In the present paper, we report the genomic organization of the Allantoicase gene in mouse and in man. Both genes are constituted by 11 exons that appear to be very conserved; introns are more variable in length while maintain the same phase but for intron 4. We have also detected a second transcript of the human Allantoicase gene in which exon 1 is absent. Moreover, the mouse gene maps in chromosome 12 at 13.0 cM from the centromere.

  • Property comparison of recombinant amphibian and mammalian Allantoicases.
    FEBS Letters, 2002
    Co-Authors: Davide Vigetti, Giovanni Bernardini, Claudio Monetti, Mariangela Prati, Loredano Pollegioni, Rosalba Gornati

    Abstract:

    Allantoicase is an enzyme involved in uric acid degradation. Although it is commonly accepted that Allantoicase is lost in mammals, birds and reptiles, we have recently identified its transcripts in mice and humans. The mouse mRNA seems capable of encoding a functional Allantoicase, therefore we expressed the Xenopus and mouse Allantoicases (MAlc and XAlc, respectively) in Escherichia coli and characterized the recombinant enzymes. The two recombinant Allantoicases show a similar temperature and pH stability but, although XAlc and MAlc share a 54% amino acid identity, they differ in sensitivity to bivalent cations, in substrate affinity and in the level of expression in tissues (as revealed by means of Western blot analysis). We propose that the loss of Allantoicase activity in mouse is due to a low substrate affinity and to a reduced expression level of the enzyme.

Claudio Monetti – 3rd expert on this subject based on the ideXlab platform

  • Selective Pressure on the Allantoicase Gene During Vertebrate Evolution
    Journal of Molecular Evolution, 2003
    Co-Authors: Davide Vigetti, Giovanni Bernardini, Claudio Monetti, Mariangela Prati, Giorgio Binelli, Rosalba Gornati

    Abstract:

    During vertebrate evolution, the uric acid degradation pathway has been modified and several enzymes have been lost. Consequently, the end product of purine catabolism varies from species to species. In the past few years, we have focused our attention on vertebrate Allantoicase (an uricolytic pathway enzyme), whose activity is present in certain fish and amphibians only, but whose mRNA we detected also in mammals. As Allantoicase activity disappeared in amniotes, we wonder why these sequences not only remain present in the mammalian genome, but are still transcribed. To elucidate this issue, we have cloned and analyzed comparable cDNA sequences of different organisms from ascidians to mammals. The analysis of the nonsynonymous–synonymous substitution rate that we performed on the coding region comprising exons 3 to 8 by means of maximum likelihood suggested that a certain amount of purifying selection is acting on the Allantoicase sequences. Some implications of the preservation of an apparently unnecessary gene in higher vertebrates are discussed.

  • genomic organization and chromosome localization of the murine and human Allantoicase gene
    Gene, 2002
    Co-Authors: Davide Vigetti, Claudio Monetti, Mariangela Prati, Rosalba Gornati, Giovanni Bernardini

    Abstract:

    Abstract Allantoicase is one of the enzymes involved in uricolysis. The enzymes of this catabolic pathway (i.e. allantoinase, Allantoicase, ureidoglycolate lyase and urease) were lost during vertebrate evolution and the causes for this loss are still unclear. In mammals, as well as in birds and reptiles, the activity of Allantoicase is absent; notwithstanding, we recently cloned human and mouse cDNA sequences with high similarity with previously characterized Allantoicases. In the present paper, we report the genomic organization of the Allantoicase gene in mouse and in man. Both genes are constituted by 11 exons that appear to be very conserved; introns are more variable in length while maintain the same phase but for intron 4. We have also detected a second transcript of the human Allantoicase gene in which exon 1 is absent. Moreover, the mouse gene maps in chromosome 12 at 13.0 cM from the centromere.

  • Property comparison of recombinant amphibian and mammalian Allantoicases.
    FEBS Letters, 2002
    Co-Authors: Davide Vigetti, Giovanni Bernardini, Claudio Monetti, Mariangela Prati, Loredano Pollegioni, Rosalba Gornati

    Abstract:

    Allantoicase is an enzyme involved in uric acid degradation. Although it is commonly accepted that Allantoicase is lost in mammals, birds and reptiles, we have recently identified its transcripts in mice and humans. The mouse mRNA seems capable of encoding a functional Allantoicase, therefore we expressed the Xenopus and mouse Allantoicases (MAlc and XAlc, respectively) in Escherichia coli and characterized the recombinant enzymes. The two recombinant Allantoicases show a similar temperature and pH stability but, although XAlc and MAlc share a 54% amino acid identity, they differ in sensitivity to bivalent cations, in substrate affinity and in the level of expression in tissues (as revealed by means of Western blot analysis). We propose that the loss of Allantoicase activity in mouse is due to a low substrate affinity and to a reduced expression level of the enzyme.