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Property comparison of recombinant amphibian and mammalian allantoicases
Author(s) -
Vigetti Davide,
Pollegioni Loredano,
Monetti Claudio,
Prati Mariangela,
Bernardini Giovanni,
Gornati Rosalba
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02264-0
Subject(s) - recombinant dna , xenopus , enzyme , escherichia coli , western blot , bivalent (engine) , biology , microbiology and biotechnology , biochemistry , amino acid , chemistry , gene , organic chemistry , metal
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.