Property comparison of recombinant amphibian and mammalian allantoicases

FEBS Letters

Prati, Mariangela¹  Gornati, Rosalba¹  Monetti, Claudio¹  Vigetti, Davide¹  Bernardini, Giovanni¹  Pollegioni, Loredano¹ 

[1] Dipartimento di Biologia Strutturale e Funzionale, Università degli Studi dell'Insubria, Via J.H. Dunant 3, 21100 Varese, Italy

关键词: Purine degradation;    Uric acid;    Uricolysis;    Animal evolution;    XAlc;    purified His-tagged Xenopus allantoicase;    MAlc;    purified His-tagged mouse allantoicase;    ORF;    open reading frame;    PCR;    polymerase chain reaction;    IPTG;    isopropyl-β-D-thiogalactopyranoside;   

DOI  :  10.1016/S0014-5793(02)02264-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown