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.
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http://dx.doi.org/10.1016/s0014-5793(02)02264-0 | DOI Listing |
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January 2025
State Key Laboratory of Green Pesticide, International Joint Research Center for Intelligent Biosensing Technology and Health, College of Chemistry, Central China Normal University, Wuhan, 430079, P. R. China.
The severe environmental and human health hazards posed by organophosphorus compounds underscore the pressing need for advancements in their degradation and detection. However, practical implementation is impeded by prolonged degradation durations and limited efficiency. Herein, an effective interfacial modification approach is proposed involving the integration of photoactive Au nanoparticles (NPs) onto metal-organic frameworks, resulting in the synthesis of UiO-66/Au NPs exhibiting enhanced hydrolysis activity under light excitation.
View Article and Find Full Text PDFNano Lett
January 2025
Department of Mechanical Engineering, University of Alberta, 9211-116 Street NW, Edmonton, Alberta T6G 1H9, Canada.
Uncontrolled lithium (Li) dendrite formation presents major safety risks and challenges in the Li host design. A novel approach is introduced, using a valence gradient in iron nanoparticles (Fe, Fe, Fe) to stabilize the anodes. An Fe component, with fast Li diffusion, ensures a steady supply of Li to Fe and Fe components, which have slower Li diffusion.
View Article and Find Full Text PDFProtein phosphatases are critical for regulating cell signaling, cell cycle, and cell fate decisions, and their dysregulation leads to an array of human diseases like cancer. The dual specificity phosphatases (DUSPs) have emerged as important factors driving tumorigenesis and cancer therapy resistance. DUSP12 is a poorly characterized atypical DUSP widely conserved throughout evolution.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Life Science, Hebei University, Innovation Center for Bioengineering and Biotechnology of Hebei Province, Baoding 071002, China. Electronic address:
Nowadays, metal-organic frameworks (MOFs) have been emerged as an efficient platform for enzyme immobilization due to their high porosity, tunability, and chemical versatility. In this study, a series of hybrid lipase@NKMOF-101-M (M = Mg, Mn, Zn, Co, or Ni) biocatalysts were constructed through a facile in situ encapsulation method, and the encapsulation and immobilization of lipase in MOFs were carefully validated. The catalytic activity of lipase@NKMOF-101-Mn was 2-fold higher than that of lipase@ZIF-8 and 3-fold higher than that of lipase@MCM-41 due to its excellent dispersibility and hydrophobicity in hexane.
View Article and Find Full Text PDFACS Biomater Sci Eng
January 2025
Department of Materials Science and Bioengineering, Nagaoka University of Technology, Kamitomioka 1603-1, Nagaoka, Niigata 940-2188, Japan.
Octacalcium phosphate (OCP) has been used as a bone replacement material due to its higher bone affinity. However, the mechanism of affinity has not been clarified. Since the 100 crystalline plane of OCP is closely involved in the biological reactions during osteogenesis, it is important to expose the 100 crystalline plane of OCP to the biological fluid to precisely measure the interfacial reactions.
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