Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism
Articolo
Data di Pubblicazione:
2018
Citazione:
Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism / G. Degani, A. Barbiroli, L. Regazzoni, L. Popolo, M.A. Vanoni. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1422-0067. - 19:4(2018 Apr), pp. 945.1-945.19. [10.3390/ijms19040945]
Abstract:
Abstract: Reactive intermediate deaminase (Rid) protein family is a recently discovered group of
enzymes that is conserved in all domains of life and is proposed to play a role in the detoxification
of reactive enamines/imines. UK114, the mammalian member of RidA subfamily, was identified
in the early 90s as a component of perchloric acid-soluble extracts from goat liver and exhibited
immunomodulatory properties. Multiple activities were attributed to this protein, but its function
is still unclear. This work addressed the question of whether UK114 is a Rid enzyme. Biochemical
analyses demonstrated that UK114 hydrolyzes -imino acids generated by L- or D-amino acid
oxidases with a preference for those deriving from Ala > Leu = L-Met > L-Gln, whereas it was
poorly active on L-Phe and L-His. Circular Dichroism (CD) analyses of UK114 conformational
stability highlighted its remarkable resistance to thermal unfolding, even at high urea concentrations.
The half-life of heat inactivation at 95 C, measured from CD and activity data, was about 3.5 h.
The unusual conformational stability of UK114 could be relevant in the frame of a future evaluation
of its immunogenic properties. In conclusion, mammalian UK114 proteins are RidA enzymes that
may play an important role in metabolism homeostasis also in these organisms.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
UK114; Rid family; metabolic damage; thermal stability; 2-aminoacrylate; imino acids; D-amino acid oxidase; L-amino acid oxidase
Elenco autori:
G. Degani, A. Barbiroli, L. Regazzoni, L. Popolo, M.A. Vanoni
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