ITPA dimer dephosphorylates RBV-TP to RBV-MP

Stable Identifier
Reaction [transition]
Homo sapiens
ITPA dimer hydrolyzes RBV-TP
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Ribavirin triphosphate (RBV-TP) was dephosphorylated in vitro by recombinant ITP triphosphatase (ITPAse, ITPA) to a similar extent as its naturally occurring substrate ITP. Reduced ITPase activity in one third of humans causes increased intracellular levels of RBV-TP, leading to increased treatment efficacy (Nystrom et al, 2018; Tanaka et al, 2018). Polymorphisms in the gene encoding ITPase (ITPA) have been associated with protection against ribavirin-induced anemia (Fellay et al, 2010).
Literature References
PubMed ID Title Journal Year
29580856 Induction of inosine triphosphatase activity during ribavirin treatment for chronic hepatitis C

Yokomori, H, Tanaka, Y, Otori, K

Clin Chim Acta 2018
30045981 Inosine Triphosphate Pyrophosphatase Dephosphorylates Ribavirin Triphosphate and Reduced Enzymatic Activity Potentiates Mutagenesis in Hepatitis C Virus

Nyström, K, Lagging, M, Adamek, L, Tang, KW, Hellstrand, K, Wind-Rotolo, M, Waldenström, J, Nilsson, S, Said, J, Brunet, S, Wanrooij, PH, Norder, H

J Virol 2018
20173735 ITPA gene variants protect against anaemia in patients treated for chronic hepatitis C

Sulkowski, M, Albrecht, J, Qiu, P, Brass, C, Bertelsen, AH, Thompson, AJ, Warner, A, Little, LD, Fellay, J, Watson, M, Goldstein, DB, Muir, AJ, Gumbs, CE, Urban, TJ, McHutchison, JG, Shianna, KV, Ge, D

Nature 2010
Catalyst Activity

nucleoside triphosphate diphosphatase activity of ITPA dimer [cytosol]

Orthologous Events
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