Reactome | Guanylate-binding protein 1 (GBP1) mediates a two-step hydro...

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created	[InstanceEdit:9953154] Shamovsky, Veronica, 2025-05-28
dbId	9953166
displayName	Guanylate-binding protein 1 (GBP1) mediates a two-step hydro...
literatureReference	[LiteratureReference:9947890] Structural insights into the activation mechanism of antimicrobial GBP1 [LiteratureReference:9947931] How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP [LiteratureReference:9953136] Insight into temperature dependence of GTPase activity in human guanylate binding protein-1 [LiteratureReference:9953147] Transient kinetic investigation of GTP hydrolysis catalyzed by interferon-gamma-induced hGBP1 (human guanylate binding protein 1)
modified	[InstanceEdit:9954263] Shamovsky, Veronica, 2025-06-06
schemaClass	Summation
text	Guanylate-binding protein 1 (GBP1) mediates a two-step hydrolysis, first converting GTP to GDP and then GDP to GMP, a process facilitated by repositioning the nucleotide within the active site after the first hydrolysis (Ghosh et al., 2006; Schwemmle & Staeheli, 1994; Weismehl M et al., 2024). Following GDP hydrolysis, the GBP1 oligomer undergoes conformational changes that destabilize the GMP-bound GBP1 complex, ultimately leading to the release of GMP and GBP1 (Weismehl M et al., 2024). Released GMP is catabolized to uric acid, which may activate the NLRP3 inflammasome under certain conditions such as Chlamydia trachomatis infection (Xavier et al., 2020).

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