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Details on Person Guanylate-binding protein 1 (GBP1) mediates a two-step hydro...

Class:IdSummation:9953166
_displayNameGuanylate-binding protein 1 (GBP1) mediates a two-step hydro...
_timestamp2025-06-06 22:19:27
created[InstanceEdit:9953154] Shamovsky, Veronica, 2025-05-28
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
textGuanylate-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).
(summation)[Reaction:9953173] GMP dissociates from the GBP1 oligomer [Homo sapiens]
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