GMP synthase

Function GMP synthase (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate. GMPS is active in purine and glutamate metabolism. GMPS is a bifunctional two-domain enzyme with the dominates extracts ammonia from glutamine and the adds amine group to XMP to produce GMP. Structural highlights Human GMPS structure contains . The . . N-terminal glutaminase domain contains . 3D structures of GMP synthase Updated on 04-May-2025 2vpi – hGMPS glutaminase domain – human 2vxo - hGMPS + XMP 1wl8, 2d7j – PhGMPS subunit A – Pyrococcus horikoshii 2dpl, 3a4i - PhGMPS subunit B 2ywb – TtGMPS – Thermus thermophilus 2ywc – TtGMPS + XMP 3tqi – GMPS – Coxiella burnetii 1kxj – TmGMPS – Thermotoga maritima 2iss – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS 2a9v – GMPS – Thermoplasma acidophilum 2lxn, 7d40, 7d95 – MjGMPS subunit A – Methanocaldococcus jannaschii 7d96, 7d97 – MjGMPS subunit A (mutant) 6jp9 – MjGMPS subunit B + XMP 1gpm – GMPS + pyrophosphate + AMP – Escherichia coli 5tw7 – GMPS – Neisseria gonorrhoeae 7mo6 – GMPS – Aspergillus fumigatus 7sbc – GMPS – Acinetobacter baumannii

spinqualitylabelsall models Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate (PDB entry 2vxo) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image