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[1]. 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 [2].
3D structures of GMP synthase
Updated on 04-June-2017
1wl8, 2d7j – PhGMPS subunit A – Pyrococcus horikoshii
2dpl, 3a4i - PhGMPS subunit B
2ywb – TtGMPS – Thermus thermophilus
3tqi – GMPS – Coxiella burnetii
1kxj – TmGMPS – Thermotoga maritima
2a9v – GMPS – Thermoplasma acidophilum
2lxn – GMPS subunit A – Methanocaldococcus jannaschii
2vpi – hGMPS glutaminase domain – human
2vxo - hGMPS + XMP
2ywc – TtGMPS + XMP
2iss – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS
1gpm – GMPS + pyrophosphate + AMP – Escherichia coli
5tw7 – GMPS – Neisseria gonorrhoeae
References
- ↑ Reddy BA, van der Knaap JA, Bot AG, Mohd-Sarip A, Dekkers DH, Timmermans MA, Martens JW, Demmers JA, Verrijzer CP. Nucleotide biosynthetic enzyme GMP synthase is a TRIM21-controlled relay of p53 stabilization. Mol Cell. 2014 Feb 6;53(3):458-70. doi: 10.1016/j.molcel.2013.12.017. Epub 2014, Jan 23. PMID:24462112 doi:http://dx.doi.org/10.1016/j.molcel.2013.12.017
- ↑ Welin M, Lehtio L, Johansson A, Flodin S, Nyman T, Tresaugues L, Hammarstrom M, Graslund S, Nordlund P. Substrate Specificity and Oligomerization of Human GMP Synthetase. J Mol Biol. 2013 Jun 28. pii: S0022-2836(13)00427-0. doi:, 10.1016/j.jmb.2013.06.032. PMID:23816837 doi:10.1016/j.jmb.2013.06.032
