CHEBI:58115 - guanosine 5'-monophosphate(2−)

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ChEBI Name guanosine 5'-monophosphate(2−) ChEBI ID CHEBI:58115 ChEBI ASCII Name guanosine 5'-monophosphate(2-) Definition A nucleoside 5'-monophosphate(2−) that results from the removal of two protons from the phosphate group of GMP. Stars This entity has been manually annotated by the ChEBI Team. Supplier Information No supplier information found for this compound. Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C10H12N5O8P Net Charge -2 Average Mass 361.20470 Monoisotopic Mass 361.04345 InChI InChI=1S/C10H14N5O8P/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(23-9)1-22-24(19,20)21/h2-3,5-6,9,16-17H,1H2,(H2,19,20,21)(H3,11,13,14,18)/p-2/t3-,5-,6-,9-/m1/s1 InChIKey RQFCJASXJCIDSX-UUOKFMHZSA-L SMILES Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O Metabolite of Species Details Saccharomyces cerevisiae (NCBI:txid4932) Source: yeast.sf.net See: PubMed Homo sapiens (NCBI:txid9606) See: DOI Roles Classification Biological Role(s): Saccharomyces cerevisiae metabolite Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ). human metabolite Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens). View more via ChEBI Ontology ChEBI Ontology Outgoing guanosine 5'-monophosphate(2−) (CHEBI:58115) has role Saccharomyces cerevisiae metabolite (CHEBI:75772) guanosine 5'-monophosphate(2−) (CHEBI:58115) has role human metabolite (CHEBI:77746) guanosine 5'-monophosphate(2−) (CHEBI:58115) is a nucleoside 5'-monophosphate(2−) (CHEBI:58043) guanosine 5'-monophosphate(2−) (CHEBI:58115) is conjugate base of guanosine 5'-monophosphate (CHEBI:17345) Incoming Nε-(5'-guanylyl)-L-lysine(1−) residue (CHEBI:138294) has functional parent guanosine 5'-monophosphate(2−) (CHEBI:58115) N2-(1-hydroxy-2-oxoethyl)-GMP(2−) (CHEBI:141576) has functional parent guanosine 5'-monophosphate(2−) (CHEBI:58115) N2-(1-hydroxy-2-oxopropyl)-GMP(2−) (CHEBI:141575) has functional parent guanosine 5'-monophosphate(2−) (CHEBI:58115) N2-(ADP-D-ribosyl)-GMP(4−) (CHEBI:142717) has functional parent guanosine 5'-monophosphate(2−) (CHEBI:58115) disodium 5'-guanylate (CHEBI:132932) has part guanosine 5'-monophosphate(2−) (CHEBI:58115) guanosine 5'-monophosphate (CHEBI:17345) is conjugate acid of guanosine 5'-monophosphate(2−) (CHEBI:58115) IUPAC Name 5'-O-phosphonatoguanosine Synonyms Sources GMP UniProt GMP ChEBI GMP dianion ChEBI GMP(2−) ChEBI guanosine 5'-phosphate ChEBI guanosine 5'-phosphate dianion ChEBI guanosine 5'-phosphate(2−) ChEBI Registry Number Type Source 3598735 Reaxys Registry Number Reaxys Citation Keough DT, Hocková D, Holý A, Naesens LM, Skinner-Adams TS, Jersey Jd, Guddat LW (2009) Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: a new class of antimalarial therapeutics. Journal of medicinal chemistry 52, 4391-4399 [PubMed:19527031] [show Abstract] The purine salvage enzyme hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) is essential for purine nucleotide and hence nucleic acid synthesis in the malaria parasite, Plasmodium falciparum. Acyclic nucleoside phosphonates (ANPs) are analogues of the nucleotide product of the reaction, comprising a purine base joined by a linker to a phosphonate moiety. K(i) values for 19 ANPs were determined for Pf HGXPRT and the corresponding human enzyme, HGPRT. Values for Pf HGXPRT were as low as 100 nM, with selectivity for the parasite enzyme of up to 58. Structures of human HGPRT in complex with three ANPs are reported. On binding, a large mobile loop in the free enzyme moves to partly cover the active site. For three ANPs, the IC(50) values for Pf grown in cell culture were 1, 14, and 46 microM, while the cytotoxic concentration for the first compound was 489 microM. These results provide a basis for the design of potent and selective ANP inhibitors of Pf HGXPRT as antimalarial drug leads. Last Modified 05 December 2017