Chemical Formula: C10H12N5O7P
Chemical Formula C10H12N5O7P
Found 30 metabolite its formula value is C10H12N5O7P
Cyclic GMP
Cyclic-gmp, also known as cgmp or guanosine 3,5-cyclic monophosphate, is a member of the class of compounds known as 3,5-cyclic purine nucleotides. 3,5-cyclic purine nucleotides are purine nucleotides in which the oxygen atoms linked to the C3 and C5 carbon atoms of the ribose moiety are both bonded the same phosphorus atom of the phosphate group. Cyclic-gmp is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Cyclic-gmp can be found in a number of food items such as common sage, jews ear, java plum, and pepper (c. chinense), which makes cyclic-gmp a potential biomarker for the consumption of these food products. Cyclic-gmp can be found primarily in blood and cerebrospinal fluid (CSF), as well as throughout most human tissues. Cyclic-gmp exists in all living species, ranging from bacteria to humans. Moreover, cyclic-gmp is found to be associated with headache. Guanosine cyclic 3,5-(hydrogen phosphate). A guanine nucleotide containing one phosphate group which is esterified to the sugar moiety in both the 3- and 5-positions. It is a cellular regulatory agent and has been described as a second messenger. Its levels increase in response to a variety of hormones, including acetylcholine, insulin, and oxytocin and it has been found to activate specific protein kinases. (From Merck Index, 11th ed). Acquisition and generation of the data is financially supported in part by CREST/JST. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS
Guanosine 2',3'-cyclic phosphate
2,3-Cyclic GMP is a cyclic guanosine derivative that is a precursor to 3-GMP. The enzyme 23-cyclic-nucleotide 2-phosphodiesterase (E.C. 3.1.4.16) catalyses the hydrolysis of both 2,3-cyclic AMP and 2,3-cyclic GMP into 3-AMP and 3-GMP, respectively, at the 3-terminal of RNA. 2,3-cyclic phosphate termini are produced, as either intermediates or final products, during RNA cleavage by many different endoribonucleases. The enzyme RNA 3-phosphate cyclase also converts the 3-terminal phosphate in RNA into the 2,3-cyclic phosphodiester in the ATP-dependent reaction which involves formation of the covalent cyclase-AMP and the RNA-N3 pp5 A intermediates (PMID: 10397337). This enzyme could be involved in the maintenance of cyclic ends in tRNA splicing intermediates or in the cyclization of the 3 end of U6 snRNA (PMID: 9184239). Guanosine-2,3-cyclic phosphate is capable of blocking DNA synthesis in vitro (PMID: 7528887). 2, 3-cGMP seems to preferentially stimulate mature T-cells while 3, 5-cGMP preferentially acts on B-cells (PMID: 163786).
Molybdopterin precursor Z
Molybdopterin precursor Z is a molybdopterin precursor. All molybdenum-containing oxotransferases use molybdenum in the form of a pterin-containing cofactor. In some of these enzymes, this cofactor consists of molybdenum ligated to a phosphorylated pterin, called molybdopterin (MPT). MPT is a tricyclic pyranopterin containing a cis-dithiolene group. Together, the metal and the pterin moiety form the redox reactive molybdenum cofactor (MoCo). Conversion of precursor Z to molybdopterin requires the opening of a cyclic phosphate to produce a terminal mono-ester and the transfer of sulfur to generate the dithiolene function essential for molybdenum ligation. Molybdopterin (MPT)-synthase is the enzyme necessary for the conversion of precursor Z into molybdopterin. The large and small subunits of molybdopterin synthase are both encoded from a single gene by overlapping open reading frames. Mutations in patients with deficiencies in MoCo biosynthesis usually occur in the enzymes catalyzing the first and second steps of biosynthesis, leading to the formation of precursor Z and MPT, respectively. The second step is catalyzed by the heterotetrameric MPT synthase protein consisting of two large (MoaE) and two small (MoaD) subunits with the MoaD subunits located at opposite ends of a central MoaE dimer. Previous studies have determined that the conversion of the sulfur- and metal-free precursor Z to MPT by MPT synthase involves the transfer of sulfur atoms from a C-terminal MoaD thiocarboxylate to the C-1 and C-2 positions of precursor Z. [HMDB] Molybdopterin precursor Z is a molybdopterin precursor. All molybdenum-containing oxotransferases use molybdenum in the form of a pterin-containing cofactor. In some of these enzymes, this cofactor consists of molybdenum ligated to a phosphorylated pterin, called molybdopterin (MPT). MPT is a tricyclic pyranopterin containing a cis-dithiolene group. Together, the metal and the pterin moiety form the redox reactive molybdenum cofactor (MoCo). Conversion of precursor Z to molybdopterin requires the opening of a cyclic phosphate to produce a terminal mono-ester and the transfer of sulfur to generate the dithiolene function essential for molybdenum ligation. Molybdopterin (MPT)-synthase is the enzyme necessary for the conversion of precursor Z into molybdopterin. The large and small subunits of molybdopterin synthase are both encoded from a single gene by overlapping open reading frames. Mutations in patients with deficiencies in MoCo biosynthesis usually occur in the enzymes catalyzing the first and second steps of biosynthesis, leading to the formation of precursor Z and MPT, respectively. The second step is catalyzed by the heterotetrameric MPT synthase protein consisting of two large (MoaE) and two small (MoaD) subunits with the MoaD subunits located at opposite ends of a central MoaE dimer. Previous studies have determined that the conversion of the sulfur- and metal-free precursor Z to MPT by MPT synthase involves the transfer of sulfur atoms from a C-terminal MoaD thiocarboxylate to the C-1 and C-2 positions of precursor Z.
precursor Z
A linear-fused organic heterotetracyclic compound consisting of a [1,3,2]dioxaphosphinane fused to a pyran-4-one ring which is in turn fused to a pteridine ring system.
3,5-cyclic GMP
A 3,5-cyclic purine nucleotide in which the purine nucleobase is specified as guanidine.
Cyclic GMP
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8-amino-2-hydroxy-4a,5a,9,11,11a,12a-hexahydro[1,3,2]dioxaphosphinino[4,5:5,6]pyrano[3,2-g]pteridine-10,12(4H,6H)-dione 2-oxide
(1R,10R)-5-amino-14-hydroxy-14-oxo-13,15,18-trioxa-2,4,6,9-tetraza-14lambda5-phosphatetracyclo[8.8.0.03,8.012,17]octadeca-3(8),4-diene-7,11-dione
(4aR,6R,7R,7aS)-6-(6-amino-1-oxo-9H-1lambda(5)-purin-9-yl)-2,7-dihydroxytetrahydro-2H,4H-2lambda(5)-furo[3,2-d][1,3,2]dioxaphosphinin-2-one
8,5-Cyclo-2-deoxyguanosine monophosphate
An organic heterotetracyclic compound obtained by intramolecular formation of a C-C bond between positions 8 and 5 of dGMP.
5-Amino-11,14-dihydroxy-14-oxo-13,15,18-trioxa-2,4,6,9-tetraza-14lambda5-phosphatetracyclo[8.8.0.03,8.012,17]octadeca-3(8),4,11-trien-7-one
2,3-Cyclic GMP
A 2,3-cyclic purine nucleotide in which guanosine is used as the parent nucleoside.
3-AMP(2-)
The organophosphate oxoanion which results from the removal of two protons from the phosphate group of 3-AMP; major species at pH 7.3.
2-deoxyguanosine 5-monophosphate(2-)
A 2-deoxyribonucleoside 5-monophosphate(2-) obtained by deprotonation of the phosphate OH groups of 2-deoxyguanosine 5-monophosphate (dGMP).
8-oxo-dAMP(2-)
An organophosphate oxoanion obtained by deprotonation of the diphosphate OH groups of 8-oxo-dAMP.
2-amino-9-(2,7-dihydroxy-2-oxo-4a,6,7,7a-tetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinin-6-yl)-3H-purin-6-one
Adenosine 2-phosphate(2-)
An organophosphate oxoanion obtained by removal of two protons from the phosphate group of adenosine 2-phosphate; major species at pH 7.3.
adenosine 5-monophosphate(2-)
A nucleoside 5-monophosphate(2-) that results from the removal of two protons from the phosphate group of adenosine 5-monophosphate (AMP).
Guanosine 3'5-cyclic monophosphate
cGMP. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=7665-99-8 (retrieved 2024-07-02) (CAS RN: 7665-99-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).