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Cas Database

85-32-5

85-32-5

Identification

  • Product Name:5'-Guanylic acid

  • CAS Number: 85-32-5

  • EINECS:201-598-8

  • Molecular Weight:363.224

  • Molecular Formula: C10H14 N5 O8 P

  • HS Code:

  • Mol File:85-32-5.mol

Synonyms:5'-GMP; E626; GMP; Guanidine monophosphate; Guanosine 5'-(dihydrogen phosphate);Guanosine 5'-monophosphate; Guanosine 5'-phosphate; Guanosine 5'-phosphoricacid; Guanosine monophosphate; Guanylic acid

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Safety information and MSDS view more

  • Pictogram(s):Xi

  • Hazard Codes:Xi

  • Signal Word:No signal word.

  • Hazard Statement:none

  • First-aid measures: General adviceConsult a physician. Show this safety data sheet to the doctor in attendance.If inhaled If breathed in, move person into fresh air. If not breathing, give artificial respiration. Consult a physician. In case of skin contact Wash off with soap and plenty of water. Consult a physician. In case of eye contact Rinse thoroughly with plenty of water for at least 15 minutes and consult a physician. If swallowed Never give anything by mouth to an unconscious person. Rinse mouth with water. Consult a physician.

  • Fire-fighting measures: Suitable extinguishing media Use water spray, alcohol-resistant foam, dry chemical or carbon dioxide. Wear self-contained breathing apparatus for firefighting if necessary.

  • Accidental release measures: Use personal protective equipment. Avoid dust formation. Avoid breathing vapours, mist or gas. Ensure adequate ventilation. Evacuate personnel to safe areas. Avoid breathing dust. For personal protection see section 8. Prevent further leakage or spillage if safe to do so. Do not let product enter drains. Discharge into the environment must be avoided. Pick up and arrange disposal. Sweep up and shovel. Keep in suitable, closed containers for disposal.

  • Handling and storage: Avoid contact with skin and eyes. Avoid formation of dust and aerosols. Avoid exposure - obtain special instructions before use.Provide appropriate exhaust ventilation at places where dust is formed. For precautions see section 2.2. Store in cool place. Keep container tightly closed in a dry and well-ventilated place.

  • Exposure controls/personal protection:Occupational Exposure limit valuesBiological limit values Handle in accordance with good industrial hygiene and safety practice. Wash hands before breaks and at the end of workday. Eye/face protection Safety glasses with side-shields conforming to EN166. Use equipment for eye protection tested and approved under appropriate government standards such as NIOSH (US) or EN 166(EU). Skin protection Wear impervious clothing. The type of protective equipment must be selected according to the concentration and amount of the dangerous substance at the specific workplace. Handle with gloves. Gloves must be inspected prior to use. Use proper glove removal technique(without touching glove's outer surface) to avoid skin contact with this product. Dispose of contaminated gloves after use in accordance with applicable laws and good laboratory practices. Wash and dry hands. The selected protective gloves have to satisfy the specifications of EU Directive 89/686/EEC and the standard EN 374 derived from it. Respiratory protection Wear dust mask when handling large quantities. Thermal hazards

Supplier and reference price

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  • Manufacture/Brand:TRC
  • Product Description:5-GuanylicAcid
  • Packaging:500mg
  • Price:$ 45
  • Delivery:In stock
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  • Manufacture/Brand:TRC
  • Product Description:5-GuanylicAcid
  • Packaging:5g
  • Price:$ 150
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  • Manufacture/Brand:Sigma-Aldrich
  • Product Description:(5-(2-Amino-6-oxo-1H-purin-9(6H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl dihydrogen phosphate
  • Packaging:1 g
  • Price:$ 388
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  • Manufacture/Brand:Medical Isotopes, Inc.
  • Product Description:Guanosine5?-monophosphate
  • Packaging:50 g
  • Price:$ 575
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  • Manufacture/Brand:Crysdot
  • Product Description:((2R,3S,4R,5R)-5-(2-Amino-6-oxo-1H-purin-9(6H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyldihydrogenphosphate 97%
  • Packaging:100g
  • Price:$ 535
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  • Manufacture/Brand:Crysdot
  • Product Description:((2R,3S,4R,5R)-5-(2-Amino-6-oxo-1H-purin-9(6H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyldihydrogenphosphate 97%
  • Packaging:25g
  • Price:$ 178
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  • Manufacture/Brand:Chemenu
  • Product Description:((2R,3S,4R,5R)-5-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyldihydrogenphosphate 97%
  • Packaging:100g
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  • Manufacture/Brand:Biosynth Carbosynth
  • Product Description:Guanosine 5'-monophosphate
  • Packaging:50 g
  • Price:$ 175
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  • Manufacture/Brand:Biosynth Carbosynth
  • Product Description:Guanosine 5'-monophosphate
  • Packaging:250 g
  • Price:$ 675
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  • Manufacture/Brand:Biosynth Carbosynth
  • Product Description:Guanosine 5'-monophosphate
  • Packaging:100 g
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Relevant articles and documentsAll total 50 Articles be found

Biochemical characterization of recombinant guaA-encoded guanosine monophosphate synthetase (EC 6.3.5.2) from Mycobacterium tuberculosis H37Rv strain

Franco, Tathyana Mar A.,Rostirolla, Diana C.,Ducati, Rodrigo G.,Lorenzini, Daniel M.,Basso, Luiz A.,Santos, Diogenes S.

, p. 1 - 11 (2012)

Administration of the current tuberculosis (TB) vaccine to newborns is not a reliable route for preventing TB in adults. The conversion of XMP to GMP is catalyzed by guaA-encoded GMP synthetase (GMPS), and deletions in the Shiguella flexneri guaBA operon led to an attenuated auxotrophic strain. Here we present the cloning, expression, and purification of recombinant guaA-encoded GMPS from Mycobacterium tuberculosis (MtGMPS). Mass spectrometry data, oligomeric state determination, steady-state kinetics, isothermal titration calorimetry (ITC), and multiple sequence alignment are also presented. The homodimeric MtGMPS catalyzes the conversion of XMP, MgATP, and glutamine into GMP, ADP, PP i, and glutamate. XMP, NH4+, and Mg2+ displayed positive homotropic cooperativity, whereas ATP and glutamine displayed hyperbolic saturation curves. The activity of ATP pyrophosphatase domain is independent of glutamine amidotransferase domain, whereas the latter cannot catalyze hydrolysis of glutamine to NH3 and glutamate in the absence of substrates. ITC data suggest random order of binding of substrates, and PPi is the last product released. Sequence comparison analysis showed conservation of both Cys-His-Glu catalytic triad of N-terminal Class I amidotransferase and of amino acid residues of the P-loop of the N-type ATP pyrophosphatase family.

Histidine and thermal copolymers of amino acids containing histidine as prebiotic inhibitor for the template-directed formation of oligoguanylate on a poly(C) template

Kawamura, Kunio,Kuranoue, Kazuhiro

, p. 1070 - 1071 (2001)

Possibility of the cooperative chemical evolution of nucleic acids and proteins has been investigated using the template-directed formation of oligoguanylate with amino acids and thermal copolymers of amino acids, in which strong inhibition by histidine containing thermal copolymer and histidine itself was observed. The inhibition is regarded as prebiotic enzymatic activities for the hydrolysis of activated nucleotide monomer and the formation of pyrophospho-capped oligoguanylate.

Characterization of complexes of nucleoside-5′-phosphorothioate analogues with zinc ions

Sayer, Alon Haim,Itzhakov, Yehudit,Stern, Noa,Nadel, Yael,Fischer, Bilha

, p. 10886 - 10896 (2013)

On the basis of the high affinity of Zn2+ to sulfur and imidazole, we targeted nucleotides such as GDP-β-S, ADP-β-S, and AP3(β-S)A, as potential biocompatible Zn2+-chelators. The thiophosphate moiety enhanced the stability of the Zn2+- nucleotide complex by about 0.7 log units. ATP-α,β-CH 2-γ-S formed the most stable Zn2+-complex studied here, log K 6.50, being ~0.8 and ~1.1 log units more stable than ATP-γ-S-Zn2+ and ATP-Zn2+ complexes, and was the major species, 84%, under physiological pH. Guanine nucleotides Zn2+ complexes were more stable by 0.3-0.4 log units than the corresponding adenine nucleotide complexes. Likewise, AP3(β-S)A-zinc complex was ~0.5 log units more stable than AP3A complex. 1H- and 31P NMR monitored Zn2+ titration showed that Zn 2+ coordinates with the purine nucleotide N7-nitrogen atom, the terminal phosphate, and the adjacent phosphate. In conclusion, replacement of a terminal phosphate by a thiophosphate group resulted in decrease of the acidity of the phosphate moiety by approximately one log unit, and increase of stability of Zn2+-complexes of the latter analogues by up to 0.7 log units. A terminal phosphorothioate contributed more to the stability of nucleotide-Zn2+ complexes than a bridging phosphorothioate.

-

Lomakina,Grinewa

, (1965)

-

A phosphatase specific for nucleoside diphosphates.

GIBSON,AYENGAR,SANADI

, p. 536 - 538 (1955)

-

High Level Expression of XMP Aminase in Escherichia coli and Its Application for the Industrial Production of 5′-Guanylic Acid

Fujio, Tatsuro,Nishi, Tatsunari,Ito, Seiga,Maruyama, Akihiko

, p. 840 - 845 (1997)

To improve the efficiency of the enzymatic conversion of 5′-xanthylic acid (XMP) to 5′-guanylic acid (GMP), we attempted to increase the activity of the conversion enzyme, XMP aminase (GMP synthetase) encoded by the guaA gene in Escherichia coli. By connecting the PL promoter of λ phage, the SD sequence of trpL of E. coli, and ATG, at a suitable position upstream of the guaA gene, we obtained plasmid pPLA66. Sequencing of the nucleotides of the upstream region of the guaA gene on pPLA66 showed that the C-terminal region of the guaB gene, which encodes IMP dehydrogenase, was conserved and a short peptide consisted of 14 amino acids was coded. E. coli MP347/pPLA66 showed an increase in the activity of approximately 370 times when compared with that of the strain MM294, and the amount of the enzyme protein represented approx. 34% of the total cellular protein. Strain MP347/pPLA66 was cultivated in a 5-liter jar fermentor using a medium which contained mainly corn steep liquor. The culture broth had high XMP aminase activity. In the conversion reaction using mixed broths consisted of 600ml of XMP-fermentation broth of Corynebacterium ammoniagenes KY13203 and 30 ml of cultured broth of E. coli MP347/pPLA66, a surfactant, Nymeen S-215 and xylene were added to the reaction mixture to make the cell membrane permeable to nucleotides. After 23 h of the reaction, 70mg/ml (131 mM) of GMP·Na2·7H2O was accumulated from 83 mg/ml (155 mM) of XMP·Na3 ·7H2O, without addition of ATP. The molar conversion yield was approx. 85%. The facts that the cell membrane was treated to allow nucleotides to permeate and that the conversion reaction proceeded well enough in spite of a small amount of E. coli cells indicate ATP was regenerated from AMP by C. ammoniagenes cells and supplied to E. coli cells. Therefore, it was considered that the coupling reaction between these two kind of strains was established.

Catalytic activity of human guanylate-binding protein 1 coupled to the release of structural restraints imposed by the C-terminal domain

Ince, Semra,Zhang, Ping,Kutsch, Miriam,Krenczyk, Oktavian,Shydlovskyi, Sergii,Herrmann, Christian

, p. 582 - 599 (2020/06/02)

Human guanylate-binding protein 1 (hGBP-1) shows a dimer-induced acceleration of the GTPase activity yielding GDP as well as GMP. While the head-to-head dimerization of the large GTPase (LG) domain is well understood, the role of the rest of the protein, particularly of the GTPase effector domain (GED), in dimerization and GTP hydrolysis is still obscure. In this study, with truncations and point mutations on hGBP-1 and by means of biochemical and biophysical methods, we demonstrate that the intramolecular communication between the LG domain and the GED (LG:GED) is crucial for protein dimerization and dimer-stimulated GTP hydrolysis. In the course of GTP binding and γ-phosphate cleavage, conformational changes within hGBP-1 are controlled by a chain of amino acids ranging from the region near the nucleotide-binding pocket to the distant LG:GED interface and lead to the release of the GED from the LG domain. This opening of the structure allows the protein to form GED:GED contacts within the dimer, in addition to the established LG:LG interface. After releasing the cleaved γ-phosphate, the dimer either dissociates yielding GDP as the final product or it stays dimeric to further cleave the β-phosphate yielding GMP. The second phosphate cleavage step, that is, the formation of GMP, is even more strongly coupled to structural changes and thus more sensitive to structural restraints imposed by the GED. Altogether, we depict a comprehensive mechanism of GTP hydrolysis catalyzed by hGBP-1, which provides a detailed molecular understanding of the enzymatic activity connected to large structural rearrangements of the protein. Database: Structural data are available in RCSB Protein Data Bank under the accession numbers: 1F5N, 1DG3, 2B92.

Helices on Interdomain Interface Couple Catalysis in the ATPPase Domain with Allostery in Plasmodium falciparum GMP Synthetase

Shivakumaraswamy, Santosh,Pandey, Nivedita,Ballut, Lionel,Violot, Sébastien,Aghajari, Nushin,Balaram, Hemalatha

, p. 2805 - 2817 (2020/06/25)

GMP synthetase catalyses the conversion of XMP to GMP through a series of reactions that include hydrolysis of Gln to generate ammonia in the glutamine amidotransferase (GATase) domain, activation of XMP to adenyl-XMP intermediate in the ATP pyrophosphatase (ATPPase) domain and reaction of ammonia with the intermediate to generate GMP. The functioning of GMP synthetases entails bidirectional domain crosstalk, which leads to allosteric activation of the GATase domain, synchronization of catalytic events and tunnelling of ammonia. Herein, we have taken recourse to the analysis of structures of GMP synthetases, site-directed mutagenesis and steady-state and transient kinetics on the Plasmodium falciparum enzyme to decipher the molecular basis of catalysis in the ATPPase domain and domain crosstalk. Our results suggest an arrangement at the interdomain interface, of helices with residues that play roles in ATPPase catalysis as well as domain crosstalk enabling the coupling of ATPPase catalysis with GATase activation. Overall, the study enhances our understanding of GMP synthetases, which are drug targets in many infectious pathogens.

Synthesis of ribonucleotides from the corresponding ribonucleosides under plausible prebiotic conditions within self-assembled supramolecular structures

Franco,Ascenso,Ilharco,Da Silva

supporting information, p. 2206 - 2209 (2020/02/20)

Abiotic synthesis of ribonucleotides, mainly at the 5′ position, from the corresponding ribonucleosides within self-assembled supramolecular structures, based on guanosine:borate hydrogels, was carried out in the temperature range of 70-90 °C, using urea and a phosphate source (K2HPO4 or hydroxyapatite). Phosphorylation is possible at initial concentrations of guanosine lower than 20 mM and it is more efficient using wet/dry cycles. Monoamidophosphate (and, eventually, diamidophosphate), diamidodiphosphate and pyrophosphate are intermediates in the synthesis of ribonucleotides. These conclusions are supported by NMR spectroscopy and mass spectrometry analysis of samples. On the other hand, after reaction, hydrogels can produce globular aggregates by the addition of water and decreasing temperature, thus confirming that ribonucleotides, once activated under suitable conditions, could form polyribonucleotides.

Thermophilic phosphoribosyltransferases Thermus thermophilus HB27 in nucleotide synthesis

Fateev, Ilja V.,Sinitsina, Ekaterina V.,Bikanasova, Aiguzel U.,Kostromina, Maria A.,Tuzova, Elena S.,Esipova, Larisa V.,Muravyova, Tatiana I.,Kayushin, Alexei L.,Konstantinova, Irina D.,Esipov, Roman S.

, p. 3098 - 3105 (2019/01/21)

Phosphoribosyltransferases are the tools that allow the synthesis of nucleotide analogues using multi-enzymatic cascades. The recombinant adenine phosphoribosyltransferase (TthAPRT) and hypoxanthine phosphoribosyltransferase (TthHPRT) from Thermus thermophilus HB27 were expressed in E.coli strains and purified by chromatographic methods with yields of 10-13 mg per liter of culture. The activity dependence of TthAPRT and TthHPRT on different factors was investigated along with the substrate specificity towards different heterocyclic bases. The kinetic parameters for TthHPRT with natural substrates were determined. Two nucleotides were synthesized: 9-(β-D-ribofuranosyl)-2-chloroadenine 5'-monophosphate (2-l-AMP) using TthAPRT and 1-(β-Dribofuranosyl)pyrazolo[3,4-d]pyrimidine-4-one 5'-monophosphate (Allop-MP) using TthPRT.

Cloning, expression and biochemical characterization of xanthine and adenine phosphoribosyltransferases from Thermus thermophilus HB8

Del Arco, Jon,Martinez, María,Donday, Manuel,Clemente-Suarez, Vicente Javier,Fernández-Lucas, Jesús

, p. 216 - 223 (2017/09/30)

Purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5′-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-α-D-ribosyl-1-pyrophosphate (PRPP) to purine nucleobases in the presence of Mg2+. Herein, we report a simple and thermostable process for the one-pot, one-step synthesis of some purine NMPs using xanthine phosphoribosyltransferase, XPRT or adenine phosphoribosyltransferase, APRT2, from Thermus thermophilus HB8. In this sense, the cloning, expression and purification of TtXPRT and TtAPRT2 is described for the first time. Both genes, xprt and aprt2 were expressed as his-tagged enzymes in E. coli BL21(DE3) and purified by a heat-shock treatment, followed by Ni-affinity chromatography and a final, polishing gel-filtration chromatography. Biochemical characterization revealed TtXPRT as a tetramer and TtAPRT2 as a dimer. In addition, both enzymes displayed a strong temperature dependence (relative activity >75% in a temperature range from 70 to 90 °C), but they also showed very different behaviour under the influence of pH. While TtXPRT is active in a pH range from 5 to 7, TtAPRT2 has a high dependence of alkaline conditions, showing highest activity values in a pH range from 8 to 10. Finally, substrate specificity studies were performed in order to explore their potential as industrial biocatalyst for NMPs synthesis.

Process route upstream and downstream products

Process route

C<sub>49</sub>H<sub>62</sub>N<sub>20</sub>O<sub>31</sub>P<sub>4</sub>

C49H62N20O31P4

cytidine monophosphate
63-37-6,30811-80-4

cytidine monophosphate

5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
venom phosphodiesterase; Product distribution;
C<sub>51</sub>H<sub>67</sub>N<sub>21</sub>O<sub>34</sub>P<sub>5</sub><sup>(1-)</sup>

C51H67N21O34P5(1-)

[5']adenylic acid mono-(2-amino-ethyl) ester
6216-59-7

[5']adenylic acid mono-(2-amino-ethyl) ester

cytidine monophosphate
63-37-6,30811-80-4

cytidine monophosphate

5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
nuclease P1; Product distribution;
5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
With ethylenediaminetetraacetic acid; Pyrococcus horikoshii OT3 ATP pyrophosphatase; ammonium chloride; magnesium chloride; Cleland's reagent; at 49.84 ℃; for 0.05h; pH=8; aq. buffer; Enzymatic reaction;
yeast RNA

yeast RNA

cytidine monophosphate
63-37-6,30811-80-4

cytidine monophosphate

5'-Uridylic Acid
58-97-9,27416-86-0

5'-Uridylic Acid

5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
With barley roots 5'-phosphodiesterase; at 70 ℃; for 0.5h; pH=5; aq. acetate buffer; Enzymatic reaction;
A(2'p5'A)3'p5'G

A(2'p5'A)3'p5'G

5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
With SVP (1 unit); In water; at 37 ℃; for 12h; Product distribution; HPLC analysis; no reaction with RNaseT2 or spleen phosphodiesterase;
A(2'p5'G)3'p5'U

A(2'p5'G)3'p5'U

5'-Uridylic Acid
58-97-9,27416-86-0

5'-Uridylic Acid

5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
With SVP (1 unit); In water; at 37 ℃; for 12h; Product distribution; HPLC analysis; no reaction with RNaseT2 or spleen phosphodiesterase;
A(2'p5'G)3'p5'C

A(2'p5'G)3'p5'C

cytidine monophosphate
63-37-6,30811-80-4

cytidine monophosphate

5'-adenosine monophosphate
61-19-8,24937-83-5,67583-85-1

5'-adenosine monophosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

Conditions
Conditions Yield
With SVP (1 unit); In water; at 37 ℃; for 12h; Product distribution; HPLC analysis; no reaction with RNaseT2 or spleen phosphodiesterase;
C<sub>21</sub>H<sub>27</sub>N<sub>10</sub>O<sub>18</sub>P<sub>3</sub><sup>(2-)</sup>

C21H27N10O18P3(2-)

7-methylguanine
578-76-7

7-methylguanine

7-methylguanosine-5'-monophosphate
10162-58-0,94889-81-3

7-methylguanosine-5'-monophosphate

7-methylguanosine 5'-diphosphate
26467-11-8

7-methylguanosine 5'-diphosphate

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

C<sub>10</sub>H<sub>15</sub>N<sub>5</sub>O<sub>11</sub>P<sub>2</sub>

C10H15N5O11P2

P<sup>1</sup>-(ribofuranos-5-yl) P<sup>3</sup>-(guanosin-5'-yl) triphosphate

P1-(ribofuranos-5-yl) P3-(guanosin-5'-yl) triphosphate

Conditions
Conditions Yield
With copper(II) nitrate; at 60 ℃; Rate constant; Product distribution; pH 5.0; kinetic study of the Cu2+-promoted cleavage of mRNA 5'-cap analogs; partial reactions; time-dependent product distribution; half-lives of the partial reactions;
adenylyl(2'-5')guanosine
22976-82-5

adenylyl(2'-5')guanosine

Guanosine 5'-monophosphate
85-32-5

Guanosine 5'-monophosphate

adenosine
58-61-7

adenosine

Conditions
Conditions Yield
With Vipera lebetina venom phosphodiesterase; at 37 ℃; for 1h; pH=9; aq. buffer; Enzymatic reaction;
Phosphoric acid (2R,3S,4R,5R)-5-(2-amino-6-hydroxy-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl ester (2R,3R,4R,5R)-2-(6-amino-purin-9-yl)-4-hydroxy-5-hydroxymethyl-tetrahydro-furan-3-yl ester

Phosphoric acid (2R,3S,4R,5R)-5-(2-amino-6-hydroxy-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl ester (2R,3R,4R,5R)-2-(6-amino-purin-9-yl)-4-hydroxy-5-hydroxymethyl-tetrahydro-furan-3-yl ester

guanosine 5'-monophosphate
85-32-5

guanosine 5'-monophosphate

adenosine
58-61-7

adenosine

Conditions
Conditions Yield
snake venom phosphodiesterase; Product distribution;

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