PHOSPHODIESTERASE I

Base Information

• Chemical Name: PHOSPHODIESTERASE I
• CAS No.: 9025-82-5
• Molecular Formula: NULL
• Molecular Weight: 0
• Mol file: 9025-82-5.mol

Synonyms:5'-Exonuclease;5'-Nucleotide phosphodiesterase; 5'-Phosphodiesterase; Alkalinephosphodiesterase; Alkaline phosphodiesterase I; Crotalus adamanteus venomexonuclease; E.C. 3.1.15.1; E.C. 3.1.4.1; Enzyme RP-1; Nuclease Amano G;Phosphodiesterase I; Polynucleotide 5'-phosphodiesterase; Snake venomphosphodiesterase; Venom phosphodiesterase

Chemical Property of PHOSPHODIESTERASE I

Chemical Property:

• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: −20°C

Purity/Quality:

98%,99%, ^*data from raw suppliers

Phosphodiesterase I from Crotalus adamanteus venom Type VI, crude dried venom, ≥0.01 unit/mg solid ^*data from reagent suppliers

Safty Information:

• Pictogram(s): T+
• Hazard Codes: T+
• Statements: 26/27/28
• Safety Statements: 36/37/39-45

MSDS Files:

Total 1 MSDS from other Authors

Useful:

• Uses: Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. It is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is used in phosphodiesterase activation assays to hydrolyze AMP. Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. It is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is used in phosphodiesterase activation assays to hydrolyze AMP. Product P3243 is from Crotalus adamanteus venom and is purified. Product P3243 has been used to hydrolyze tRNA with wyosine derivatives into mononucleosides. Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. It is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is used in phosphodiesterase activation assays to hydrolyze AMP. Product P3134 is from crude, dried Crotalus adamanteus venom.

Refernces

STEROIDAL SAPONINS FROM THE TUBERS OF DICHELOSTEMMA MULTIFLORUM AND THEIR INHIBITORY ACTIVITY ON CYCLIC-AMP PHOSPHODIESTERASE

10.1016/0031-9422(95)00117-P

The study focused on the phytochemical composition of the tubers of Dichelostemma multiflorum, a plant of the lily family native to the Pacific coast of the United States. The aim of the study was to isolate and identify steroidal saponins from the methanol extract of the tubers and evaluate their inhibitory activity against cAMP phosphodiesterase, which is essential for identifying compounds with medicinal potential. The researchers successfully isolated three new steroidal saponins along with two known saponins and evaluated their inhibitory activity. The chemicals used in the process included various solvents such as methanol, chloroform, and dioxane for extraction and chromatography, and reagents for acid and alkaline hydrolysis and derivatization for sugar analysis. The results showed that the isolated saponins, especially those with specific glycosylation patterns and acetyl groups, showed significant inhibitory activity against cAMP phosphodiesterase, indicating their potential use in the pharmaceutical field.

Pentacovalent phosphorus-containing models of P(V) H₂O- or enzyme-cAMP adducts. Nonchair conformations of the phosphorus-containing rings as determined by 1 H NMR spectroscopy and X-ray crystallography

10.1021/ja00177a002

The research aims to investigate the nonchair conformations of phosphorus-containing rings in models designed to mimic P(V) H2O-cAMP or enzyme-cAMP adducts. The study employs 'H NMR spectroscopy and X-ray crystallography to determine the configuration and conformation of a series of pentacovalent phosphorus-containing molecules (3-6). Their conclusions suggest that the 1,3,2-dioxaphosphorinane ring in these models adopts a nonchair (likely twist) conformation both in the crystal state and in solution, with the ring being apical/equatorial to phosphorus. The study postulates that this nonchair conformation could play a crucial role in the catalyzed hydrolysis of cAMP by phosphodiesterase, potentially assisting in the formation and scission of the P(V) adduct.