P9041
Phosphodiesterase II from bovine spleen
lyophilized powder, ≥5.0 units/mg protein
Synonym(s):
3′-Exonuclease, Spleen exonuclease, Spleen phosphodiesterase
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About This Item
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form
lyophilized powder
Quality Level
specific activity
≥5.0 units/mg protein
mol wt
65 kDa
UniProt accession no.
foreign activity
5′-Nucleotidase ≤1% of base activity
storage temp.
−20°C
Gene Information
cow ... PDE2A(281971)
General description
Research area: Cell signaling. Phosphodiesterase (PDE) II belongs to the PDE superfamily and includes subtypes from one to 11.[1] They exist as a dimer and comprise of N-terminal regulatory domain, C-terminal prenylated domain, and a Zn2+containing catalytic domain.[1] The bovine spleen PDE2 corresponds to a molecular weight of 65 kDa. It requires divalent cations for its enzymatic activity and has an optimum pH of 7.5.[2]
Application
Phosphodiesterase (PDE) is any enzyme that is used to break phosphodiester bonds. It is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase II has been used in the enzymatic digestions of purified proteins such as the P8-dGMP complex[3]. Bovine spleen phosphodiesterase has been used to digest N-cadherin[4]. Phosphodiesterase II from bovine is suitable for sequential and end-group analysis of poly and oligonucleotides. It may be used in kinetic studieson substrate degradation of macro-molecules.
Phosphodiesterase II from bovine spleen has been used in the:
- excision of pyridyloxobutyl (POB) base adducts from DNA[5]
- digestion of DNA prior to cycloadenosine enrichment[6]
- hydrolysis of DNA from blue mussels gill tissue into deoxyribonucleoside 3′-monophosphates[7]
The product has been used in the characterization of polynucleotide chain length, base composition, and identity of terminal nucleotide. The enzyme has also been used in excision of pyridyloxobutyl (POB) base adducts from DNA.[5] Furthermore, it has been used along with micrococcal endonuclease to hydrolyze purified DNA to 3 -nucleoside monophosphates.[8]
Biochem/physiol Actions
Hydrolyzes RNA, RNA-Core, 3′-alkyl- and 3′-aryl-nucleoside phosphates, and polydeoxyribonucleotides with 3′-phosphate end groups to 3′-mononucleotides.
Polynucleotides having 5′-phosphomonoester end groups are not attacked.
Polynucleotides having 5′-phosphomonoester end groups are not attacked.
Phosphodiesterase (PDE) breaks phosphodiester bonds.[9] 3-Isobutyl-methylxanthine (IBMX) is a potential PDE2 inhibitor.[10]
The enzyme acts on poly(A), poly(U), and poly(I). Native DNA and poly(C) are quite resistant to the action of this enzyme.
Unit Definition
One unit will produce acid soluble nucleotides equivalent to a ΔA260 of 16 in 30 min at pH 6.5 at 37 °C, in a 2.0 mL reaction mixture. Substrate: RNA-Core. Actual A260 is measured on the supernatant after precipitation of the unhydrolyzed RNA with uranyl acetate-perchloric acid reagent.
Analysis Note
Protein determined by biuret
Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Hisao Saneyoshi et al.
The Journal of organic chemistry, 70(25), 10453-10460 (2005-12-06)
[reaction: see text] An effective method for the synthesis of 2'-O-cyanoethylated oligoribonucleotides as a new class of 2'-O-modified RNAs was developed. The reaction of appropriately protected ribonucleoside derivatives with acrylonitrile in t-BuOH in the presence of Cs2CO3 gave 2'-O-cyanoethylated ribonucleoside
Phosphodiesterase inhibitors, congestive heart failure, and sudden death: Time for re-evaluation
Varma A, et al.
Congestive Heart Failure (Greenwich, Conn.), 18(4), 229-233 (2012)
María Jesús Juan-Fita et al.
European journal of pharmacology, 512(2-3), 207-213 (2005-04-21)
The effects of phosphodiesterase (PDE) inhibitors (1-3) on tissue cAMP concentrations and the inotropic responses to dobutamine and glucagon were investigated in electrically driven right ventricular strips of the rat heart. Dobutamine (0.3-100 microM) produced a concentration-dependent positive inotropic effect
Hong Feng et al.
Biochemistry, 44(34), 11486-11495 (2005-08-24)
Endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3' side one nucleotide from a deaminated base lesion. Site-directed mutagenesis analysis was conducted at seven conserved motifs of the thermostable
Dynamic regulation of cAMP signaling by cGMP in the cardiovascular system: roles of phosphodiesterase 2 and phosphodiesterase 3 enzymes.
Donald H Maurice
Proceedings of the Western Pharmacology Society, 46, 32-36 (2004-01-01)
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