Literature

Abstract

During the isolation of RNA and DNA ligase from extracts of phage T4 infected Escherichia coli [ 1,2], I observed phosphatase activity which attacked 5'-phosphates of the oligonucleotide substrates. Since a characterized phosphatase would be useful in the structural studies of nucieotides and nucleic acids, puri~cation of the phosphatase activity was undertaken. The phosphatase activity is also present in uninfected Escherichia coli Al 9 extracts and the enzyme has unique substrate specificity.

DOI： 10.1016/0014-5793(81)80309-2

An Escherichia coli acid phosphatase which hydrolyzes preferentially nucleoside 3',5'‐diphosphates

FEBS Letters 1981.0

Polynucleotide phosphorylase from Streptomyces aureofaciens: Purification and properties

Biochimica et Biophysica Acta (BBA) - Protein Structure 1975.0

Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p -nitrophenyl phosphotriesters

Bioorganic & Medicinal Chemistry Letters 2000.0

Novel synthesis of nucleoside 5′-polyphosphates

Bioorganic & Medicinal Chemistry Letters 1996.0

Overexpression and Initial Characterization of the Chromosomal Aminoglycoside 3′- O -Phosphotransferase APH(3′)-IIb from Pseudomonas aeruginosa

Antimicrobial Agents and Chemotherapy 2007.0

Stereoelectronic factors in the binding of substrate analogs and inhibitors to purine nucleoside phosphorylase isolated from human erythrocytes