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Literature summary extracted from

  • Timofeev, V.I.; Zhukhlistova, N.E.; Abramchik, Y.A.; Muravieva, T.I.; Esipov, R.S.; Kuranova, I.P.
    Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir (2018), Acta Crystallogr. Sect. F, 74, 402-409 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.4.2.1 drug development owing to their key role in the purine salvage pathway, PNPs are attractive targets for drug design against some pathogens Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.1 gene pnp, sequence comparisons of Escherichia coli enzyme with human and Bacillus subtilis enzymes, recombinant expression in Escherichia coli strain BL21(DE3)/pERPUPHOI Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.1 purified enzyme PNP in complex with inhibitor ACV, liquid diffusion method, mixing of 0.0035 ml of 32 mg/ml protein in 0.02 M Tris-HCl, pH 7.5, with 0.0035 ml of reservoir solution containing 25% ammonium sulfate, 0.05 M sodium citrate, pH 4.9, 0.04% sodium azide, and 5 mM acycloguanosine, and equilbration against 0.18 ml of reservoir solution, X-ray diffraction structure determination at 2.32 A resolution using the molecular replacement method. The ACV molecule is observed in two conformations and sulfate ions are located in both the nucleoside-binding and phosphate-binding pockets of the enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.1 acyclovir ACV, an acyclic derivative of the PNP substrate guanosine, an acyclic analogue of 2'-deoxyguanosine, that is used as an antiviral drug for the treatment of some human viral infections. The ACV molecule occupies the nucleoside-binding pocket in the active-site cavity, where it adopts two conformations. Sulfate ions are located in both the nucleoside-binding and phosphate-binding pockets of the enzyme. Binding structure, overview Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.1 adenosine + phosphate Escherichia coli
-
 adenine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 guanosine + phosphate Escherichia coli
-
 guanine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 inosine + phosphate Escherichia coli
-
 hypoxanthine + alpha-D-ribose 1-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.1 Escherichia coli P0ABP8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.1 recombinant enzyme from Escherichia coli strain BL21(DE3)/pERPUPHOI cell extract supernatant by anion exchange chromatography, ultrafiltration, and gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.1 adenosine + phosphate
-
 Escherichia coli adenine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 guanosine + phosphate
-
 Escherichia coli guanine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 inosine + phosphate
-
 Escherichia coli hypoxanthine + alpha-D-ribose 1-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.4.2.1 homohexamer the hexameric molecule can be considered as a trimer of dimers, where each dimer contains two complete active sites. Each monomer consists of a central core comprising mixed beta-sheet surrounded by alpha-helices with an extended C-terminal alpha7 helix. The active sites are located within the deep cavity between the dimer subunits and comprise amino-acid residues from both subunits. The active-site cavity is predominantly lined by hydrophobic amino acids from strands beta5, beta7, beta8, beta9, and beta10 and helix alpha7. The adjacent dimer subunit contributes the side chains of His4* and Arg43* to the active site Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.4.2.1 DeoD
-
 Escherichia coli
2.4.2.1 PNP
-
 Escherichia coli
2.4.2.1 purine nucleoside phosphorylase
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.4.2.1 evolution the enzyme belongs to the type I PNP family of hexameric enzymes Escherichia coli
2.4.2.1 metabolism PNPs play a key role in the purine salvage pathway Escherichia coli
2.4.2.1 physiological function the enzyme catalyzes the reversible phosphorolysis of purine ribonucleosides Escherichia coli