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Literature summary for 2.4.2.1 extracted from

  • Stefanic, Z.; Narczyk, M.; Mikleusevic, G.; Wielgus-Kutrowska, B.; Bzowska, A.; Luic, M.
    New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A (2012), FEBS Lett., 586, 967-971.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
ternary complex of enzyme with a phosphate ion and formycin A, to 0.975 A resolution. The structure reveals, in some active sites, an unexpected binding site for phosphate and exhibits a stoichiometry of two phosphate molecules per enzyme subunit. In these active sites, the phosphate and nucleoside molecules are found not to be in direct contact but being bridged by three water molecules Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABP8
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