Inhibition of nucleoside-binding sites by nucleoside analogues in Escherichia coli

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Inhibition of nucleoside-binding sites by nucleoside analogues in Escherichia coli.

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Nucleoside diphosphate (NDP) kinase from Escherichia coli was purified to homogeneity and was crystallized. Gel filtration analysis of the purified enzyme indicated that it forms a tetramer. The enzyme was phosphorylated with [gamma-32P]ATP, and the pH stability profile of the phosphoenzyme indicated that two different amino acid residues were phosphorylated. Both a histidine residue and serine...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 1974

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/1.3.491