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Gene Review:

ECs2779 - AMP nucleosidase

Escherichia coli O157:H7 str. Sakai

Leung, H.B. et al., Leung, H.B. et al., Zhang, Y. et al., Kvalnes-Krick, K. et al.

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Disease relevance of ECs2779

These results establish that the sequence DGSELTLD in E. coli AMP nucleosidase is not required for binding of AMP, MgATP, or inorganic phosphate [1].

High impact information on ECs2779

E. coli (Rec-) which contains the 9-kb plasmid of pBR322 containing amn overproduces AMP nucleosidase when grown in the presence of ampicillin [2].
Adenylate degradation experiments indicate that AMP nucleosidase is the major enzyme of AMP catabolism in E. coli [3].
The structure of unliganded AMN was determined at 2.7 A resolution, and structures of the complexes with either formycin 5'-monophosphate or inorganic phosphate were determined at 2.6 A and 3.0 A resolution, respectively [4].

Biological context of ECs2779

The episome from FP4102 was used as the source of DNA for cloning amn [2].

Analytical, diagnostic and therapeutic context of ECs2779

Restriction mapping of the plasmid has identified ClaI and PstI sites which appear to be within the amn locus [2].
Purified, homogeneous AMP nucleosidase gives a subunit Mr = 52,000 on denaturing gel electrophoresis and an oligomer molecular weight of approximately 280,000 by comparative gel filtration [3].

References

Mutagenic analysis of AMP nucleosidase from Escherichia coli. Deletion of a region similar to AMP deaminase and peptide characterization by mass spectrometry. Kvalnes-Krick, K., Labdon, J.E., Ma, X., Nieves, E., Schramm, V.L. J. Biol. Chem. (1993) [Pubmed]
The structural gene for AMP nucleosidase. Mapping, cloning, and overproduction of the enzyme. Leung, H.B., Schramm, V.L. J. Biol. Chem. (1984) [Pubmed]
Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme. Leung, H.B., Schramm, V.L. J. Biol. Chem. (1980) [Pubmed]
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases. Zhang, Y., Cottet, S.E., Ealick, S.E. Structure (Camb.) (2004) [Pubmed]

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