PMID:11591349

Citation	Lee, JE, Cornell, KA, Riscoe, MK and Howell, PL (2001) Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure 9:941-53
Abstract	5'-methylthioadenosine/S-adenosyl-homocysteine (MTA/AdoHcy) nucleosidase catalyzes the irreversible cleavage of 5'-methylthioadenosine and S-adenosylhomocysteine to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. While this enzyme is crucial for the metabolism of AdoHcy and MTA nucleosides in many prokaryotic and lower eukaryotic organisms, it is absent in mammalian cells. This metabolic difference represents an exploitable target for rational drug design.
Links	PubMed
Keywords	Adenine/metabolism; Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Chemical; Models, Molecular; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry; Protein Structure, Quaternary; Protein Structure, Tertiary; Purine-Nucleoside Phosphorylase/chemistry; Ribose/metabolism; Sequence Homology, Amino Acid
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.