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Literature summary for 3.2.2.9 extracted from

  • Lee, J.E.; Smith, G.D.; Horvatin, C.; Huang, D.J.; Cornell, K.A.; Riscoe, M.K.; Howell, P.L.
    Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis (2005), J. Mol. Biol., 352, 559-574.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method. Three structures along the reaction coordinate of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase are solved: Asp197Asn 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5'-methylthioadenosine complex, Glu12Gln 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5-methylthioribose/adenine complex, and wild-type 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/glycerol complex. These structures provide insight into the conformational flexibility of the enzyme and nucleoside during catalysis Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AF12
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Three structures along the reaction coordinate of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase are solved: Asp197Asn 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5'-methylthioadenosine complex, Glu12Gln 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5-methylthioribose/adenine complex, and wild-type 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/glycerol complex. These structures provide insight into the conformational flexibility of the enzyme and nucleoside during catalysis Escherichia coli ?
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Synonyms

Synonyms Comment Organism
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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Escherichia coli
MTA/AdoHcy nucleosidase
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Escherichia coli
MTAN
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Escherichia coli