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Literature summary for 3.2.2.16 extracted from

  • Lee, J.E.; Cornell, K.A.; Riscoe, M.K.; Howell, P.L.
    Structure of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis (2003), J. Biol. Chem., 278, 8761-8770.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, complexed with formycin A and 5'-methylthiotubercidin Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5'-methylthiotubercidin competitive inhibition Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli key role in biological methylation, polyamine biosynthesis, methionine recycling and bacterial quorum sensing ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-methylthioadenosine + H2O
-
Escherichia coli 5-methylthio-D-ribose + adenine
-
ir
additional information key role in biological methylation, polyamine biosynthesis, methionine recycling and bacterial quorum sensing Escherichia coli ?
-
?
S-adenosylhomocysteine + H2O
-
Escherichia coli adenine + S-ribosylhomocysteine
-
ir

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.01
-
5'-methylthiotubercidin
-
Escherichia coli