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Literature summary for 3.2.2.30 extracted from

  • Ronning, D.R.; Iacopelli, N.M.; Mishra, V.
    Enzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase (2010), Protein Sci., 19, 2498-2510.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.2.30

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme only or in complex with formycin A or adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C Helicobacter pylori

Inhibitors

Inhibitors Comment Organism Structure
Tris weak inhibitor, about 20% residual activity at 250 mM Helicobacter pylori

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-amino-6-deoxyfutalosine + H2O Helicobacter pylori
-
 dehypoxanthine futalosine + adenine
-
 ?

Organism

Organism UniProt Comment Textmining
Helicobacter pylori Q9ZMY2
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography and Superdex 200 gel filtration Helicobacter pylori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-amino-6-deoxyfutalosine + H2O
-
 Helicobacter pylori dehypoxanthine futalosine + adenine
-
 ?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Helicobacter pylori

Synonyms

Synonyms Comment Organism
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
 Helicobacter pylori
MTAN
-
 Helicobacter pylori