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Literature summary for 2.4.2.28 extracted from

  • Cacciapuoti, G.; Moretti, M.A.; Forte, S.; Brio, A.; Camardella, L.; Zappia, V.; Porcelli, M.
    Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds (2004), Eur. J. Biochem., 271, 4834-4844.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus furiosus

General Stability

General Stability Organism
transition midpoint for guanidinium chloride-induced unfolding is 3.0 M after 22 h incubation. The value decreases to 2.0 M in presence of 30 mM dithiothreitol. The guanidinium chloride-induced unfolding is completely reversible Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pyrococcus furiosus

Renatured (Commentary)

Renatured (Comment) Organism
guanidinium chloride-induced unfolding is completely reversible Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-methylthioadenosine + phosphate
-
Pyrococcus furiosus adenine + 5-methylthio-D-ribose 1-phosphate
-
?

Synonyms

Synonyms Comment Organism
methylthioadenosine phosphorylase
-
Pyrococcus furiosus