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Literature summary for 2.4.2.28 extracted from

  • Lee, J.E.; Settembre, E.C.; Cornell, K.A.; Riscoe, M.K.; Sufrin, J.R.; Ealick, S.E.; Howell, P.L.
    Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design (2004), Biochemistry, 43, 5159-5169.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13126
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-methylthioadenosine + phosphate structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design Homo sapiens adenine + 5-methylthio-D-ribose 1-phosphate
-
?

Synonyms

Synonyms Comment Organism
MTA phosphorylase
-
Homo sapiens
MTAP
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Homo sapiens