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Literature summary for 2.4.2.28 extracted from

  • Guan, R.; Ho, M.C.; Brenowitz, M.; Tyler, P.C.; Evans, G.B.; Almo, S.C.; Schramm, V.L.
    Entropy-driven binding of picomolar transition state analogue inhibitors to human 5-methylthioadenosine phosphorylase (2011), Biochemistry, 50, 10408-10417.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of apo MTAP and MTAP in complex with p-Cl-PhT-DADMe-ImmA are determined at 1.9 and 2.0 A resolution, respectively. Inhibitor binding causes condensation of the enzyme active site, reorganization at the trimer interfaces, the release of water from the active sites and subunit interfaces, and compaction of the trimeric structure. These structural changes cause the entropy-favored binding of transition state analogues Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
p-Cl-PhT-DADMe-ImmA
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13126
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine + phosphate
-
Homo sapiens adenine + D-ribose 1-phosphate
-
?

Synonyms

Synonyms Comment Organism
MTAP
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens