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Literature summary for 5.3.1.9 extracted from

  • Lin, H.Y.; Liu, J.H.; Cheng, K.L.; Lin, J.Y.; Liu, N.R.; Meng, M.
    A novel binding of GTP stabilizes the structure and modulates the activities of human phosphoglucose isomerase/autocrine motility factor (2015), Biochem. Biophys. Rep., 2, 14-22 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling and dynamics simulation of GTP binding Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
GTP competitive inhibitor, also compromises the autocrine motility factor function of the enzyme. The GTP-binding site partially overlaps with the catalytic site. In addition,GTP stabilizes the structure of PGI against heat- and detergent-induced denaturation. GTP is bound in a syn-conformation with the gamma-phosphate group located near the phosphate-binding loop and the ribose moiety positioned away from the active-site residues Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.063
-
GTP pH 7.5, 30°C Homo sapiens