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Literature summary for 2.3.2.13 extracted from

  • Pardin, C.; Roy, I.; Chica, R.A.; Bonneil, E.; Thibault, P.; Lubell, W.D.; Pelletier, J.N.; Keillor, J.W.
    Photolabeling of tissue transglutaminase reveals the binding mode of potent cinnamoyl inhibitors (2009), Biochemistry, 48, 3346-3353.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of enzyme photolabeled by 3-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide. In the closed conformation of enzyme, C230 is more solvent-exposed than in the open conformation. Docking experiments suggest binding modes that block access to the tunnel leading to the active site Cavia porcellus

Inhibitors

Inhibitors Comment Organism Structure
3-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide reversible inhibitor and photolabel. In labeling experiments, specific labeling of residue C230 Cavia porcellus

Organism

Organism UniProt Comment Textmining
Cavia porcellus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Cavia porcellus
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.028
-
 pH 7.0, 25°C Cavia porcellus 3-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide