EC Number   |
Activating Compound |
Reference |
|---|
    1.2.1.70 | cycloheximide |
- |
694706 |
| 1.2.1.70 | GluBP regulator |
the GluTR regulator, GluTR binding protein (GluBP), spatially organizes tetrapyrrole synthesis by distributing enzyme GluTR into different suborganellar locations. GluBP belongs to a heme-binding family involved in heme metabolism. Complex structure of GluTR-GluBP from Arabidopsis thaliana, overview. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, guarding the door for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. GluBP stimulates GluTR catalytic efficiency with an approximate 3fold increase of the 5-aminolevulinic acid formation rate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde. GluBP stimulates GluTR activity and regulates GSA release |
743681 |
| 1.2.1.70 | glutamate-1-semialdehyde aminotransferase |
2.5fold activity in presence of glutamate-1-semialdehyde aminotransferase |
674242, 674450 |
| 1.2.1.70 | heme |
under high heme requirement for respiration levels of GluTR increase |
676889 |
| 1.2.1.70 | more |
is induced in photosynthetic tissues by oxidative stresses such as wounding |
694706 |
| 1.2.1.70 | Ozone |
induces expression in photosynthetic tissues |
694706 |
| 1.2.1.70 | protein GSAM |
stimulation of GluTR by glutamate semialdehyde 1-2 aminomutase, GSAM. GluTR activity is stimulated upon formation ofa complex with protein GSAM. This effect is observed only when GluTR contained a heme/protein ratio of 1/12. GluTR activity and the stimulation of this enzyme by protein GSAM are reduced by treatment with H2O2 |
742701 |
| 1.2.1.70 | puromycin |
- |
694706 |
