EC Number   |
Activating Compound |
Reference |
|---|
   3.6.5.3 | 1-propanol |
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol |
724475 |
| 3.6.5.3 | 2-propanol |
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol |
724475 |
| 3.6.5.3 | 50S ribosome |
stimulates the enzyme |
735266 |
| 3.6.5.3 | 70S ribosome |
required, stimulates the enzyme |
735266 |
| 3.6.5.3 | bluensomycin |
- |
644144 |
| 3.6.5.3 | eIF1A |
GTPase-activating protein (GAP) for eIF2, the interaction is mediated by an eIF5B-binding motif located at the C-terminus of eIF1A. The C-terminal tail of eIF1A is located in the ribosomal P-site and counteracts the transition from open to closed complex. EIF5 competes with eIF1A for binding to eIF5B |
756055 |
| 3.6.5.3 | eIF5 |
eIF5 is the GTPase-activating protein (GAP) of eIF2, eIF5 promotes GTP hydrolysis by eIF2, followed by phosphate release. EIF2-GDP has lower affinity for Met-tRNAi than eIF2-GTP, and is released together with its GAP, eIF5 |
756055 |
| 3.6.5.3 | eIF5 |
human eIF5, the GTPase-activating protein (GAP) for eIF2, also binds to eIF5B, with affinity that is about two orders of magnitude higher than that of eIF1A. The interaction is mediated by an eIF5B-binding motif located at the C-terminus of eIF5, similar to that of eIF1A and the two proteins compete for binding to eIF5B. NMR structure analysis of the binding interface between eIF5-CT39 and eIF5B-D4, structure of the human eIF5B-D4-eIF5-C-terminal tail (CTT) complex, overview |
756055 |
| 3.6.5.3 | ethanol |
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol |
724475 |
| 3.6.5.3 | ethylene glycoI |
60%, 300fold stimulation |
724475 |
