EC Number   |
Inhibitors |
Structure |
|---|
   2.3.2.8 | aminophenylarsenoxide |
50% inhibition at 0.0025 mM |
   |
| 2.3.2.8 | aurothioglucose |
complete inhibition at 0.003 mM |
|
| 2.3.2.8 | Di- and tripeptides |
with glutamyl-, asparagyl- and to a lesser extent cystinyl-NH2-terminal residues, competitive to bovine serum albumin acceptor |
|
| 2.3.2.8 | Di- and tripeptides |
most potent inhibitor is Glu-Val-Phe, inhibits transfer of arginine to acceptor proteins |
|
| 2.3.2.8 | Disulfiram |
complete inhibition at 0.003 mM |
|
| 2.3.2.8 | DNAse |
- |
|
| 2.3.2.8 | hemin |
Fe3+-heme, inhibits arginyl-transferase through a redox mechanism that involves the formation of disulfide between the enzymes Cys-71 and Cys-72 residues |
|
| 2.3.2.8 | heparin |
50% inhibition at 0.05 mg/ml, kinetics, competitive to L-arginyl-tRNA |
|
| 2.3.2.8 | homocysteine-responsive endoplasmic reticlulum protein |
i.e. HERP, a key inhibitor of the turnover and N-terminal arginylation of molecular chaperone BiP. HERP is a 43-kDa endoplasmic reticlulum (ER) membrane-integrated protein that is an essential component of ER-associated protein degradation |
|
| 2.3.2.8 | isoasparagine |
- |
|
