EC Number   |
Natural Substrates |
|---|
   3.4.11.18 | glutathione-S-transferase + H2O |
removal of Met(init) from glutathione-S-transferase. Processing of glutathione-S-transferase in yeast relies almost entirely on MetAP1 function |
| 3.4.11.18 | Met-peptide + H2O |
- |
| 3.4.11.18 | Met-peptide + H2O |
the biological function is removing the terminal methionine from nascent peptides |
| 3.4.11.18 | Met-peptide + H2O |
the enzyme catalyzes the removal of an amino-terminal methionine from a newly synthesized polypeptide |
| 3.4.11.18 | Met-peptide + H2O |
the enzyme is responsible for hydrolysis of the initiator methionine residue from the majority of newly synthesized proteins. Potentially important role in the production of recombinant proteins, since failure to correctly remove initiator methionine residues can result in a product that is inactive or immunogenic |
| 3.4.11.18 | Met-peptide + H2O |
the enzyme is directly involved in the regulation of growth factor-stimulated endothelial cell proliferation |
| 3.4.11.18 | Met-peptide + H2O |
the biological function is removing the terminal methionine from nascent peptides during protein synthesis |
| 3.4.11.18 | Met-peptide + H2O |
the enzyme removes the N-terminal Met from polypeptides, and thus plays a key role in protein synthesis, modification and transport |
| 3.4.11.18 | more |
together with N-myristoyltransferase, enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family |
| 3.4.11.18 | more |
the isozymes act on peptides in the cytosol, that are N-terminal fragments from digestion of hemoglobin in the digestive vacuole. The hemoglobin-derived peptides show leucine and alanine as most abundant amino acids |
