EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.5.1.88 | (RS)-phenylalanine nitrile + formate |
- |
Escherichia coli |
(S)-N-formyl-phenylalanine nitrile |
99% (S)-enantiomer |
r |
| 3.5.1.88 | 2-formyloxycaproylleucyl-p-nitroanilide + H2O |
esterase activity, 10fold lower activity compared to N-formyl-Met-Leu-p-nitroanilide |
Escherichia coli |
? |
- |
? |
| 3.5.1.88 | formyl-L-Met-Leu-p-nitroanilide + H2O |
- |
Escherichia coli |
formate + Met-Leu-p-nitroanilide |
- |
? |
| 3.5.1.88 | formyl-L-Met-Leu-p-nitroanilide + H2O |
- |
Homo sapiens |
formate + Met-Leu-p-nitroanilide |
- |
? |
| 3.5.1.88 | formyl-L-Met-Leu-p-nitroanilide + H2O |
- |
Borreliella burgdorferi |
formate + Met-Leu-p-nitroanilide |
- |
? |
| 3.5.1.88 | formyl-L-methionyl peptide + H2O |
- |
Helicobacter pylori |
formate + L-methionyl peptide |
- |
? |
| 3.5.1.88 | formyl-L-methionyl peptide + H2O |
peptide deformylase catalyzes the removal of N-terminal formyl groups from nascent ribosome-synthesized polypeptides |
Borreliella burgdorferi |
formate + L-methionyl peptide |
- |
? |
| 3.5.1.88 | formyl-L-methionyl peptide + H2O |
theoretical study of the catalytic mechanism and metal-ion dependence of peptide deformylase |
Escherichia coli |
formate + L-methionyl peptide |
- |
? |
| 3.5.1.88 | formyl-L-methionyl peptide + H2O |
- |
Staphylococcus aureus |
formate + methionyl peptide |
- |
? |
| 3.5.1.88 | formyl-L-methionyl peptide + H2O |
- |
Haemophilus influenzae |
formate + methionyl peptide |
- |
? |
