EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   3.4.16.6 | angiotensin 1 + H2O |
truncated KexA releases amino acid residues from the C terminus of angiotensin I |
Aspergillus oryzae |
? |
- |
? |
| 3.4.16.6 | benzoyl-Gly-Arg + H2O |
enzyme shows very low activity |
Aspergillus oryzae |
benzoyl-Gly + L-arginine |
- |
? |
| 3.4.16.6 | benzyloxycarbonyl-Gly-Lys + H2O |
enzyme shows very low activity |
Aspergillus oryzae |
benzyloxycarbonyl-Gly + L-lysine |
- |
? |
| 3.4.16.6 | benzyloxycarbonyl-Phe-Leu + H2O |
enzyme shows very low activity |
Aspergillus oryzae |
benzyloxycarbonyl-Phe + L-leucine |
- |
? |
| 3.4.16.6 | benzyloxycarbonyl-Phe-Tyr-Leu + H2O |
- |
Aspergillus oryzae |
benzyloxycarbonyl-Phe-Tyr + L-leucine |
- |
? |
| 3.4.16.6 | benzyloxycarbonyl-Tyr-Leu + H2O |
enzyme shows very low activity |
Aspergillus oryzae |
benzyloxycarbonyl-Tyr + L-leucine |
- |
? |
| 3.4.16.6 | bradykinin I + H2O |
truncated KexA releases amino acid residues from the C terminus of bradykinin I |
Aspergillus oryzae |
? |
- |
? |
| 3.4.16.6 | Dansyl-Phe-Ala-Arg + H2O |
- |
Drosophila melanogaster |
Dansyl-Phe-Ala + Arg |
- |
? |
| 3.4.16.6 | more |
activity of individual domains of the enzyme. Domain 1B is more active at neutral pH and greatly prefers C-terminal Arg over Lys, whereas domain 2 is more active at pH 5-6 and slightly prefers C-terminal Lys over Arg |
Drosophila melanogaster |
? |
- |
? |
| 3.4.16.6 | more |
the enzyme functions in processing of proteins that transit the secretory pathway |
Drosophila melanogaster |
? |
- |
? |
