EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   3.4.11.25 | insulin + rac-3-aminobutanamide |
enatioselectivity for beta-alanine is more than 300:1 |
Sphingosinicella xenopeptidilytica |
? |
- |
r |
| 3.4.11.25 | more |
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded |
Sphingosinicella xenopeptidilytica |
? |
- |
? |
| 3.4.11.25 | more |
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded |
Sphingosinicella microcystinivorans |
? |
- |
? |
| 3.4.11.25 | more |
in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized |
Sphingosinicella microcystinivorans |
? |
- |
? |
| 3.4.11.25 | more |
in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized |
Sphingosinicella xenopeptidilytica |
? |
- |
? |
| 3.4.11.25 | more |
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamic acid-p-nitroanilide |
Sphingosinicella microcystinivorans |
? |
- |
? |
| 3.4.11.25 | more |
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamyl-p-nitroanilide |
Sphingosinicella xenopeptidilytica |
? |
- |
? |
| 3.4.11.25 | more |
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded |
Sphingosinicella xenopeptidilytica 3-2W4 |
? |
- |
? |
| 3.4.11.25 | more |
in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized |
Sphingosinicella xenopeptidilytica 3-2W4 |
? |
- |
? |
| 3.4.11.25 | more |
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamyl-p-nitroanilide |
Sphingosinicella xenopeptidilytica 3-2W4 |
? |
- |
? |
