KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.7 | - |
N-acetyl-Ala-Ala-Arg-Gly | - |
Oryctolagus cuniculus | |
2 | - |
N-acetyl-Ala-Ala-Phe-Gly | - |
Oryctolagus cuniculus | |
2.1 | - |
N-acetyl-Ala-Ala-Ala-Ala | - |
Oryctolagus cuniculus | |
3.6 | - |
N-acetyl-Ala-Ala-Pro-Ala | - |
Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-Ala-Ala-Phe-Gly + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
acetyl-Ala-Gly-D-Ala-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
additional information | N-acetylated peptides with D-Ala in position 3 or 4 as are good substrates as those containing L-Ala. Peptides with Pro in position 2 are inactive, and most of the peptides with Pro in the third position are very good substrates. Only the peptide acetyl-AAP gives 30% of the activity of acetyl-AAA, which is reduced to 1-2% if additional residues are present at the C-terminus, acety-AAPA or acetyl-AAPAA. The presence of a positive charge in position 2,3,4,5 and 6 gives strong reduction in hydrolase activity, varying with the charge's distance from the N-terminus from 9 to 15-20% of the rate obtained with the reference peptides without positive charges. Deprotonation of His at high pH generates excellent substrates, and removal of the positive charges of Lys by acetylation or succinylation give improved substrate quality. Long peptides with 10-29 residues, are poor substrates, especially when they contain positive charges and Pro | Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala + H2O | - |
Oryctolagus cuniculus | N-acetyl-Ala + Ala | - |
? | |
N-acetyl-Ala-Ala-Ala + H2O | - |
Oryctolagus cuniculus | N-acetyl-Ala + Ala-Ala | - |
? | |
N-acetyl-Ala-Ala-Ala-Ala + H2O | - |
Oryctolagus cuniculus | N-acetyl-Ala + Ala-Ala-Ala | - |
? | |
N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-Arg-Gly + H2O | - |
Oryctolagus cuniculus | N-acetyl-Ala + Ala-Arg-Gly | - |
? | |
N-acetyl-Ala-Ala-Gln-Nepsilon-acetyl-Lys + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-Gln-Nepsilon-succinyl-Lys + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-His-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-Phe-Gly + H2O | - |
Oryctolagus cuniculus | N-acetyl-Ala + Ala-Phe-Gly | - |
? | |
N-acetyl-Ala-Ala-Pro + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-Ala-Pro-Ala + H2O | - |
Oryctolagus cuniculus | N-acetyl-Ala + Ala-Pro-Ala | - |
? | |
N-acetyl-Ala-Gly-Ala-D-Ala-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Ala-His-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Met-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O | - |
Oryctolagus cuniculus | ? | - |
? | |
N-acetyl-Met-Asp-Glu-Thr-Gly-Asp-Thr-Ala-Leu-Val-Ala + H2O | - |
Oryctolagus cuniculus | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Oryctolagus cuniculus |