Any feedback?
Literature summary extracted from
- Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum (2012), Mol. Biochem. Parasitol., 183, 70-77.
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.20 | 0.015 | - |
Leu-Gly-Leu | pH 7.5, 30°C | Plasmodium falciparum |  |
| 3.4.11.20 | 0.2 | - |
Leu-Gly-Pro | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.4 | - |
Arg-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.42 | - |
Leu-Gly-NH2 | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.43 | - |
Lys-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.64 | - |
Leu-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.7 | - |
Leu-Gly-Gly | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.95 | - |
Leu-Gly | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 4.2 | - |
His-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 4.9 | - |
Leu-NH2 | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 8.9 | - |
Lys-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 9 | - |
Arg-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 10 | - |
Leu-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 35 | - |
His-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.20 | Plasmodium falciparum | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.20 | Arg-Ala + H2O | - |
Plasmodium falciparum | L-Arg + L-Ala | - |
? | |
| 3.4.11.20 | His-Ala + H2O | - |
Plasmodium falciparum | L-His + L-Ala | - |
? | |
| 3.4.11.20 | Leu-Ala + H2O | - |
Plasmodium falciparum | L-Leu + L-Ala | - |
? | |
| 3.4.11.20 | Leu-Gly + H2O | - |
Plasmodium falciparum | L-Leu + Gly | - |
? | |
| 3.4.11.20 | Leu-Gly-Gly + H2O | - |
Plasmodium falciparum | ? | - |
? | |
| 3.4.11.20 | Leu-Gly-Leu + H2O | - |
Plasmodium falciparum | ? | - |
? | |
| 3.4.11.20 | Leu-Gly-NH2 + H2O | - |
Plasmodium falciparum | ? | - |
? | |
| 3.4.11.20 | Leu-Gly-Pro + H2O | - |
Plasmodium falciparum | ? | - |
? | |
| 3.4.11.20 | Leu-NH2 + H2O | - |
Plasmodium falciparum | L-Leu + NH3 | - |
? | |
| 3.4.11.20 | Lys-Ala + H2O | - |
Plasmodium falciparum | L-Lys + L-Ala | - |
? | |
| 3.4.11.20 | additional information | both S1 and S1' subsite exhibit a preference for basic and hydrophobic side chains over polar and acidic side chains. The relative specificity of the S1 subsite is similar over the pH range 5.5-7.5. Substrate P1 and P1' residues affect both Km and kcat, revealing that side chain-subsite interactions not only drive the formation of the Michaelis complex but also influence the rates of ensuing chemical steps. There is no correlation between S1 and S1' specificities and amino acid abundance in hemoglobin. Interactions between PfA-M1 and the backbone atoms of the P1' and P2' residues as well as the P2' side chain further contribute to the catalytic efficiency of substrate hydrolysis | Plasmodium falciparum | ? | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.20 | 1 | - |
His-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 2.4 | - |
His-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 4.8 | - |
Leu-Gly-Leu | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 6.5 | - |
Leu-Gly | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 9.3 | - |
Leu-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 9.5 | - |
Arg-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 12 | - |
Leu-NH2 | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 12 | - |
Leu-Gly-Pro | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 12 | - |
Leu-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 15 | - |
Arg-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 21 | - |
Leu-Gly-Gly | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 21 | - |
Leu-Gly-NH2 | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 27 | - |
Lys-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 27 | - |
Lys-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.20 | 0.027 | - |
His-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 0.56 | - |
His-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 1.2 | - |
Leu-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 1.7 | - |
Arg-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 2.4 | - |
Leu-NH2 | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 3 | - |
Lys-Ala | pH 5.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 6.8 | - |
Leu-Gly | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 14 | - |
Leu-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 23 | - |
Arg-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 30 | - |
Leu-Gly-Gly | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 49 | - |
Leu-Gly-NH2 | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 60 | - |
Leu-Gly-Pro | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 65 | - |
Lys-Ala | pH 7.5, 30°C | Plasmodium falciparum | |
| 3.4.11.20 | 330 | - |
Leu-Gly-Leu | pH 7.5, 30°C | Plasmodium falciparum | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
