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Literature summary extracted from
- Identification and biochemical characterization of plant acylamino acid-releasing enzyme (2003), J. Biochem., 134, 251-257.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | expression in Escherichia coli as a functional enzyme | Cucumis sativus |
| 3.4.19.1 | expression in Escherichia coli as a functional enzyme | Arabidopsis thaliana |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.19.1 | Cu2+ | 1 mM, complete inhibition of recombinant enzyme | Arabidopsis thaliana |  |
| 3.4.19.1 | Cu2+ | 1 mM, complete inhibition of recombinant enzyme | Cucumis sativus | |
| 3.4.19.1 | diisopropyl fluorophosphate | 1 mM, complete inactivation | Arabidopsis thaliana | |
| 3.4.19.1 | diisopropyl fluorophosphate | 1 mM, complete inactivation | Cucumis sativus | |
| 3.4.19.1 | NEM | 1 mM | Arabidopsis thaliana | |
| 3.4.19.1 | NEM | 1 mM | Cucumis sativus | |
| 3.4.19.1 | PCMB | 0.1 mM | Arabidopsis thaliana | |
| 3.4.19.1 | PCMB | 0.1 mM | Cucumis sativus | |
| 3.4.19.1 | PMSF | 1 mM, 50% inhibition | Arabidopsis thaliana | |
| 3.4.19.1 | PMSF | 1 mM, 50% inhibition | Cucumis sativus | |
| 3.4.19.1 | Zn2+ | 1 mM, complete inhibition of recombinant enzyme | Arabidopsis thaliana | |
| 3.4.19.1 | Zn2+ | 1 mM, complete inhibition of recombinant enzyme | Cucumis sativus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.19.1 | 1.5 | - |
N-acetyl-Ala-p-nitroanilide | pH 7.0, 37°C | Arabidopsis thaliana | |
| 3.4.19.1 | 4.6 | - |
N-acetyl-Ala-p-nitroanilide | pH 7.0, 37°C | Cucumis sativus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.19.1 | chloroplast stroma | - |
Cucumis sativus | 9570 | - |
| 3.4.19.1 | chloroplast stroma | - |
Arabidopsis thaliana | 9570 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.19.1 | 82000 | - |
4 * 82000, SDS-PAGE | Cucumis sativus |
| 3.4.19.1 | 82000 | - |
4 * 82000, SDS-PAGE | Arabidopsis thaliana |
| 3.4.19.1 | 350000 | - |
gel filtration | Cucumis sativus |
| 3.4.19.1 | 350000 | - |
gel filtration | Arabidopsis thaliana |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.19.1 | additional information | Cucumis sativus | the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.1 | Arabidopsis thaliana | Q84LM4 | - |
- |
| 3.4.19.1 | Cucumis sativus | - |
L. suyo | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | - |
Cucumis sativus |
| 3.4.19.1 | - |
Arabidopsis thaliana |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.19.1 | leaf | - |
Cucumis sativus | - |
| 3.4.19.1 | shoot | - |
Cucumis sativus | - |
| 3.4.19.1 | shoot | - |
Arabidopsis thaliana | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.19.1 | 1.9 | - |
- |
Cucumis sativus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.19.1 | acetyl-Ala-Ala + H2O | - |
Cucumis sativus | acetyl-Ala + Ala | - |
? | |
| 3.4.19.1 | acetyl-Ala-Ala + H2O | - |
Arabidopsis thaliana | acetyl-Ala + Ala | - |
? | |
| 3.4.19.1 | Acetyl-Ala-Ala-Ala + H2O | native enzyme shows 147% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | Acetyl-Ala + Ala-Ala | - |
? | |
| 3.4.19.1 | Acetyl-Ala-Ala-Ala + H2O | native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | Acetyl-Ala + Ala-Ala | - |
? | |
| 3.4.19.1 | acetyl-Ala-Ala-Ala-Ala + H2O | native enzyme shows 126% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | acetyl-Ala + Ala-Ala-Ala | - |
? | |
| 3.4.19.1 | acetyl-Ala-Ala-Ala-Ala + H2O | native enzyme shows 85.6% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Ala + Ala-Ala-Ala | - |
? | |
| 3.4.19.1 | acetyl-Ala-Met + H2O | native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Ala + Met | - |
? | |
| 3.4.19.1 | acetyl-Gly-Gly + H2O | native enzyme shows 37% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Gly + Gly | - |
? | |
| 3.4.19.1 | acetyl-Gly-Gly + H2O | native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | acetyl-Gly + Gly | - |
? | |
| 3.4.19.1 | acetyl-Gly-Leu + H2O | native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Gly + Leu | - |
? | |
| 3.4.19.1 | acetyl-Met-Ala + H2O | native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Met + Ala | - |
? | |
| 3.4.19.1 | acetyl-Met-Ala + H2O | native enzyme shows 45% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | acetyl-Met + Ala | - |
? | |
| 3.4.19.1 | acetyl-Met-Asn + H2O | native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Met + Asn | - |
? | |
| 3.4.19.1 | acetyl-Met-Glu + H2O | native enzyme shows 4.3% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | acetyl-Met + Glu | - |
? | |
| 3.4.19.1 | acetyl-Met-Glu + H2O | native enzyme shows 6% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | acetyl-Met + Glu | - |
? | |
| 3.4.19.1 | acetyl-Met-Phe + H2O | native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | acetyl-Met + Phe | - |
? | |
| 3.4.19.1 | butyryl-Ala-Ala-Ala + H2O | native enzyme shows 33.6% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | butyryl-Ala + Ala-Ala | - |
? | |
| 3.4.19.1 | butyryl-Ala-Ala-Ala + H2O | native enzyme shows 77% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | butyryl-Ala + Ala-Ala | - |
? | |
| 3.4.19.1 | formyl-Ala-Ala-Ala + H2O | native enzyme shows 62.4% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | formyl-Ala + Ala-Ala | - |
? | |
| 3.4.19.1 | formyl-Ala-Ala-Ala + H2O | native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate | Arabidopsis thaliana | formyl-Ala + Ala-Ala | - |
? | |
| 3.4.19.1 | formyl-Gly-Val + H2O | native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate | Cucumis sativus | formyl-Gly + Val | - |
? | |
| 3.4.19.1 | glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O | no degradation of the native protein | Cucumis sativus | ? | - |
? | |
| 3.4.19.1 | additional information | the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins | Cucumis sativus | ? | - |
? | |
| 3.4.19.1 | N-acetyl-Ala-p-nitroanilide + H2O | substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide | Cucumis sativus | N-acetyl-Ala + p-nitroaniline | - |
? | |
| 3.4.19.1 | N-acetyl-Ala-p-nitroanilide + H2O | substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide | Arabidopsis thaliana | N-acetyl-Ala + p-nitroaniline | - |
? | |
| 3.4.19.1 | N-acetyl-Gly-p-nitroanilide + H2O | substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide | Cucumis sativus | N-acetyl-Gly + p-nitroaniline | - |
? | |
| 3.4.19.1 | N-acetyl-Gly-p-nitroanilide + H2O | substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide | Arabidopsis thaliana | N-acetyl-Gly + p-nitroaniline | - |
? | |
| 3.4.19.1 | N-acetyl-Met-p-nitroanilide + H2O | substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide | Cucumis sativus | N-acetyl-Met + p-nitroaniline | - |
? | |
| 3.4.19.1 | N-acetyl-Met-p-nitroanilide + H2O | substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide | Arabidopsis thaliana | N-acetyl-Met + p-nitroaniline | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | tetramer | 4 * 82000, SDS-PAGE | Cucumis sativus |
| 3.4.19.1 | tetramer | 4 * 82000, SDS-PAGE | Arabidopsis thaliana |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | AtAARE | - |
Arabidopsis thaliana |
| 3.4.19.1 | cAARE | - |
Cucumis sativus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.19.1 | 37 | - |
- |
Cucumis sativus |
| 3.4.19.1 | 37 | - |
- |
Arabidopsis thaliana |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.19.1 | 7 | - |
- |
Cucumis sativus |
| 3.4.19.1 | 7 | - |
- |
Arabidopsis thaliana |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.19.1 | Cucumis sativus | isoelectric focusing | - |
5.5 |
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