Any feedback?
Literature summary for 3.4.19.5 extracted from
- Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog (2004), Eur. J. Biochem., 271, 3215-3226.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS | Lupinus luteus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | inhibits autoproteolysis, other divalent cations than Zn2+ have no effect on the process | Lupinus luteus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.136 | - |
beta-L-aspartyl-L-leucine | pH 7.5, 22°C | Lupinus luteus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme is potassium-independent | Lupinus luteus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 75000 | - |
about, recombinant His-tagged enzyme, gel filtration | Lupinus luteus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-asparagine + H2O | Lupinus luteus | - |
L-aspartate + NH3 | - |
? | |
| additional information | Lupinus luteus | the enzyme shows both isoaspartyl dipeptidase and L-asparaginase activities. Identification of Thr193 in enzyme LlA as the catalytic nucleophile and classification of the enzyme as Ntn-hydrolase | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lupinus luteus | Q9ZSD6 | yellow lupin with roots infected with Bradyrhizobium sp. | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration | Lupinus luteus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-L-aspartyl-L-leucine + H2O | - |
Lupinus luteus | ? | - |
? | |
| L-asparagine + H2O | - |
Lupinus luteus | L-aspartate + NH3 | - |
? | |
| additional information | the enzyme shows both isoaspartyl dipeptidase and L-asparaginase activities. Identification of Thr193 in enzyme LlA as the catalytic nucleophile and classification of the enzyme as Ntn-hydrolase | Lupinus luteus | ? | - |
? | |
| additional information | no activity with L-glutamine, L-asparagine amide, L-aspartic acid amide, glycyl-L-asparagine, and N4-(beta-N-acetylglucosaminyl)-L-asparagine | Lupinus luteus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | alphabeta, 1 * 23000, alpha-subunit + 1 * 14000, beta-subunit, SDS-PAGE, 1 * 22893, His-tagged alpha-subunit + 1 * 13605, beta-subunit, mass spectrometry | Lupinus luteus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| asparagine beta-amidohydrolase | - |
Lupinus luteus |
| isoaspartyl peptidase | - |
Lupinus luteus |
| isoaspartyl peptidase/L-asparaginase | UniProt | Lupinus luteus |
| LlA | - |
Lupinus luteus |
| Ntn-hydrolase | - |
Lupinus luteus |
| potassium-independent asparaginase | - |
Lupinus luteus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Lupinus luteus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
purified recombinant His-tagged enzyme, stable up to | Lupinus luteus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.813 | - |
beta-L-aspartyl-L-leucine | pH 7.5, 22°C | Lupinus luteus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Lupinus luteus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the N-terminal nucleophile hydrolase family | Lupinus luteus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5.98 | - |
beta-L-aspartyl-L-leucine | pH 7.5, 22°C | Lupinus luteus | |
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
