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 | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | inhibits autoproteolysis, other divalent cations than Zn2+ have no effect on the process | Lupinus luteus |
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 | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is potassium-independent | Lupinus luteus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
75000 | - |
about, recombinant His-tagged enzyme, gel filtration | Lupinus luteus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Lupinus luteus | Q9ZSD6 | yellow lupin with roots infected with Bradyrhizobium sp. | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration | Lupinus luteus |
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 | 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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Lupinus luteus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
purified recombinant His-tagged enzyme, stable up to | Lupinus luteus |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Lupinus luteus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the N-terminal nucleophile hydrolase family | Lupinus luteus |
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 |