EC Number | Application | Comment | Organism |
---|---|---|---|
3.4.11.1 | food industry | application of recombinant leucine aminopeptidase rLap1 from Aspergillus sojae in debittering | Aspergillus sojae |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.11.1 | gene lap1, recombinant overexpression of truncated Lap1 without a signal peptide in Pichia pastoris | Aspergillus sojae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.1 | EDTA | significant inhibition, Co2+, Mn2+, and Ca2+ ions, but not Zn2+ ions, restore the enzyme activity | Aspergillus sojae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.1 | Aspergillus sojae | Q8J2N2 | - |
- |
3.4.11.1 | Aspergillus sojae GIM3.30 | Q8J2N2 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.11.1 | Arg 4-nitroanilide + H2O | - |
Aspergillus sojae | Arg + 4-nitroaniline | - |
? | |
3.4.11.1 | Arg 4-nitroanilide + H2O | - |
Aspergillus sojae GIM3.30 | Arg + 4-nitroaniline | - |
? | |
3.4.11.1 | Leu 4-nitroanilide + H2O | - |
Aspergillus sojae | Leu + 4-nitroaniline | - |
? | |
3.4.11.1 | Leu 4-nitroanilide + H2O | - |
Aspergillus sojae GIM3.30 | Leu + 4-nitroaniline | - |
? | |
3.4.11.1 | Lys 4-nitroanilide + H2O | - |
Aspergillus sojae | Lys + 4-nitroaniline | - |
? | |
3.4.11.1 | Lys 4-nitroanilide + H2O | - |
Aspergillus sojae GIM3.30 | Lys + 4-nitroaniline | - |
? | |
3.4.11.1 | Met 4-nitroanilide + H2O | - |
Aspergillus sojae | Met + 4-nitroaniline | - |
? | |
3.4.11.1 | Met 4-nitroanilide + H2O | - |
Aspergillus sojae GIM3.30 | Met + 4-nitroaniline | - |
? | |
3.4.11.1 | additional information | rLap1 shows the highest activity against Arg-pNA, followed by Leu-, Lys-, Met-, and Phe-4-nitroanilide in descending order | Aspergillus sojae | ? | - |
? | |
3.4.11.1 | additional information | rLap1 shows the highest activity against Arg-pNA, followed by Leu-, Lys-, Met-, and Phe-4-nitroanilide in descending order | Aspergillus sojae GIM3.30 | ? | - |
? | |
3.4.11.1 | Phe 4-nitroanilide + H2O | - |
Aspergillus sojae | Phe + 4-nitroaniline | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.11.1 | ? | x * 36700, recombinant enzyme lacking the signal peptide, SDS-PAGE | Aspergillus sojae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.11.1 | LAP1 | - |
Aspergillus sojae |
3.4.11.1 | leucine aminopeptidase | - |
Aspergillus sojae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.1 | 50 | - |
recombinant enzyme | Aspergillus sojae |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.1 | 50 | - |
purified recombinant enzyme, 1 h, 50% activity remaining | Aspergillus sojae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.11.1 | 8 | - |
recombinant enzyme | Aspergillus sojae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.11.1 | additional information | recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis | Aspergillus sojae |
3.4.11.1 | physiological function | enzyme Lap1 improves the degree of hydrolysis of casein and soy protein hydrolysates and also decreases their bitterness, indicating its potential utility in food production | Aspergillus sojae |