Protein Variants | Comment | Organism |
---|---|---|
N79A | glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a combination of increased KM and decreased kcat. the mutant enzyme exhibits considerably reduced thermostaility relative to wild-type | Aspergillus awamori |
N79Q | glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a considerably decreased kcat. the mutant enzyme exhibits considerably reduced thermostability relative to wild-type | Aspergillus awamori |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.26 | - |
alpha-naphthylbutyrate | 37°C, pH 5.0, wild-type enzyme | Aspergillus awamori | |
0.28 | - |
alpha-naphthylbutyrate | 37°C, pH 5.0, mutant enzyme N79Q | Aspergillus awamori | |
0.66 | - |
alpha-naphthylbutyrate | 37°C, pH 5.0, mutant enzyme N79A | Aspergillus awamori |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
x * 35000, mutant enzyme N79A, SDS-PAGE | Aspergillus awamori |
35000 | - |
x * 35000, mutant enzyme N79Q, SDS-PAGE | Aspergillus awamori |
37000 | - |
x * 37000, wild-type enzyme, SDS-PAGE | Aspergillus awamori |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus awamori | - |
NBRC4033 | - |
Aspergillus awamori NBRC4033 | - |
NBRC4033 | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the native enzyme possesses N-linked oligosaccharides. the recombinant enzyme has a greater mannose content than the wild-type enzyme | Aspergillus awamori |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes N79A and N79Q | Aspergillus awamori |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-naphthyl butyrate + H2O | - |
Aspergillus awamori | 1-naphthol + butyrate | - |
? | |
1-naphthyl butyrate + H2O | - |
Aspergillus awamori NBRC4033 | 1-naphthol + butyrate | - |
? | |
1-naphthyl caprylate + H2O | - |
Aspergillus awamori | 1-naphthol + caprylate | - |
? | |
1-naphthyl caprylate + H2O | - |
Aspergillus awamori NBRC4033 | 1-naphthol + caprylate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 35000, mutant enzyme N79A, SDS-PAGE | Aspergillus awamori |
? | x * 35000, mutant enzyme N79Q, SDS-PAGE | Aspergillus awamori |
? | x * 37000, wild-type enzyme, SDS-PAGE | Aspergillus awamori |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
wild-type enzyme and mutant enzymes N79A and N79Q | Aspergillus awamori |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
48 | - |
T50-value for mutant enzyme N79A is 48.1°C | Aspergillus awamori |
48 | - |
T50-value for mutant enzyme N79Q is 47.7°C | Aspergillus awamori |
50 | - |
60 min, wild-type enzyme retains 70% of its activity, mutant enzymes N79A and N79Q retain no activity | Aspergillus awamori |
52 | - |
T50-value for mutant enzyme is 51.6°C | Aspergillus awamori |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
21 | - |
alpha-naphthylbutyrate | 37°C, pH 5.0, mutant enzyme N79Q | Aspergillus awamori | |
97 | - |
alpha-naphthylbutyrate | 37°C, pH 5.0, mutant enzyme N79A | Aspergillus awamori | |
153 | - |
alpha-naphthylbutyrate | 37°C, pH 5.0, wild-type enzyme | Aspergillus awamori |