EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.1.73 | gene AufaeA, subcloning in Escherichia coli strains DH5alpha and JM109, expression in Pichia pastoris strain GS115, the enzyme is secreted | Aspergillus usamii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.1.73 | additional information | - |
additional information | Michaelis-Menten kinetics | Aspergillus usamii | |
3.1.1.73 | 4.64 | - |
methyl ferulate | pH 5.0, 45°C | Aspergillus usamii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.1.73 | additional information | the enzyme activity is not significantly affected by EDTA and metal ions tested, i.e. Na+, Li+, Ca2+, Co2+, Ba2+, Fe2+, Mg2+, Cu2+, Mn2+, Sn2+, Zn2+, Fe3+, Al3+ | Aspergillus usamii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.1.73 | 28300 | - |
x * 36000, recombinant enzyme, SDS-PAGE, x * 28300, about, sequence calculation | Aspergillus usamii |
3.1.1.73 | 36000 | - |
x * 36000, recombinant enzyme, SDS-PAGE, x * 28300, about, sequence calculation | Aspergillus usamii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.73 | Aspergillus usamii | - |
isolated from the soil in China, gene AufaeA, type-A feruloyl esterase | - |
3.1.1.73 | Aspergillus usamii E001 | - |
isolated from the soil in China, gene AufaeA, type-A feruloyl esterase | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.1.73 | glycoprotein | one putative N-linked glycosylation site in the AuFaeA sequence | Aspergillus usamii |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.1.73 | recombinnat extracellular enzyme from Pichia pastoris strain GS115 by ammonium sulfate fractionation, dialysis, and ultrafiltration | Aspergillus usamii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.73 | methyl ferulate + H2O | - |
Aspergillus usamii | methanol + ferulate | - |
? | |
3.1.1.73 | methyl ferulate + H2O | - |
Aspergillus usamii E001 | methanol + ferulate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.1.73 | ? | x * 36000, recombinant enzyme, SDS-PAGE, x * 28300, about, sequence calculation | Aspergillus usamii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.73 | AuFaeA | - |
Aspergillus usamii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.73 | 45 | - |
recombinant enzyme | Aspergillus usamii |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.73 | 30 | 60 | activity range | Aspergillus usamii |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.73 | 45 | - |
purified recombinant enzyme, highly stable below | Aspergillus usamii |
3.1.1.73 | 50 | - |
purified recombinant enzyme, loss of 45% activity after 60 min | Aspergillus usamii |
3.1.1.73 | 55 | - |
purified recombinant enzyme, loss of 50% activity after 5 min, inactivation after 40 min | Aspergillus usamii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.73 | 5 | - |
recombinant enzyme | Aspergillus usamii |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.73 | 4 | 6.5 | purified recombinant enzyme, highly stable within this range | Aspergillus usamii |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.1.1.73 | Aspergillus usamii | sequence calculation | - |
4.3 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.1.73 | additional information | the enzyme shows a synergistic interaction with the Aspergillus usamii GH family 11 xylanase A. Three-dimensional structure determination, modeling, overview. The enzyme has a globular shape with a catalytic triad Ser133-Asp194-His247, and is composed mainly of one major nine-stranded beta-sheet, two minor two-stranded beta-sheets, and seven alpha-helices, core topology is alpha/beta-hydrolase fold | Aspergillus usamii |