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Literature summary for 3.1.1.73 extracted from
- Cloning, expression of a feruloyl esterase from Aspergillus usamii E001 and its applicability in generating ferulic acid from wheat bran (2013), J. Ind. Microbiol. Biotechnol., 40, 1433-1441.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene AufaeA, subcloning in Escherichia coli strains DH5alpha and JM109, expression in Pichia pastoris strain GS115, the enzyme is secreted | Aspergillus usamii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Aspergillus usamii | |
| 4.64 | - |
methyl ferulate | pH 5.0, 45°C | Aspergillus usamii |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28300 | - |
x * 36000, recombinant enzyme, SDS-PAGE, x * 28300, about, sequence calculation | Aspergillus usamii |
| 36000 | - |
x * 36000, recombinant enzyme, SDS-PAGE, x * 28300, about, sequence calculation | Aspergillus usamii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus usamii | - |
isolated from the soil in China, gene AufaeA, type-A feruloyl esterase | - |
| Aspergillus usamii E001 | - |
isolated from the soil in China, gene AufaeA, type-A feruloyl esterase | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | one putative N-linked glycosylation site in the AuFaeA sequence | Aspergillus usamii |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinnat extracellular enzyme from Pichia pastoris strain GS115 by ammonium sulfate fractionation, dialysis, and ultrafiltration | Aspergillus usamii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methyl ferulate + H2O | - |
Aspergillus usamii | methanol + ferulate | - |
? | |
| methyl ferulate + H2O | - |
Aspergillus usamii E001 | methanol + ferulate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 36000, recombinant enzyme, SDS-PAGE, x * 28300, about, sequence calculation | Aspergillus usamii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AuFaeA | - |
Aspergillus usamii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
recombinant enzyme | Aspergillus usamii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | activity range | Aspergillus usamii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
purified recombinant enzyme, highly stable below | Aspergillus usamii |
| 50 | - |
purified recombinant enzyme, loss of 45% activity after 60 min | Aspergillus usamii |
| 55 | - |
purified recombinant enzyme, loss of 50% activity after 5 min, inactivation after 40 min | Aspergillus usamii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant enzyme | Aspergillus usamii |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 6.5 | purified recombinant enzyme, highly stable within this range | Aspergillus usamii |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Aspergillus usamii | sequence calculation | - |
4.3 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
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