Literature summary extracted from
Suzuki, K.; Hori, A.; Kawamoto, K.; Thangudu, R.R.; Ishida, T.; Igarashi, K.; Samejima, M.; Yamada, C.; Arakawa, T.; Wakagi, T.; Koseki, T.; Fushinobu, S.
Crystal structure of a feruloyl esterase belonging to the tannase family: A disulfide bond near a catalytic triad (2014), Proteins, 82, 2857-2867.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.1.1.73 |
recombinant expression in Pichia pastoris strain KM71H, the enzyme is secreted |
Aspergillus oryzae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.1.1.73 |
purified recombinant deglycosylated enzyme, untreated or as iodine derivative, mixing of 0.001 ml of 30 mg/ml protein in 5 mM HEPES-NaOH, pH 7.0, with 0.001 ml of reservoir solution containing 20% PEG 1000 and 0.1M Tris-HCl, pH 7.0, hanging drop vapor diffusion method, 20°C, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution, modeling |
Aspergillus oryzae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.1.1.73 |
C202A |
site-directed mutagenesis, almost inactive mutant |
Aspergillus oryzae |
3.1.1.73 |
C202A/C458A |
site-directed mutagenesis, almost inactive mutant |
Aspergillus oryzae |
3.1.1.73 |
C458A |
site-directed mutagenesis, almost inactive mutant |
Aspergillus oryzae |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.1.1.73 |
55000 |
- |
2 * 55000, recombinant deglycosylated enzyme, SDS-PAGE, 2 * 67000, recombinant glycosylated enzyme, SDS-PAGE |
Aspergillus oryzae |
3.1.1.73 |
67000 |
- |
2 * 55000, recombinant deglycosylated enzyme, SDS-PAGE, 2 * 67000, recombinant glycosylated enzyme, SDS-PAGE |
Aspergillus oryzae |
3.1.1.73 |
101000 |
- |
recombinant deglycosylated enzyme, gel filtration |
Aspergillus oryzae |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.1.1.73 |
Aspergillus oryzae |
- |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.1.1.73 |
glycoprotein |
the recombinant extracellular enzyme is deglycosylated by endoglycosidase H |
Aspergillus oryzae |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.1.1.73 |
recombinant extracellular enzyme from Pichia pastoris strain KM71H culture supernatant by ammonium sulfate fractionation, anion exchange chromatography, and deglycosylation with endoglycosidase H, followed by hydrophobic interaction chromatography |
Aspergillus oryzae |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.1.1.73 |
dimer |
2 * 55000, recombinant deglycosylated enzyme, SDS-PAGE, 2 * 67000, recombinant glycosylated enzyme, SDS-PAGE |
Aspergillus oryzae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.1.1.73 |
AoFaeB |
- |
Aspergillus oryzae |
3.1.1.73 |
FAE B |
- |
Aspergillus oryzae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.1.1.73 |
37 |
- |
assay at |
Aspergillus oryzae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.1.1.73 |
7 |
- |
assay at |
Aspergillus oryzae |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.1.1.73 |
evolution |
the enzyme belongs to the fungal tannase family |
Aspergillus oryzae |
3.1.1.73 |
additional information |
the enzyme structure consists of a catalytic alpha/beta-hydrolase fold domain and a large lid domain with a unique fold, binding models of substrates and docking analysis, overview. The catalytic triad of the enzyme comprises residues Ser203, Asp417, and His457, and the serine and histidine residues are directly connected by a disulfide bond of the neighboring cysteine residues, Cys202 and Cys458. The CS-D-HC structural motif plays an essential role in the function of the active site |
Aspergillus oryzae |