Literature summary extracted from
Hakulinen, N.; Gasparetti, C.; Kaljunen, H.; Kruus, K.; Rouvinen, J.
The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae (2013), J. Biol. Inorg. Chem., 18, 917-929.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.10.3.1 |
exression in Trichoderma reesei |
Aspergillus oryzae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.10.3.1 |
AoCO4 is crystallised as the full-length form and truncated form from the mixture of three forms, X-ray diffraction structure determination and analysis at 2.5 A and 2.9 A resolution, respectively |
Aspergillus oryzae |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.10.3.1 |
extracellular |
- |
Aspergillus oryzae |
- |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.10.3.1 |
Cu2+ |
the enzyme contains two copper ions (CuA and CuB) within the so-called coupled type 3 copper site, in the catalytic binuclear centre. The two copper ions in the catalytic centre of AoCO4 are each coordinated by the three histidine residues: His102 (a3), His110 (loop before a4) and His119 (a4) for CuA, and His284 (a8), His288 (a8) and His312 (a9) for CuB |
Aspergillus oryzae |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.10.3.1 |
Aspergillus oryzae |
Q2UNF9 |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
1.10.3.1 |
glycoprotein |
the full-length AoCO4 shows O-glycosylation at Thr14 (mannose residue) and N-glycosylation at Asn30 (N-acetylglucosamine residue), Asn104 (N-acetylglucosamineN-acetylglucosaminemannose), Asn222 (N-acetylglucosamine) and Asn348 (N-acetylglucosamine). The glycans in AoCO4 might be involved in stabilising the secreted protein |
Aspergillus oryzae |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.10.3.1 |
dimer |
the full-length form and the truncated form of AoCO4 are dimers in solution, the dimerisation does not have a clear functional role |
Aspergillus oryzae |
1.10.3.1 |
More |
structure analysis |
Aspergillus oryzae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.10.3.1 |
AoCO4 |
- |
Aspergillus oryzae |
1.10.3.1 |
catechol oxidase |
- |
Aspergillus oryzae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.10.3.1 |
25 |
- |
assay at |
Aspergillus oryzae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.10.3.1 |
7 |
- |
assay at |
Aspergillus oryzae |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.10.3.1 |
evolution |
AoCO4 belongs to the short-tyrosinase family. The catalytic differences to the phenolases, EC 1.14.18.1, are not due to structural features |
Aspergillus oryzae |
1.10.3.1 |
additional information |
overall and active site structure analysis, catalytic binuclear centre, overview. The enzyme dimerisation does not have a clear functional role |
Aspergillus oryzae |
1.10.3.1 |
physiological function |
catechol oxidases catalyse the oxidation of different para-substituted o-diphenols, showing diphenolase activity |
Aspergillus oryzae |