Cloned (Comment) | Organism |
---|---|
exression in Trichoderma reesei | Aspergillus oryzae |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Aspergillus oryzae | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus oryzae | Q2UNF9 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
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 |
More | structure analysis | Aspergillus oryzae |
Synonyms | Comment | Organism |
---|---|---|
AoCO4 | - |
Aspergillus oryzae |
catechol oxidase | - |
Aspergillus oryzae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Aspergillus oryzae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Aspergillus oryzae |
General Information | Comment | Organism |
---|---|---|
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 |
additional information | overall and active site structure analysis, catalytic binuclear centre, overview. The enzyme dimerisation does not have a clear functional role | Aspergillus oryzae |
physiological function | catechol oxidases catalyse the oxidation of different para-substituted o-diphenols, showing diphenolase activity | Aspergillus oryzae |