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Literature summary for 1.10.3.1 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
exression in Trichoderma reesei Aspergillus oryzae

Crystallization (Commentary)

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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Aspergillus oryzae
-
-

Metals/Ions

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

Organism UniProt Comment Textmining
Aspergillus oryzae Q2UNF9
-
-

Posttranslational Modification

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-acetylglucosamine–N-acetylglucosamine–mannose), Asn222 (N-acetylglucosamine) and Asn348 (N-acetylglucosamine). The glycans in AoCO4 might be involved in stabilising the secreted protein Aspergillus oryzae

Subunits

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

Synonyms Comment Organism
AoCO4
-
Aspergillus oryzae
catechol oxidase
-
Aspergillus oryzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Aspergillus oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Aspergillus oryzae

General Information

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