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PDBsum entry 4j3q
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Oxidoreductase
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PDB id
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4j3q
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References listed in PDB file
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Key reference
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Title
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The crystal structure of an extracellular catechol oxidase from the ascomycete fungus aspergillus oryzae.
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Authors
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N.Hakulinen,
C.Gasparetti,
H.Kaljunen,
K.Kruus,
J.Rouvinen.
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Ref.
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J Biol Inorg Chem, 2013,
18,
917-929.
[DOI no: ]
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PubMed id
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Abstract
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Catechol oxidases (EC 1.10.3.1) catalyse the oxidation of o-diphenols to their
corresponding o-quinones. These oxidases contain two copper ions (CuA and CuB)
within the so-called coupled type 3 copper site as found in tyrosinases (EC
1.14.18.1) and haemocyanins. The crystal structures of a limited number of
bacterial and fungal tyrosinases and plant catechol oxidases have been solved.
In this study, we present the first crystal structure of a fungal catechol
oxidase from Aspergillus oryzae (AoCO4) at 2.5-Å resolution. AoCO4 belongs to
the newly discovered family of short-tyrosinases, which are distinct from other
tyrosinases and catechol oxidases because of their lack of the conserved
C-terminal domain and differences in the histidine pattern for CuA. The sequence
identity of AoCO4 with other structurally known enzymes is low (less than
30 %), and the crystal structure of AoCO4 diverges from that of enzymes
belonging to the conventional tyrosinase family in several ways, particularly
around the central α-helical core region. A diatomic oxygen moiety was
identified as a bridging molecule between the two copper ions CuA and CuB
separated by a distance of 4.2-4.3 Å. The UV/vis absorption spectrum of AoCO4
exhibits a distinct maximum of absorbance at 350 nm, which has been reported to
be typical of the oxy form of type 3 copper enzymes.
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