The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae

N. Hakulinen (Corresponding Author), C. Gasparetti, H. Kaljunen, Kristiina Kruus, J. Rouvinen

Research output: Contribution to journalArticleScientificpeer-review

25 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)917-929
Number of pages12
JournalJournal of Biological Inorganic Chemistry
Volume18
Issue number8
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

Aspergillus oryzae
Catechol Oxidase
Ascomycota
Monophenol Monooxygenase
Aspergillus
Fungi
Crystal structure
Copper
Enzymes
Fungal Structures
Ions
Quinones
Hemocyanin
Histidine
Absorption spectra
Oxidoreductases
Oxygen
Oxidation
Molecules

Keywords

  • binuclear copper site
  • catechol oxidase
  • type 3 copper enzymes
  • tyrosinase
  • x-ray crystallography

Cite this

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title = "The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae",
abstract = "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-{\AA} 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 {\AA}. 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.",
keywords = "binuclear copper site, catechol oxidase, type 3 copper enzymes, tyrosinase, x-ray crystallography",
author = "N. Hakulinen and C. Gasparetti and H. Kaljunen and Kristiina Kruus and J. Rouvinen",
year = "2013",
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language = "English",
volume = "18",
pages = "917--929",
journal = "Journal of Biological Inorganic Chemistry",
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The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae. / Hakulinen, N. (Corresponding Author); Gasparetti, C.; Kaljunen, H.; Kruus, Kristiina; Rouvinen, J.

In: Journal of Biological Inorganic Chemistry, Vol. 18, No. 8, 2013, p. 917-929.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae

AU - Hakulinen, N.

AU - Gasparetti, C.

AU - Kaljunen, H.

AU - Kruus, Kristiina

AU - Rouvinen, J.

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - binuclear copper site

KW - catechol oxidase

KW - type 3 copper enzymes

KW - tyrosinase

KW - x-ray crystallography

U2 - 10.1007/s00775-013-1038-9

DO - 10.1007/s00775-013-1038-9

M3 - Article

VL - 18

SP - 917

EP - 929

JO - Journal of Biological Inorganic Chemistry

JF - Journal of Biological Inorganic Chemistry

SN - 0949-8257

IS - 8

ER -