Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase.

ABSTRACT: Catechol oxidase is an enzyme that catalyzes the oxidation of o-diphenols to the corresponding o-quinones. It is a copper-containing enzyme with a binuclear copper active site. Here, the crystallization and multiple-wavelength anomalous dispersion data collection of catechol oxidase from the mould fungus Aspergillus oryzae are described. During the purification, three forms of the enzyme (39.3, 40.5 and 44.3?kDa) were obtained. A mixture of these three forms was initially crystallized and gave crystals that diffracted to 2.5?Å resolution and belonged to space group P3(2)21, with unit-cell parameters a = b = 118.9, c = 84.5?Å, ? = ? = 90, ? = 120°. A preparation containing only the shorter form (39.3?kDa) produced crystals that diffracted to 2.9?Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 51.8, b = 95.3, c = 139.5?Å, ? = ? = ? = 90°.

SUBMITTER: Kaljunen H 

PROVIDER: S-EPMC3107139 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature