silencing of the glx1 gene results in mutants with more than 90% expression reduction and the absence of glyoxal oxidase catalytic activity. The mutants show delayed hyphal growth, reduced colony and conidial hydrophobicity, but no changes in their biocontrol ability. Mutants exhibit a loss of growth directionality resulting in a curled phenotype that is eliminated in the presence of exogenous H2O2
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homology modeling of structure. An N-terminal beta-propeller structure containing the catalytic copper center is linked to a C-terminal immunoglobulin-like domain, with both domains being involved in forming the active site. Residues His804, His889, and Tyr803 compose the first-shell coordination of the copper ion and Cys522-Tyr581 stabilize the free-radical species
efficient expression in Pichia pastoris and Trichoderma reesei with subsequent purification by anion exchange and hydrophobic interaction chromatography. Both processes are suitable for the production of the target protein at high levels. GLOX produced in T. reesei carries mainly Man5 glycosylation while the enzyme produced in P. pastoris exhibits the typical high-mannose type N-glycosylation. The enzyme expressed in P. pastoris shows slightly higher specific activities which correlates with the higher copper loading of 65.5 % compared to 51.9 % for the protein from T. reesei