Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Wohlschlager, L.; Csarman, F.; Zrilic, M.; Seiboth, B.; Ludwig, R.
    Comparative characterization of glyoxal oxidase from Phanerochaete chrysosporium expressed at high levels in Pichia pastoris and Trichoderma reesei (2021), Enzyme Microb. Technol., 145, 109748 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.2.3.15 synthesis 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 Phanerodontia chrysosporium

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.15 Phanerodontia chrysosporium Q01772
-
-

Synonyms

EC Number Synonyms Comment Organism
1.2.3.15 GLOX
-
Phanerodontia chrysosporium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.3.15 6
-
GLOX activity is highly affected by different buffer species Phanerodontia chrysosporium