8BXL

Patulin Synthase from Penicillium expansum

Summary for 8BXL

• Entry DOI: 10.2210/pdb8bxl/pdb
• Descriptor: Patulin synthase, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: oxidoreductase, gmc-type flavoprotein, biocatalysis, flavoprotein
• Biological source: Penicillium expansum
• Total number of polymer chains: 6
• Total formula weight: 425335.91

Authors

Tjallinks, G.,Boverio, A.,Rozeboom, H.J.,Fraaije, M.W. (deposition date: 2022-12-09, release date: 2023-09-06, Last modification date: 2024-10-23)

Primary citation

Tjallinks, G.,Boverio, A.,Maric, I.,Rozeboom, H.,Arentshorst, M.,Visser, J.,Ram, A.F.J.,Mattevi, A.,Fraaije, M.W.
Structure elucidation and characterization of patulin synthase, insights into the formation of a fungal mycotoxin.
Febs J., 290:5114-5126, 2023

PubMed Abstract: Patulin synthase (PatE) from Penicillium expansum is a flavin-dependent enzyme that catalyses the last step in the biosynthesis of the mycotoxin patulin. This secondary metabolite is often present in fruit and fruit-derived products, causing postharvest losses. The patE gene was expressed in Aspergillus niger allowing purification and characterization of PatE. This confirmed that PatE is active not only on the proposed patulin precursor ascladiol but also on several aromatic alcohols including 5-hydroxymethylfurfural. By elucidating its crystal structure, details on its catalytic mechanism were revealed. Several aspects of the active site architecture are reminiscent of that of fungal aryl-alcohol oxidases. Yet, PatE is most efficient with ascladiol as substrate confirming its dedicated role in biosynthesis of patulin.

PubMed: 37366079
DOI: 10.1111/febs.16804

Experimental method

X-RAY DIFFRACTION (2.4 Å)