8BMU

Engineered Fructosyl Peptide Oxidase - X04 mutant

Summary for 8BMU

• Entry DOI: 10.2210/pdb8bmu/pdb
• Descriptor: Fructosyl Peptide Oxidase mutant (X04), FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: fad, deglycating enzyme, amadori product, fructosyl peptide oxidase, oxidoreductase
• Biological source: Parastagonospora nodorum SN15
• Total number of polymer chains: 1
• Total formula weight: 49119.27

Authors

Estiri, H.,Bhattacharya, S.,Rodriguez-Buitrago, J.A.,Parisini, E. (deposition date: 2022-11-11, release date: 2023-11-22, Last modification date: 2024-11-06)

Primary citation

Estiri, H.,Bhattacharya, S.,Buitrago, J.A.R.,Castagna, R.,Legzdina, L.,Casucci, G.,Ricci, A.,Parisini, E.,Gautieri, A.
Tailoring FPOX enzymes for enhanced stability and expanded substrate recognition.
Sci Rep, 13:18610-18610, 2023

PubMed Abstract: Fructosyl peptide oxidases (FPOX) are deglycating enzymes that find application as key enzymatic components in diabetes monitoring devices. Indeed, their use with blood samples can provide a measurement of the concentration of glycated hemoglobin and glycated albumin, two well-known diabetes markers. However, the FPOX currently employed in enzymatic assays cannot directly detect whole glycated proteins, making it necessary to perform a preliminary proteolytic treatment of the target protein to generate small glycated peptides that can act as viable substrates for the enzyme. This is a costly and time consuming step. In this work, we used an in silico protein engineering approach to enhance the overall thermal stability of the enzyme and to improve its catalytic activity toward large substrates. The final design shows a marked improvement in thermal stability relative to the wild type enzyme, a distinct widening of its access tunnel and significant enzymatic activity towards a range of glycated substrates.

PubMed: 37903872
DOI: 10.1038/s41598-023-45428-1

Experimental method

X-RAY DIFFRACTION (1.6 Å)