8BMU

Engineered Fructosyl Peptide Oxidase - X04 mutant

8BMU の概要

• エントリーDOI: 10.2210/pdb8bmu/pdb
• 分子名称: Fructosyl Peptide Oxidase mutant (X04), FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: fad, deglycating enzyme, amadori product, fructosyl peptide oxidase, oxidoreductase
• 由来する生物種: Parastagonospora nodorum SN15
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49119.27

構造登録者

Estiri, H.,Bhattacharya, S.,Rodriguez-Buitrago, J.A.,Parisini, E. (登録日: 2022-11-11, 公開日: 2023-11-22, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)