8DAJ

Structure and Biochemistry of a Promiscuous Thermophilic Polyhydroxybutyrate Depolymerase from Lihuaxuella thermophilia

8DAJ の概要

• エントリーDOI: 10.2210/pdb8daj/pdb
• 分子名称: Esterase, PHB depolymerase family, 1,2-ETHANEDIOL, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: bioplastic, thermophile, enzyme, polyhydroxyalkanoates, biosynthetic protein
• 由来する生物種: Lihuaxuella thermophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33302.93

構造登録者

Thomas, G.M.,Quirk, S.,Huard, D.J.E.,Lieberman, R.L. (登録日: 2022-06-13, 公開日: 2023-02-15, 最終更新日: 2024-10-23)

主引用文献

Thomas, G.M.,Quirk, S.,Huard, D.J.E.,Lieberman, R.L.
Bioplastic degradation by a polyhydroxybutyrate depolymerase from a thermophilic soil bacterium.
Protein Sci., 31:e4470-e4470, 2022

PubMed Abstract: As the epidemic of single-use plastic worsens, it has become critical to identify fully renewable plastics such as those that can be degraded using enzymes. Here we describe the structure and biochemistry of an alkaline poly[(R)-3-hydroxybutyric acid] (PHB) depolymerase from the soil thermophile Lihuaxuella thermophila. Like other PHB depolymerases or PHBases, the Lihuaxuella enzyme is active against several different polyhydroxyalkanoates, including homo- and heteropolymers, but L. thermophila PHB depolymerase (LtPHBase) is unique in that it also hydrolyzes polylactic acid and polycaprolactone. LtPHBase exhibits optimal activity at 70°C, and retains 88% of activity upon incubation at 65°C for 3 days. The 1.2 Å resolution crystal structure reveals an α/β-hydrolase fold typical of PHBases, but with a shallow active site containing the catalytic Ser-His-Asp-triad that appears poised for broad substrate specificity. LtPHBase holds promise for the depolymerization of PHB and related bioplastics at high temperature, as would be required in bioindustrial operations like recycling or landfill management.

PubMed: 36222314
DOI: 10.1002/pro.4470

実験手法

X-RAY DIFFRACTION (1.2 Å)