8AIS

Crystal structure of cutinase PsCut from Pseudomonas saudimassiliensis

8AIS の概要

• エントリーDOI: 10.2210/pdb8ais/pdb
• 分子名称: Lipase 1, ACETATE ION (3 entities in total)
• 機能のキーワード: cutinase, ester bond, cleavage, pet, hydrolase
• 由来する生物種: Pseudomonas saudimassiliensis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 100776.42

構造登録者

Zahn, M.,Allen, M.D.,Pickford, A.R.,McGeehan, J.E. (登録日: 2022-07-27, 公開日: 2023-03-08, 最終更新日: 2024-02-07)

主引用文献

Avilan, L.,Lichtenstein, B.R.,Konig, G.,Zahn, M.,Allen, M.D.,Oliveira, L.,Clark, M.,Bemmer, V.,Graham, R.,Austin, H.P.,Dominick, G.,Johnson, C.W.,Beckham, G.T.,McGeehan, J.E.,Pickford, A.R.
Concentration-Dependent Inhibition of Mesophilic PETases on Poly(ethylene terephthalate) Can Be Eliminated by Enzyme Engineering.
ChemSusChem, 16:e202202277-e202202277, 2023

PubMed Abstract: Enzyme-based depolymerization is a viable approach for recycling of poly(ethylene terephthalate) (PET). PETase from Ideonella sakaiensis (IsPETase) is capable of PET hydrolysis under mild conditions but suffers from concentration-dependent inhibition. In this study, this inhibition is found to be dependent on incubation time, the solution conditions, and PET surface area. Furthermore, this inhibition is evident in other mesophilic PET-degrading enzymes to varying degrees, independent of the level of PET depolymerization activity. The inhibition has no clear structural basis, but moderately thermostable IsPETase variants exhibit reduced inhibition, and the property is completely absent in the highly thermostable HotPETase, previously engineered by directed evolution, which simulations suggest results from reduced flexibility around the active site. This work highlights a limitation in applying natural mesophilic hydrolases for PET hydrolysis and reveals an unexpected positive outcome of engineering these enzymes for enhanced thermostability.

PubMed: 36811288
DOI: 10.1002/cssc.202202277

実験手法

X-RAY DIFFRACTION (1.56 Å)