A Possible Mechanism of Graphene Oxide to Enhance Thermostability of D-Psicose 3-Epimerase Revealed by Molecular Dynamics Simulations

被引：5

作者：

Li, Congcong ^{[1
]}

Lu, Zhongkui ^{[1
]}

Wang, Min ^{[1
]}

Chen, Siao ^{[1
]}

Han, Lu ^{[1
]}

Han, Weiwei ^{[1
]}

机构：

[1] Jilin Univ, Sch Life Sci, Key Lab Mol Enzymol & Engn, Minist Educ, 2699 Qianjin St, Changchun 130012, Peoples R China

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2021年 / 22卷 / 19期

基金：

中国国家自然科学基金;

关键词：

graphene oxide (GO); molecular dynamics simulations; thermostability; D-psicose; 3-epimerase; D-FRUCTOSE; AGROBACTERIUM-TUMEFACIENS; PROTEIN-PROTEIN; CARBON-NANOTUBE; IMMOBILIZATION; STABILITY; CATALYSIS; ENZYMES; LYSOZYME; BINDING;

D O I：

10.3390/ijms221910813

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Thermal stability is a limiting factor for effective application of D-psicose 3-epimerase (DPEase) enzyme. Recently, it was reported that the thermal stability of DPEase was improved by immobilizing enzymes on graphene oxide (GO) nanoparticles. However, the detailed mechanism is not known. In this study, we investigated interaction details between GO and DPEase by performing molecular dynamics (MD) simulations. The results indicated that the domain (K248 to D268) of DPEase was an important anchor for immobilizing DPEase on GO surface. Moreover, the strong interactions between DPEase and GO can prevent loop alpha 1'-alpha 1 and beta 4-alpha 4 of DPEase from the drastic fluctuation. Since these two loops contained active site residues, the geometry of the active pocket of the enzyme remained stable at high temperature after the DPEase was immobilized by GO, which facilitated efficient catalytic activity of the enzyme. Our research provided a detailed mechanism for the interaction between GO and DPEase at the nano-biology interface.

引用

页数：17

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