| Title : Structural insight into catalytic mechanism of PET hydrolase - Han_2017_Nat.Commun_8_2106 |
| Author(s) : Han X , Liu W , Huang JW , Ma J , Zheng Y , Ko TP , Xu L , Cheng YS , Chen CC , Guo RT |
| Ref : Nat Commun , 8 :2106 , 2017 |
|
Abstract :
PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated. |
| PubMedSearch : Han_2017_Nat.Commun_8_2106 |
| PubMedID: 29235460 |
| Gene_locus related to this paper: idesa-peth |
| Inhibitor | Terephthalic-acid MHET |
| Substrate | MHET HEMT BHET Polyethylene-terephthalate |
| Gene_locus | idesa-peth |
| Family | Polyesterase-lipase-cutinase |
| Structure | 5XFY 5XFZ 5XG0 5XH2 5XH3 |
| Chemical | Terephthalic-acid |
Han X, Liu W, Huang JW, Ma J, Zheng Y, Ko TP, Xu L, Cheng YS, Chen CC, Guo RT (2017)
Structural insight into catalytic mechanism of PET hydrolase
Nat Commun
8 :2106
Han X, Liu W, Huang JW, Ma J, Zheng Y, Ko TP, Xu L, Cheng YS, Chen CC, Guo RT (2017)
Nat Commun
8 :2106