(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Vibrionales: NE > Vibrionaceae: NE > Vibrio: NE > Vibrio gazogenes: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Vibrio gazogenes DSM 21264: N, E.
Vibrio gazogenes DSM 21264 = NBRC 103151: N, E.
Molecular evidence
Database
No mutation 1 structure: 7Z6B: PET hydrolase PET6 from halophilic organsim Vibrio gazogenes No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MNVLTKCKLALGIIVAFFSLPSFAVPCSDCSNGFERGQVPRVDQLESSRG PYSVKTINVSRLARGFGGGTIHYSTESGGQQGIIAVVPGYVSYESSIQWW GPRLASWGFTVITINTNTIYDQPDNRAGQLSAAIDYVIDKSKDRTSPIYG LVDPNRVGVIGWSMGGGGSLKLATDRKIDAVIPQAPWYLGLNRFSTITSP TMIIACQADAVAPVSVHASRFYNQIPRTTPKAYFEIALGSHFCANTGYPS EDILGRNGVAWMKRFIDKDERYTQFLCGQNFDSSLRVSEYRDNCSYY
The handling of plastic waste and the associated ubiquitous occurrence of microplastic poses one of the biggest challenges of our time. Recent investigations of plastic degrading enzymes have opened new prospects for biological microplastic decomposition as well as recycling applications. For polyethylene terephthalate, in particular, several natural and engineered enzymes are known to have such promising properties. From a previous study that identified new PETase candidates by homology search, we chose the candidate PET6 from the globally distributed, halophilic organism Vibrio gazogenes for further investigation. By mapping the occurrence of Vibrios containing PET6 homologs we demonstrated their ubiquitous prevalence in the pangenome of several Vibrio strains. The biochemical characterization of PET6 showed that PET6 has a comparatively lower activity than other enzymes but also revealed a superior turnover at very high salt concentrations. The crystal structure of PET6 provides structural insights into this adaptation to saline environments. By grafting only a few beneficial mutations from other PET degrading enzymes onto PET6, we increased the activity up to three-fold, demonstrating the evolutionary potential of the enzyme. MD simulations of the variant helped rationalize the mutational effects of those mutants and elucidate the interaction of the enzyme with a PET substrate. With tremendous amounts of plastic waste in the Ocean and the prevalence of Vibrio gazogenes in marine biofilms and estuarine marshes, our findings suggest that Vibrio and the PET6 enzyme are worthy subjects to study the PET degradation in marine environments. This article is protected by copyright. All rights reserved.
Vibrio gazogenes cutinase PET6
