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8YTU

Mipa-PETase from Micromonospora pattaloongensis

Summary for 8YTU
Entry DOI10.2210/pdb8ytu/pdb
Descriptorcutinase, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total)
Functional Keywordspet hydrolase, hydrolase
Biological sourceMicromonospora pattaloongensis
Total number of polymer chains3
Total formula weight84004.52
Authors
Hong, H.,Seo, H.,Park, J.,Kim, K.-J. (deposition date: 2024-03-26, release date: 2025-01-15)
Primary citationSeo, H.,Hong, H.,Park, J.,Lee, S.H.,Ki, D.,Ryu, A.,Sagong, H.Y.,Kim, K.J.
Landscape profiling of PET depolymerases using a natural sequence cluster framework.
Science, 387:eadp5637-eadp5637, 2025
Cited by
PubMed Abstract: Enzymes capable of breaking down polymers have been identified from natural sources and developed for industrial use in plastic recycling. However, there are many potential starting points for enzyme optimization that remain unexplored. We generated a landscape of 170 lineages of 1894 polyethylene terephthalate depolymerase (PETase) candidates and performed profiling using sampling approaches with features associated with PET-degrading capabilities. We identified three promising yet unexplored PETase lineages and two potent PETases, Mipa-P and Kubu-P. An engineered variant of Kubu-P outperformed benchmarks in terms of PET depolymerization in harsh environments, such as those with high substrate load and ethylene glycol as the solvent.
PubMed: 39745946
DOI: 10.1126/science.adp5637
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.34 Å)
Structure validation

237992

数据于2025-06-25公开中

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