Structural highlights
Function
PETH2_THECS Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263).[1] [2] [UniProtKB:A0A0K8P6T7]
References
- ↑ Herrero Acero E, Ribitsch D, Dellacher A, Zitzenbacher S, Marold A, Steinkellner G, Gruber K, Schwab H, Guebitz GM. Surface engineering of a cutinase from Thermobifida cellulosilytica for improved polyester hydrolysis. Biotechnol Bioeng. 2013 Oct;110(10):2581-90. doi: 10.1002/bit.24930. Epub 2013 , Apr 29. PMID:23592055 doi:http://dx.doi.org/10.1002/bit.24930
- ↑ Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Lyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Acero EH, Guebitz GM. Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica. Biotechnol Bioeng. 2017 Jul 3. doi: 10.1002/bit.26372. PMID:28671263 doi:http://dx.doi.org/10.1002/bit.26372
