| Structural highlights
Function
PETH2_THEAE Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (By similarity). Can also depolymerize the synthetic polyesters poly(epsilon-caprolactone) (PCL), poly(butylene succinate-co-adipate) (PBSA), poly(butylene succinate) (PBS), and poly(lactic acid) (PLA) (PubMed:20393707, PubMed:22183084).[UniProtKB:D4Q9N1][1] [2] [3] [4]
References
- ↑ Hu X, Thumarat U, Zhang X, Tang M, Kawai F. Diversity of polyester-degrading bacteria in compost and molecular analysis of a thermoactive esterase from Thermobifida alba AHK119. Appl Microbiol Biotechnol. 2010 Jun;87(2):771-9. PMID:20393707 doi:10.1007/s00253-010-2555-x
- ↑ Thumarat U, Nakamura R, Kawabata T, Suzuki H, Kawai F. Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119. Appl Microbiol Biotechnol. 2012 Jul;95(2):419-30. PMID:22183084 doi:10.1007/s00253-011-3781-6
- ↑ Thumarat U, Kawabata T, Nakajima M, Nakajima H, Sugiyama A, Yazaki K, Tada T, Waku T, Tanaka N, Kawai F. Comparison of genetic structures and biochemical properties of tandem cutinase-type polyesterases from Thermobifida alba AHK119. J Biosci Bioeng. 2015 Nov;120(5):491-7. PMID:25910960 doi:10.1016/j.jbiosc.2015.03.006
- ↑ Zhang Z, Wang W, Li D, Xiao J, Wu L, Geng X, Wu G, Zeng Z, Hu J. Decolorization of molasses alcohol wastewater by thermophilic hydrolase with practical application value. Bioresour Technol. 2021 Mar;323:124609. PMID:33387709 doi:10.1016/j.biortech.2020.124609
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