| 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]
Publication Abstract from PubMed
Cutinases are enzymes known to degrade polyester-type plastics. Est119, a plastic-degrading type of cutinase from Thermobifida alba AHK119 (herein called Ta_cut), shows a broad substrate specificity toward polyesters, and can degrade substrates including polylactic acid (PLA). However, the PLA-degrading mechanism of cutinases is still poorly understood. Here, we report the structure complexes of cutinase with ethyl lactate (EL), the constitutional unit. From this complex structure, the electron density maps clearly showed one lactate (LAC) and one EL occupying different positions in the active site cleft. The binding mode of EL is assumed to show a figure prior to reaction and LAC is an after-reaction product. These complex structures demonstrate the role of active site residues in the esterase reaction and substrate recognition. The complex structures were compared with other documented complex structures of cutinases and with the structure of PETase from Ideonella sakaiensis. The amino acid residues involved in substrate interaction are highly conserved among these enzymes. Thus, mapping the precise interactions in the Ta_cut and EL complex will pave the way for understanding the plastic-degrading mechanism of cutinases and suggest ways of creating more potent enzymes by structural protein engineering. This article is protected by copyright. All rights reserved.
Structural insights into the unique polylactate-degrading mechanism of Thermobifida alba cutinase.,Kitadokoro K, Mizuki K, Matsui S, Osokoshi R, Uschara T, Kawai F, Kamitani S FEBS J. 2019 Feb 14. doi: 10.1111/febs.14781. PMID:30761732[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Kitadokoro K, Mizuki K, Matsui S, Osokoshi R, Uschara T, Kawai F, Kamitani S. Structural insights into the unique polylactate-degrading mechanism of Thermobifida alba cutinase. FEBS J. 2019 Feb 14. doi: 10.1111/febs.14781. PMID:30761732 doi:http://dx.doi.org/10.1111/febs.14781
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