| Structural highlights
Function
TPDB1_COMSP Component of the terephthalate 1,2-dioxygenase multicomponent enzyme system which catalyzes the dioxygenation of terephthalate (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). It can also use 2,5-dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as substrates, and preferentially uses NADPH which is the physiological electron donor.[1] [2] [3]
Publication Abstract from PubMed
SignificanceMore than 400 million tons of plastic waste is produced each year, the overwhelming majority of which ends up in landfills. Bioconversion strategies aimed at plastics have emerged as important components of enabling a circular economy for synthetic plastics, especially those that exhibit chemically similar linkages to those found in nature, such as polyesters. The enzyme system described in this work is essential for mineralization of the xenobiotic components of poly(ethylene terephthalate) (PET) in the biosphere. Our description of its structure and substrate preferences lays the groundwork for in vivo or ex vivo engineering of this system for PET upcycling.
Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.,Kincannon WM, Zahn M, Clare R, Lusty Beech J, Romberg A, Larson J, Bothner B, Beckham GT, McGeehan JE, DuBois JL Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2121426119. doi: , 10.1073/pnas.2121426119. Epub 2022 Mar 21. PMID:35312352[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sasoh M, Masai E, Ishibashi S, Hara H, Kamimura N, Miyauchi K, Fukuda M. Characterization of the terephthalate degradation genes of Comamonas sp. strain E6. Appl Environ Microbiol. 2006 Mar;72(3):1825-32. PMID:16517628 doi:http://dx.doi.org/72/3/1825
- ↑ Fukuhara Y, Kasai D, Katayama Y, Fukuda M, Masai E. Enzymatic properties of terephthalate 1,2-dioxygenase of Comamonas sp. strain E6. Biosci Biotechnol Biochem. 2008 Sep;72(9):2335-41. doi: 10.1271/bbb.80236. Epub, 2008 Sep 7. PMID:18776687 doi:http://dx.doi.org/10.1271/bbb.80236
- ↑ Schlafli HR, Weiss MA, Leisinger T, Cook AM. Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component. J Bacteriol. 1994 Nov;176(21):6644-52. doi: 10.1128/jb.176.21.6644-6652.1994. PMID:7961417 doi:http://dx.doi.org/10.1128/jb.176.21.6644-6652.1994
- ↑ Kincannon WM, Zahn M, Clare R, Lusty Beech J, Romberg A, Larson J, Bothner B, Beckham GT, McGeehan JE, DuBois JL. Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism. Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2121426119. doi:, 10.1073/pnas.2121426119. Epub 2022 Mar 21. PMID:35312352 doi:http://dx.doi.org/10.1073/pnas.2121426119
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