7q05
Crystal structure of TPADO in complex with TPA
Structural highlights
FunctionTPDB1_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 PubMedSignificanceMore 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
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