Abstract
Polyphenol oxidases (PPOs) are copper containing enzymes which catalyze the oxidation of o-dihydroxyphenols [1]. The resulting, highly reactive, quinones undergo secondary reactions among themselves and covalently modify a variety of cellular constituents, including proteins [1]. Since PPO is believed to take part in protecting plants against herbivores and pathogens [1, 2] it is not surprising that the enzyme is sequestered in the thylakoid lumen, away from its substrates in the vacuole. PPO, the largest lumen protein described, is routed to its location in two steps. The 67 kDa precursor (pPPO) is processed by a stromal peptidase (SPP) to a 62 kDa intermediate (iPPO). The latter traverses the thylakoid and is converted by a thylakoid processing peptidase (TPP) to a 59 kDa mature protein [3, 4, 5]. It appears that translocation of iPPO across thylakoids may proceed by both the ΔpH- and Sec-dependent pathways (Koussevitzky, Ne’eman and Harel, unpublished observations).
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© 1999 Springer Science+Business Media Dordrecht
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Koussevitzky, S., Ne’eman, E., Harel, E. (1999). Import and Processing of E. Coli Expressed Polyphenol Oxidase by Isolated Chloroplasts. In: Argyroudi-Akoyunoglou, J.H., Senger, H. (eds) The Chloroplast: From Molecular Biology to Biotechnology. NATO Science Series, vol 64. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4788-0_24
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DOI: https://doi.org/10.1007/978-94-011-4788-0_24
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