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首页> 外文会议>NATO Advanced Research Workshop on The Chloroplast: From Molecular Biology to Biotechnology Kolymbari-Chania, Crete, Greece 10-15 August 1998 >Import and processing of e. coli expressed polyphenol oxidase by isolated chloroplasts
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Import and processing of e. coli expressed polyphenol oxidase by isolated chloroplasts

机译：进口加工e。大肠埃希菌通过分离的叶绿体表达多酚氧化酶

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摘要

Polyphenol oxidases (PPOs) are copper containing enzymes which catalyze the oxidation of o-dihydroxyphenols. The resulting, highly reactive, quinones undergo secondary reactions among themselves and covalently modify a variety of cellular constituents, including proteins. Since PPO is believed to take part in protecting plants against herbivores and pathogens 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. It appears that translocation of iPPO across thylakoids may proceed by both the triangle openpH- and Sec-dependent pathways (Koussevitzky, Ne'eman and Harel, unpublished observations).
机译：多酚氧化酶（PPO）是含铜的酶，可催化邻二羟基苯酚的氧化。所得的高反应性醌之间会发生二次反应，并共价修饰包括蛋白质在内的多种细胞成分。由于人们认为PPO参与了保护植物免受草食动物和病原体侵害的过程，因此酶被隔离在类囊体腔中，远离液泡中的底物也就不足为奇了。 PPO是上述最大的管腔蛋白，可分两步发送至其位置。 67 kDa前体（pPPO）通过基质肽酶（SPP）处理成为62 kDa中间体（iPPO）。后者穿过类囊体，并由类囊体加工肽酶（TPP）转化为59 kDa的成熟蛋白。看来iPPO跨类囊体的转运可能通过三角形开放pH依赖性和Sec依赖性途径进行（Koussevitzky，Ne'eman和Harel，未发表的观察结果）。

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