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首页> 外文期刊>The FEBS journal >In vivo and in vitro studies on the carotenoid cleavage oxygenases from Sphingopyxis alaskensis RB2256 and Plesiocystis pacifica SIR-1 revealed their substrate specificities and non-retinal-forming cleavage activities
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In vivo and in vitro studies on the carotenoid cleavage oxygenases from Sphingopyxis alaskensis RB2256 and Plesiocystis pacifica SIR-1 revealed their substrate specificities and non-retinal-forming cleavage activities

机译：对来自阿拉斯加狮身人面兽RB2256和太平洋假单胞菌SIR-1的类胡萝卜素裂解加氧酶的体内和体外研究显示它们的底物特异性和非视网膜形成的裂解活性

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Carotenoid cleavage oxygenases are nonheme iron enzymes that speci?cally cleave carbon–carbon double bonds of carotenoids. Their apocarotenoid cleavage products serve as important signaling molecules that are involved in various biological processes. A database search revealed the presence of putative carotenoid cleavage oxygenase genes in the genomes of Sphingopyxis alaskensis RB2256 and Plesiocystis paci?ca SIR-1. The four genes sala_1698, sala_1008, ppsir1_15490 and ppsir1_17230 were cloned and heterologously expressed in carotenoid-producing Escherichia coli JM109 strains. Two of the four encoded proteins exhibited carotenoid cleavage activity. S. alaskensis RB2256 carotenoid cleavage oxygenase (SaCCO), which is encoded by sala_1698, was shown to cleave acyclic and monocyclic substrates. Coexpression of sala_1698 in carotenoid-producing E. coli JM109 strains revealed cleavage activity for lycopene, hydroxylycopene, and dihydroxylycopene. The monocyclic substrate apo-8′-carotenal was cleaved in vitro by puri?ed SaCCO at the 9′/10′ and 11′/12′ double bonds. The second enzyme, P. paci?ca SIR-1 carotenoid cleavage oxygenase (PpCCO), is encoded by ppsir1_15490. PpCCO-mediated carotenoid cleavage requires the presence of either hydroxy or keto groups. PpCCO cleaved zeaxanthin, hydroxylycopene, and dihydroxylycopene, and also the C50 carotenoids decaprenoxanthin, sarprenoxanthin and sarcinaxanthin, in carotenoid-producing E. coli JM109 strains. Whole cells of E. coli JM109 overexpressing ppsir1_15490mut, a mutant of ppsir1_15490 with enhanced gene expression, were applied for the conversion of carotenoids. Analysis of the carotenoid cleavage products revealed a single cleavage site at the 13′/14′ double bond for astaxanthin, and two cleavage sites at the 11′/12′ or 13′/14′ double bond for zeaxanthin, nostoxanthin, and canthaxanthin.
机译：类胡萝卜素裂解加氧酶是非血红素铁酶，可特异性裂解类胡萝卜素的碳-碳双键。他们的类胡萝卜素裂解产物是重要的信号分子，参与各种生物过程。通过数据库搜索发现，在阿拉斯哥天牛蛛RB2256和Plesiocystis paci？ca SIR-1的基因组中存在假定的类胡萝卜素裂解加氧酶基因。克隆了四个基因sala_1698，sala_1008，ppsir1_15490和ppsir1_17230，并在生产类胡萝卜素的大肠杆菌JM109菌株中异源表达。四个编码蛋白中的两个显示出类胡萝卜素裂解活性。由sala_1698编码的阿拉斯加沙门氏菌RB2256类胡萝卜素裂解加氧酶（SaCCO）被证明可裂解无环和单环底物。 sala_1698在生产类胡萝卜素的大肠杆菌JM109菌株中的共表达揭示了对番茄红素，羟基番茄红素和二羟基番茄红素的切割活性。通过纯化的SaCCO在9'/ 10'和11'/ 12'双键处体外裂解单环底物apo-8'-胡萝卜素。第二种酶是P. paci？ca SIR-1类胡萝卜素裂解加氧酶（PpCCO），由ppsir1_15490编码。 PpCCO介导的类胡萝卜素裂解需要羟基或酮基的存在。 PpCCO在产生类胡萝卜素的大肠杆菌JM109菌株中裂解了玉米黄质，羟基番茄红素和二羟基番茄红素，还裂解了C50类胡萝卜素去甲黄嘌呤，sarprenoxanthin和sarcinaxanthin。将过量表达ppsir1_15490mut（具有增强的基因表达的ppsir1_15490的突变体）的大肠杆菌JM109的全细胞用于类胡萝卜素的转化。对类胡萝卜素裂解产物的分析显示，虾青素在13'/ 14'双键处有一个裂解位点，而玉米黄质，诺泊黄质和角黄素在11'/ 12'或13'/ 14'双键处有两个裂解位点。

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