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Title:
A novel type of lycopene ε-cyclase in the marine cyanobacterium Prochlorococcus marinus MED4 | Archives of Microbiology
Description:
Chlorophyll-b-possessing cyanobacteria of the genus Prochlorococcus share the presence of high amounts of α- and β-carotenoids with green algae and higher plants. The branch point in carotenoid biosynthesis is the cyclization of lycopene, for which in higher plants two distinct enzymes are required, ε- and β-lycopene cyclase. All cyanobacteria studied so far possess a single β-cyclase. Here, two different Prochlorococcus sp. MED4 genes were functionally identified by heterologous gene complementation in Escherichia coli to encode lycopene cyclases. Whereas one is both functionally and in sequence highly similar to the β-cyclase of Synechococcus sp. strain PCC 7942 and other cyanobacteria, the other showed several intriguing features. It acts as a bifunctional enzyme catalyzing the formation of ε- as well as of β-ionone end groups. Expression of this cyclase in E. coli resulted in the simultaneous accumulation of α- β-, δ-, and ε-carotene. Such an activity is in contrast to all lycopene ε-cyclases known so far, including those of the higher plants. Thus, for the first time among prokaryotes, two individual enzymes were identified in one organism that are responsible for the formation of cyclic carotenoids with either β- or ε-end groups. These two genes are suggested to be designated as crtL-b and crtL-e. The results indicate that both enzymes might have originated from duplication of a single gene. Consequently, we suggest that multiple gene duplications followed by functional diversification resulted several times, and in independent lineages, in the appearance of enzymes for the biosynthesis of cyclic carotenoids.
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google, scholar, article, cas, lycopene, pubmed, sandmann, prochlorococcus, biosynthesis, gene, hess, cyclase, carotenoids, content, carotenoid, enzymes, access, plant, privacy, cookies, βcyclase, biochem, analysis, data, publish, search, marine, cyanobacterium, med, steiger, wolfgang, cyanobacteria, plants, genes, sequence, formation, functional, chlorophyll, cell, res, mol, author, information, log, journal, research, type, εcyclase, marinus, april,

Topics {✒️}

gov/jgi_microbial/html/prochlorococcus/prochlo_pickastrain month download article/chapter lycopene ε-cyclase c30-bonded stationary phase positions-specific gap penalties β-lycopene cyclase lycopene β-cyclase β-ionone end groups low-light suboxic environments β-carotene content lycopene epsilon-cyclases lycopene ε-cyclases cyanobacterium synechocystis sp single β-cyclase carotene isomerase involved trans carotene isomerization ε-carotene ε-end groups related subjects full article pdf lycopene cyclases involved pigment composition α- β encode lycopene cyclases lycopene isomers synthesized privacy choices/manage cookies lycopene cyclase β-cyclase cold spring harbor ionone end groups marine photosynthetic prokaryote multiple gene duplications chlamydomonas reinhardtii prochlorococcus strains med4 ocean genome legacy carotenoid biosynthetic gene european economic area scope submit manuscript heterologous gene complementation bifunctional enzyme catalyzing check access variable chain length carotenogenic gene cluster prochlorophytes twenty years 16s rrna sequences variable regions v6 reconstructing tree topologies eu program margenes instant access genus prochlorococcus share

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Cunningham FX, Gantt E (2001) One ring or two?

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         description:Chlorophyll-b-possessing cyanobacteria of the genus Prochlorococcus share the presence of high amounts of α- and β-carotenoids with green algae and higher plants. The branch point in carotenoid biosynthesis is the cyclization of lycopene, for which in higher plants two distinct enzymes are required, ε- and β-lycopene cyclase. All cyanobacteria studied so far possess a single β-cyclase. Here, two different Prochlorococcus sp. MED4 genes were functionally identified by heterologous gene complementation in Escherichia coli to encode lycopene cyclases. Whereas one is both functionally and in sequence highly similar to the β-cyclase of Synechococcus sp. strain PCC 7942 and other cyanobacteria, the other showed several intriguing features. It acts as a bifunctional enzyme catalyzing the formation of ε- as well as of β-ionone end groups. Expression of this cyclase in E. coli resulted in the simultaneous accumulation of α- β-, δ-, and ε-carotene. Such an activity is in contrast to all lycopene ε-cyclases known so far, including those of the higher plants. Thus, for the first time among prokaryotes, two individual enzymes were identified in one organism that are responsible for the formation of cyclic carotenoids with either β- or ε-end groups. These two genes are suggested to be designated as crtL-b and crtL-e. The results indicate that both enzymes might have originated from duplication of a single gene. Consequently, we suggest that multiple gene duplications followed by functional diversification resulted several times, and in independent lineages, in the appearance of enzymes for the biosynthesis of cyclic carotenoids.
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      description:Chlorophyll-b-possessing cyanobacteria of the genus Prochlorococcus share the presence of high amounts of α- and β-carotenoids with green algae and higher plants. The branch point in carotenoid biosynthesis is the cyclization of lycopene, for which in higher plants two distinct enzymes are required, ε- and β-lycopene cyclase. All cyanobacteria studied so far possess a single β-cyclase. Here, two different Prochlorococcus sp. MED4 genes were functionally identified by heterologous gene complementation in Escherichia coli to encode lycopene cyclases. Whereas one is both functionally and in sequence highly similar to the β-cyclase of Synechococcus sp. strain PCC 7942 and other cyanobacteria, the other showed several intriguing features. It acts as a bifunctional enzyme catalyzing the formation of ε- as well as of β-ionone end groups. Expression of this cyclase in E. coli resulted in the simultaneous accumulation of α- β-, δ-, and ε-carotene. Such an activity is in contrast to all lycopene ε-cyclases known so far, including those of the higher plants. Thus, for the first time among prokaryotes, two individual enzymes were identified in one organism that are responsible for the formation of cyclic carotenoids with either β- or ε-end groups. These two genes are suggested to be designated as crtL-b and crtL-e. The results indicate that both enzymes might have originated from duplication of a single gene. Consequently, we suggest that multiple gene duplications followed by functional diversification resulted several times, and in independent lineages, in the appearance of enzymes for the biosynthesis of cyclic carotenoids.
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