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We are analyzing https://link.springer.com/article/10.1007/bf00020174.

Title:
A novel carotenoid biosynthesis gene coding for ζ-carotene desaturase: functional expression, sequence and phylogenetic origin | Plant Molecular Biology
Description:
A DNA fragment which has been isolated previously from an Anabaena DNA expression library was subcloned. The corresponding protein was overexpressed in Escherichia coli. The recombinant enzyme was fully active in converting ζ-carotene into lycopene in vitro with neurosporene as an intermediate. A smaller fragment which still contained the active enzyme was sequenced. An open reading frame of 1497 bp was found coding for a protein consisting of 499 amino acids with the calculated molecular weight of 56 740. In a computer search of nucleotide sequences contained in the EMBL nucleotide sequence library, all the best-fitting comparisons were carotenoid desaturases. The highest similarity was found with the crtI phytoene desaturase genes of bacteria and the al-1 gene from Neurospora crassa. A much lower similarity was found with the pds genes coding for phytoene desaturase from cyanobacteria and higher plants. It is shown in protein similarity plots that the amino acid similarity of ζ-carotene desaturase to the latter is mainly limited to the N terminus of the polypeptides. In contrast, the protein similarity plots and a comparison of a conserved region clearly demonstrate that there is a strong relationship between ζ-carotene desaturase and the phytoene desaturases from various bacteria and fungi. Therefore we propose that the ζ-carotene desaturase gene is homologous to the crt I phytoene desaturase genes of bacteria and fungi.
Website Age:
28 years and 1 months (reg. 1997-05-29).

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  • Science
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Keywords {🔍}

google, scholar, desaturase, carotenoid, gene, phytoene, article, biosynthesis, molecular, ζcarotene, sequence, plant, sandmann, linden, misawa, genes, biology, coding, expression, dna, protein, coli, usa, biol, biochem, privacy, cookies, content, search, escherichia, similarity, access, nature, mol, proc, natl, acad, sci, carotenoids, analysis, publish, research, functional, anabaena, nucleotide, bacteria, products, pecker, chamovitz, hirschberg,

Topics {✒️}

month download article/chapter ζ-carotene desaturase gene phytoene desaturase genes pds genes coding single-stranded plasmid dna anabaena pcc 7120 norihiko misawa carotenoid biosynthesis pathway ζ-carotene desaturase open reading frame cold spring harbor carotenoid biosynthetic gene key technology converting ζ-carotene privacy choices/manage cookies full article pdf gene products expressed phytoene desaturase gene carotene patterns derives phytoene desaturase diversification check access instant access phytoene desaturase reaction calculated molecular weight carotenoid biosynthesis european economic area xanthophyllomyces dendrorhous leading related subjects mathews-roth mm nadp-binding sites single polypeptide catalyzing tomato fruit ripening chain-terminating inhibitors ribosome binding sites soybean cdna coding conditions privacy policy kluwer academic publishers ζ-carotene cyanobacterium anabaena 7120 accepting optional cookies amino acid similarity protein similarity plots nucleotide sequences contained main content log flavoprotein disulfide oxidoreductases article linden carotenoid pathway conserved enzymes mediate journal finder publish phylogenetic origin

Schema {🗺️}

WebPage:
      mainEntity:
         headline:A novel carotenoid biosynthesis gene coding for ζ-carotene desaturase: functional expression, sequence and phylogenetic origin
         description:A DNA fragment which has been isolated previously from an Anabaena DNA expression library was subcloned. The corresponding protein was overexpressed in Escherichia coli. The recombinant enzyme was fully active in converting ζ-carotene into lycopene in vitro with neurosporene as an intermediate. A smaller fragment which still contained the active enzyme was sequenced. An open reading frame of 1497 bp was found coding for a protein consisting of 499 amino acids with the calculated molecular weight of 56 740. In a computer search of nucleotide sequences contained in the EMBL nucleotide sequence library, all the best-fitting comparisons were carotenoid desaturases. The highest similarity was found with the crtI phytoene desaturase genes of bacteria and the al-1 gene from Neurospora crassa. A much lower similarity was found with the pds genes coding for phytoene desaturase from cyanobacteria and higher plants. It is shown in protein similarity plots that the amino acid similarity of ζ-carotene desaturase to the latter is mainly limited to the N terminus of the polypeptides. In contrast, the protein similarity plots and a comparison of a conserved region clearly demonstrate that there is a strong relationship between ζ-carotene desaturase and the phytoene desaturases from various bacteria and fungi. Therefore we propose that the ζ-carotene desaturase gene is homologous to the crt I phytoene desaturase genes of bacteria and fungi.
         datePublished:
         dateModified:
         pageStart:369
         pageEnd:379
         sameAs:https://doi.org/10.1007/BF00020174
         keywords:
             Anabaena PCC 7120
            carotenoid biosynthesis
            ζ-carotene desaturase
            Plant Sciences
            Biochemistry
            general
            Plant Pathology
         image:
         isPartOf:
            name:Plant Molecular Biology
            issn:
               1573-5028
               0167-4412
            volumeNumber:24
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Kluwer Academic Publishers
            logo:
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               type:ImageObject
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         author:
               name:Hartmut Linden
               affiliation:
                     name:Universität Konstanz
                     address:
                        name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
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                        name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Gerhard Sandmann
               affiliation:
                     name:Universität Konstanz
                     address:
                        name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
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      headline:A novel carotenoid biosynthesis gene coding for ζ-carotene desaturase: functional expression, sequence and phylogenetic origin
      description:A DNA fragment which has been isolated previously from an Anabaena DNA expression library was subcloned. The corresponding protein was overexpressed in Escherichia coli. The recombinant enzyme was fully active in converting ζ-carotene into lycopene in vitro with neurosporene as an intermediate. A smaller fragment which still contained the active enzyme was sequenced. An open reading frame of 1497 bp was found coding for a protein consisting of 499 amino acids with the calculated molecular weight of 56 740. In a computer search of nucleotide sequences contained in the EMBL nucleotide sequence library, all the best-fitting comparisons were carotenoid desaturases. The highest similarity was found with the crtI phytoene desaturase genes of bacteria and the al-1 gene from Neurospora crassa. A much lower similarity was found with the pds genes coding for phytoene desaturase from cyanobacteria and higher plants. It is shown in protein similarity plots that the amino acid similarity of ζ-carotene desaturase to the latter is mainly limited to the N terminus of the polypeptides. In contrast, the protein similarity plots and a comparison of a conserved region clearly demonstrate that there is a strong relationship between ζ-carotene desaturase and the phytoene desaturases from various bacteria and fungi. Therefore we propose that the ζ-carotene desaturase gene is homologous to the crt I phytoene desaturase genes of bacteria and fungi.
      datePublished:
      dateModified:
      pageStart:369
      pageEnd:379
      sameAs:https://doi.org/10.1007/BF00020174
      keywords:
          Anabaena PCC 7120
         carotenoid biosynthesis
         ζ-carotene desaturase
         Plant Sciences
         Biochemistry
         general
         Plant Pathology
      image:
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         name:Plant Molecular Biology
         issn:
            1573-5028
            0167-4412
         volumeNumber:24
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         name:Kluwer Academic Publishers
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            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
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      author:
            name:Hartmut Linden
            affiliation:
                  name:Universität Konstanz
                  address:
                     name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Norihiko Misawa
            affiliation:
                  name:Kirin Brewery Co., Ltd.
                  address:
                     name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Toshiko Saito
            affiliation:
                  name:Kirin Brewery Co., Ltd.
                  address:
                     name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
                     type:PostalAddress
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            type:Person
            name:Gerhard Sandmann
            affiliation:
                  name:Universität Konstanz
                  address:
                     name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
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         name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
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         name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
         type:PostalAddress
      name:Universität Konstanz
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         name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
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      name:Hartmut Linden
      affiliation:
            name:Universität Konstanz
            address:
               name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
               type:PostalAddress
            type:Organization
      name:Norihiko Misawa
      affiliation:
            name:Kirin Brewery Co., Ltd.
            address:
               name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
               type:PostalAddress
            type:Organization
      name:Toshiko Saito
      affiliation:
            name:Kirin Brewery Co., Ltd.
            address:
               name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
               type:PostalAddress
            type:Organization
      name:Gerhard Sandmann
      affiliation:
            name:Universität Konstanz
            address:
               name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
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      name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
      name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
      name:Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama-shi, Kanagawa, Japan
      name:Lehrstuhl Physiologie und Biochemie der Pflanzen, Universität Konstanz, Konstanz, Germany
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